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caption a7 anti slo1 antibodies  (Alomone Labs)


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    Structured Review

    Alomone Labs caption a7 anti slo1 antibodies
    Summary of <t> Slo1 </t> Antibodies
    Caption A7 Anti Slo1 Antibodies, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 119 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/caption+a7+anti+slo1+antibodies/Anti-KCNMA1+Antibody/pmc02605666-51-36-56
    Average 93 stars, based on 119 article reviews
    caption a7 anti slo1 antibodies - by Bioz Stars, 2026-09
    93/100 stars

    Images

    1) Product Images from "Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons"

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    Journal:

    doi: 10.1002/cne.20931

    Summary of  Slo1  Antibodies
    Figure Legend Snippet: Summary of Slo1 Antibodies

    Techniques Used:

    A, immunoblot analysis of brain membrane fractions from adult rats, and wild-type and Slo1-deficient mice. Proteins were fractionated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes and probed with mouse monoclonal (L6/60, 10 µg/ml) or rabbit polyclonal anti-Slo1 (Alomone, 1:500; Chemicon, 1:200), or mouse monoclonal anti-Kv2.1 (K89/41, TC supe 1:2) antibodies as noted. Numbers to left denote mobility of prestained molecular weight standards in kD.
    Figure Legend Snippet: A, immunoblot analysis of brain membrane fractions from adult rats, and wild-type and Slo1-deficient mice. Proteins were fractionated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes and probed with mouse monoclonal (L6/60, 10 µg/ml) or rabbit polyclonal anti-Slo1 (Alomone, 1:500; Chemicon, 1:200), or mouse monoclonal anti-Kv2.1 (K89/41, TC supe 1:2) antibodies as noted. Numbers to left denote mobility of prestained molecular weight standards in kD.

    Techniques Used: Western Blot, Membrane, SDS Page, Molecular Weight

    A: Immunoblot analysis of the effects of alkaline phosphatase (AP) digestion on adult rat brain Slo1. Adult rat brain membranes treated without (−) or with 0.1 U/ml AP (+) for 3 h at 37°C were separated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes, then probed with anti-Kv2.1 (K89/41 mouse mAb, TC supe 1:2), anti-Kv1.4 (K13/31 mouse mAb, TC supe 1:2), anti-GluR1 (rabbit polyclonal antibody, Upstate 1:1000), or anti-Slo1 (L6/60, 10 µg/ml) antibodies. Slo1 exhibited AP- shifts from Mr ≈ 135 to ≈ 128 kD (bands 1 and 2 indicated on the right). Brain Kv2.1 also shifted in Mr upon AP treatment, whereas Kv1.4 and GluR1 did not. B: Immunoblot analysis of developmental rat brain membrane samples. L6/60 (10 µg/ml) immunostaining at postnatal day 2 (P2) revealed at least three distinct bands as indicated in the left margin (1, 135 kD; 2, 131 kD; 3, 124 kD), which changed in their relative proportions during postnatal development. A=adult, C=adult sample incubated 3 h at 37°C without AP, AP=adult sample incubated 3 h at 37°C with AP. Numbers to left denote mobility of prestained molecular weight standards in kD.
    Figure Legend Snippet: A: Immunoblot analysis of the effects of alkaline phosphatase (AP) digestion on adult rat brain Slo1. Adult rat brain membranes treated without (−) or with 0.1 U/ml AP (+) for 3 h at 37°C were separated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes, then probed with anti-Kv2.1 (K89/41 mouse mAb, TC supe 1:2), anti-Kv1.4 (K13/31 mouse mAb, TC supe 1:2), anti-GluR1 (rabbit polyclonal antibody, Upstate 1:1000), or anti-Slo1 (L6/60, 10 µg/ml) antibodies. Slo1 exhibited AP- shifts from Mr ≈ 135 to ≈ 128 kD (bands 1 and 2 indicated on the right). Brain Kv2.1 also shifted in Mr upon AP treatment, whereas Kv1.4 and GluR1 did not. B: Immunoblot analysis of developmental rat brain membrane samples. L6/60 (10 µg/ml) immunostaining at postnatal day 2 (P2) revealed at least three distinct bands as indicated in the left margin (1, 135 kD; 2, 131 kD; 3, 124 kD), which changed in their relative proportions during postnatal development. A=adult, C=adult sample incubated 3 h at 37°C without AP, AP=adult sample incubated 3 h at 37°C with AP. Numbers to left denote mobility of prestained molecular weight standards in kD.

    Techniques Used: Western Blot, SDS Page, Membrane, Immunostaining, Incubation, Molecular Weight

    A–C: L6/60 staining in adult rat hippocampus A: overview of L6/60 (0.6 µg/ml) immunoperoxidase staining in hippocampus. B, C: higher magnification images of the staining shown in A. B: stratum lucidum of the CA3 region of the hippocampus. C: magnified view of mossy fiber axons. Arrows in A–C highlight anatomical landmarks that specify the regions magnified. D–E: double label immunofluorescence labeling of brain sections from wild-type (D, WT) and Slo1-deficient (E, KO) mice. Brain sections from these mice were stained with L6/60 (24 µg/ml) mAb in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the hilus of the dentate gyrus and CA3 stratum lucidum. Scale bars, A:, 500 µm; B, C: 100 µm; D: 50 µm.
    Figure Legend Snippet: A–C: L6/60 staining in adult rat hippocampus A: overview of L6/60 (0.6 µg/ml) immunoperoxidase staining in hippocampus. B, C: higher magnification images of the staining shown in A. B: stratum lucidum of the CA3 region of the hippocampus. C: magnified view of mossy fiber axons. Arrows in A–C highlight anatomical landmarks that specify the regions magnified. D–E: double label immunofluorescence labeling of brain sections from wild-type (D, WT) and Slo1-deficient (E, KO) mice. Brain sections from these mice were stained with L6/60 (24 µg/ml) mAb in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the hilus of the dentate gyrus and CA3 stratum lucidum. Scale bars, A:, 500 µm; B, C: 100 µm; D: 50 µm.

    Techniques Used: Staining, Immunoperoxidase Staining, Immunofluorescence, Labeling

    Magnified view of stratum lucidum of CA3 region of hippocampus. A–C: somata and apical dendrites of CA3 pyramidal neurons were negatively stained with L6/60 (A, 24 µg/ml) as well as with anti-Kv1.4 antibody (B, K13/31 mouse mAb, TC supe 1:2), which overlapped in mossy fibers (C). D–F: in contrast, somatodendritic Kv2.1 (D, KC rabbit polyclonal antibody, 1:100) staining interdigitated with L6/60 staining (E), indicating the presence of Slo1 on synaptic terminals on the Kv2.1-positive apical dendrites of CA3 pyramidal neurons (F, overlay). Scale bars, 10 µm.
    Figure Legend Snippet: Magnified view of stratum lucidum of CA3 region of hippocampus. A–C: somata and apical dendrites of CA3 pyramidal neurons were negatively stained with L6/60 (A, 24 µg/ml) as well as with anti-Kv1.4 antibody (B, K13/31 mouse mAb, TC supe 1:2), which overlapped in mossy fibers (C). D–F: in contrast, somatodendritic Kv2.1 (D, KC rabbit polyclonal antibody, 1:100) staining interdigitated with L6/60 staining (E), indicating the presence of Slo1 on synaptic terminals on the Kv2.1-positive apical dendrites of CA3 pyramidal neurons (F, overlay). Scale bars, 10 µm.

    Techniques Used: Staining

    These photomicrographs show the pattern of immunoreactivity for the indicated subunits in the unoperated, control hemisphere (A–E) and operated hemisphere (F–J) of an animal that sustained a circumscribed unilateral ibotenic acid lesion. This lesion destroyed cells in the distal CA1 subfield, prosubiculum and subiculum, and also destroyed a central portion of the dentate gyrus. The entire CA3 and proximal CA1 subfield was spared by this lesion. This lesion greatly reduced the density of Slo1 (A, F; L6/60 TC supe 1:10), and Kv1.4 (B, G; K13/31 TC supe 1:10) in stratum lucidum of CA3, but did not affect binding of secondary antibody alone (C, H), nor staining for Slo1 (D, I; L6/60 TC supe 1:10), and Kv1.4 (E, J; K13/31 TC supe 1:10) in the terminal fields of striatal effernts to globus pallidus.
    Figure Legend Snippet: These photomicrographs show the pattern of immunoreactivity for the indicated subunits in the unoperated, control hemisphere (A–E) and operated hemisphere (F–J) of an animal that sustained a circumscribed unilateral ibotenic acid lesion. This lesion destroyed cells in the distal CA1 subfield, prosubiculum and subiculum, and also destroyed a central portion of the dentate gyrus. The entire CA3 and proximal CA1 subfield was spared by this lesion. This lesion greatly reduced the density of Slo1 (A, F; L6/60 TC supe 1:10), and Kv1.4 (B, G; K13/31 TC supe 1:10) in stratum lucidum of CA3, but did not affect binding of secondary antibody alone (C, H), nor staining for Slo1 (D, I; L6/60 TC supe 1:10), and Kv1.4 (E, J; K13/31 TC supe 1:10) in the terminal fields of striatal effernts to globus pallidus.

    Techniques Used: Control, Binding Assay, Staining

    A: low magnification view of L6/60 (0.6 µg/ml) immunoperoxidase staining near the primary fissure. Note moderate to high levels of staining in the molecular layer relative to the granule cell layer, and intense staining at/near the Purkinje cell layer. B: higher magnification view of the area boxed in A, showing intense L6/60 staining in the Purkinje cell layer. The arrowheads point to a Purkinje cell soma, while the arrow points to a basket cell pinceau terminal onto a Purkinje cell initial segment. C–D: Double label immunofluorescence staining of brain sections from wild-type (C: WT) and Slo1-deficient (D: KO) mice. Brain sections from these mice were stained with L6/60 mAb (24 µg/ml) in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the Purkinje cell layer and reveal that staining in Purkinje cell somata, basket cell terminals, and the molecular layer is eliminated in the Slo1 knockout. Scale bars, A:, 100 µm; B, C: 500 µm; D: 10 µm.
    Figure Legend Snippet: A: low magnification view of L6/60 (0.6 µg/ml) immunoperoxidase staining near the primary fissure. Note moderate to high levels of staining in the molecular layer relative to the granule cell layer, and intense staining at/near the Purkinje cell layer. B: higher magnification view of the area boxed in A, showing intense L6/60 staining in the Purkinje cell layer. The arrowheads point to a Purkinje cell soma, while the arrow points to a basket cell pinceau terminal onto a Purkinje cell initial segment. C–D: Double label immunofluorescence staining of brain sections from wild-type (C: WT) and Slo1-deficient (D: KO) mice. Brain sections from these mice were stained with L6/60 mAb (24 µg/ml) in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the Purkinje cell layer and reveal that staining in Purkinje cell somata, basket cell terminals, and the molecular layer is eliminated in the Slo1 knockout. Scale bars, A:, 100 µm; B, C: 500 µm; D: 10 µm.

    Techniques Used: Immunoperoxidase Staining, Staining, Immunofluorescence, Knock-Out

    Confocal images of double label immunofluorescence staining. A–C: Slo1 and Kv1.2 localization in basket cell terminals. L6/60 (A: 24 µg/ml) staining overlaps with that for Kv1.2 (B: K14/16 mouse mAb, 16 µg/ml) in basket cell terminals (C: overlay); D–F: L6/60 (D: 24 µg/ml) staining encircles axon initial segments of Purkinje cells, stained with anti-NF-155/186 antibody (E: L11A/41 mouse mAb, TC supe 1:2; F: overlay). G–H: dendrites of multiple Purkinje cells, filled with anti-calbindin (H: Sigma mouse monoclonal, 16 µg/ml) staining, were associated with membrane-associated L6/60 staining (G: 24 µg/ml; I: overlay). J–L: localization of Slo1 in Purkinje cell somata. Slo1 staining (J: L6/60; 24 µg/ml) on the somata of Purkinje cells partially overlapped with Kv2.1 (K: KC rabbit polyclonal antibody, 1:100) surface clusters (L: overlay). Scale bars, 10 µm.
    Figure Legend Snippet: Confocal images of double label immunofluorescence staining. A–C: Slo1 and Kv1.2 localization in basket cell terminals. L6/60 (A: 24 µg/ml) staining overlaps with that for Kv1.2 (B: K14/16 mouse mAb, 16 µg/ml) in basket cell terminals (C: overlay); D–F: L6/60 (D: 24 µg/ml) staining encircles axon initial segments of Purkinje cells, stained with anti-NF-155/186 antibody (E: L11A/41 mouse mAb, TC supe 1:2; F: overlay). G–H: dendrites of multiple Purkinje cells, filled with anti-calbindin (H: Sigma mouse monoclonal, 16 µg/ml) staining, were associated with membrane-associated L6/60 staining (G: 24 µg/ml; I: overlay). J–L: localization of Slo1 in Purkinje cell somata. Slo1 staining (J: L6/60; 24 µg/ml) on the somata of Purkinje cells partially overlapped with Kv2.1 (K: KC rabbit polyclonal antibody, 1:100) surface clusters (L: overlay). Scale bars, 10 µm.

    Techniques Used: Immunofluorescence, Staining, Membrane

    A–C: Localization of endogenous Slo1. Neurons at 24 DIV were fixed, permeabilized with 0.1% Triton X-100 and stained with anti-Slo1 antibody L6/60 (A: 24 µg/ml; green) to detect the total pool of endogenous rSlo1, and anti-MAP2 (B: Sigma mouse mAb, 1:1000; C: overlay). D–F: Localization of surface hSlo1. Neurons at 11 DIV were fixed, stained with anti-Myc antibody (E: mouse monoclonal 1-9E10, 1 µg/ml) for cell surface hSlo1 (green), and then permeabilized with 0.1% Triton X-100 for L6/60 (D: 5 µg/ml) staining (red) to detect the total pool of exogenous hSlo1 and endogenous rSlo1 (F: overlay). Arrow points to a presumably untransfected neuron in the culture. Panel D inset: hSlo in both axons and dendrites was detected on a longer exposure. G: Surface Myc-positive (mouse mAb 19E10, 1 µg/ml) processes overlap with axonal tau (Sigma mouse monoclonal antibody 1:2000) staining. H–J: Surface Myc-positive (H: mouse mAb 19E10, 1 µg/ml) processes do not overlap with dendritic MAP-2 (I: Sigma mouse mAb, 1:1000) staining (J: overlay). Scale bars, A–F:, 20 µm; D inset: 50 µm ; G: 10 µm; H–J: 10 µm.
    Figure Legend Snippet: A–C: Localization of endogenous Slo1. Neurons at 24 DIV were fixed, permeabilized with 0.1% Triton X-100 and stained with anti-Slo1 antibody L6/60 (A: 24 µg/ml; green) to detect the total pool of endogenous rSlo1, and anti-MAP2 (B: Sigma mouse mAb, 1:1000; C: overlay). D–F: Localization of surface hSlo1. Neurons at 11 DIV were fixed, stained with anti-Myc antibody (E: mouse monoclonal 1-9E10, 1 µg/ml) for cell surface hSlo1 (green), and then permeabilized with 0.1% Triton X-100 for L6/60 (D: 5 µg/ml) staining (red) to detect the total pool of exogenous hSlo1 and endogenous rSlo1 (F: overlay). Arrow points to a presumably untransfected neuron in the culture. Panel D inset: hSlo in both axons and dendrites was detected on a longer exposure. G: Surface Myc-positive (mouse mAb 19E10, 1 µg/ml) processes overlap with axonal tau (Sigma mouse monoclonal antibody 1:2000) staining. H–J: Surface Myc-positive (H: mouse mAb 19E10, 1 µg/ml) processes do not overlap with dendritic MAP-2 (I: Sigma mouse mAb, 1:1000) staining (J: overlay). Scale bars, A–F:, 20 µm; D inset: 50 µm ; G: 10 µm; H–J: 10 µm.

    Techniques Used: Staining

    Related Articles

    Western Blot:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Membrane:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    SDS Page:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Molecular Weight:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Immunostaining:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Incubation:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Staining:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Immunoperoxidase Staining:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Immunofluorescence:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Labeling:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Control:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Binding Assay:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..

    Knock-Out:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons
    Article Snippet: Here we provide detailed analyses of Slo1 localization in rat and mouse brain by using a specific mAb generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice.generated against Slo1, whose specificity has been validated by a number of assays including a lack of detectable immunoreactivity against samples from Slo1 knockout mice. ... We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .. Affinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal Synthetic peptide 913–926 Sausbier et al., 2004 rabbit polyclonal GST Fusion protein 674–1115 Open in a separate window Amino acid positions correspond to original mSlo sequence of Butler et al., 1993 (NCBI accession number {"type":"entrez-protein","attrs":{"text":"AAA39746","term_id":"347144","term_text":"AAA39746"}} AAA39746 Summary of Slo1 AntibodiesAffinity Bioreagents PA1-923 rabbit polyclonal Synthetic peptide 913–926 Knaus et al., 1996 ; Hu et al., 2001 , Grunnet & Kaufman , 2004 rabbit polyclonal..



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    Summary of  Slo1  Antibodies

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: Summary of Slo1 Antibodies

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques:

    A, immunoblot analysis of brain membrane fractions from adult rats, and wild-type and Slo1-deficient mice. Proteins were fractionated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes and probed with mouse monoclonal (L6/60, 10 µg/ml) or rabbit polyclonal anti-Slo1 (Alomone, 1:500; Chemicon, 1:200), or mouse monoclonal anti-Kv2.1 (K89/41, TC supe 1:2) antibodies as noted. Numbers to left denote mobility of prestained molecular weight standards in kD.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: A, immunoblot analysis of brain membrane fractions from adult rats, and wild-type and Slo1-deficient mice. Proteins were fractionated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes and probed with mouse monoclonal (L6/60, 10 µg/ml) or rabbit polyclonal anti-Slo1 (Alomone, 1:500; Chemicon, 1:200), or mouse monoclonal anti-Kv2.1 (K89/41, TC supe 1:2) antibodies as noted. Numbers to left denote mobility of prestained molecular weight standards in kD.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Western Blot, Membrane, SDS Page, Molecular Weight

    A: Immunoblot analysis of the effects of alkaline phosphatase (AP) digestion on adult rat brain Slo1. Adult rat brain membranes treated without (−) or with 0.1 U/ml AP (+) for 3 h at 37°C were separated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes, then probed with anti-Kv2.1 (K89/41 mouse mAb, TC supe 1:2), anti-Kv1.4 (K13/31 mouse mAb, TC supe 1:2), anti-GluR1 (rabbit polyclonal antibody, Upstate 1:1000), or anti-Slo1 (L6/60, 10 µg/ml) antibodies. Slo1 exhibited AP- shifts from Mr ≈ 135 to ≈ 128 kD (bands 1 and 2 indicated on the right). Brain Kv2.1 also shifted in Mr upon AP treatment, whereas Kv1.4 and GluR1 did not. B: Immunoblot analysis of developmental rat brain membrane samples. L6/60 (10 µg/ml) immunostaining at postnatal day 2 (P2) revealed at least three distinct bands as indicated in the left margin (1, 135 kD; 2, 131 kD; 3, 124 kD), which changed in their relative proportions during postnatal development. A=adult, C=adult sample incubated 3 h at 37°C without AP, AP=adult sample incubated 3 h at 37°C with AP. Numbers to left denote mobility of prestained molecular weight standards in kD.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: A: Immunoblot analysis of the effects of alkaline phosphatase (AP) digestion on adult rat brain Slo1. Adult rat brain membranes treated without (−) or with 0.1 U/ml AP (+) for 3 h at 37°C were separated on 7.5% SDS-PAGE and transferred to nitrocellulose membranes, then probed with anti-Kv2.1 (K89/41 mouse mAb, TC supe 1:2), anti-Kv1.4 (K13/31 mouse mAb, TC supe 1:2), anti-GluR1 (rabbit polyclonal antibody, Upstate 1:1000), or anti-Slo1 (L6/60, 10 µg/ml) antibodies. Slo1 exhibited AP- shifts from Mr ≈ 135 to ≈ 128 kD (bands 1 and 2 indicated on the right). Brain Kv2.1 also shifted in Mr upon AP treatment, whereas Kv1.4 and GluR1 did not. B: Immunoblot analysis of developmental rat brain membrane samples. L6/60 (10 µg/ml) immunostaining at postnatal day 2 (P2) revealed at least three distinct bands as indicated in the left margin (1, 135 kD; 2, 131 kD; 3, 124 kD), which changed in their relative proportions during postnatal development. A=adult, C=adult sample incubated 3 h at 37°C without AP, AP=adult sample incubated 3 h at 37°C with AP. Numbers to left denote mobility of prestained molecular weight standards in kD.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Western Blot, SDS Page, Membrane, Immunostaining, Incubation, Molecular Weight

    A–C: L6/60 staining in adult rat hippocampus A: overview of L6/60 (0.6 µg/ml) immunoperoxidase staining in hippocampus. B, C: higher magnification images of the staining shown in A. B: stratum lucidum of the CA3 region of the hippocampus. C: magnified view of mossy fiber axons. Arrows in A–C highlight anatomical landmarks that specify the regions magnified. D–E: double label immunofluorescence labeling of brain sections from wild-type (D, WT) and Slo1-deficient (E, KO) mice. Brain sections from these mice were stained with L6/60 (24 µg/ml) mAb in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the hilus of the dentate gyrus and CA3 stratum lucidum. Scale bars, A:, 500 µm; B, C: 100 µm; D: 50 µm.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: A–C: L6/60 staining in adult rat hippocampus A: overview of L6/60 (0.6 µg/ml) immunoperoxidase staining in hippocampus. B, C: higher magnification images of the staining shown in A. B: stratum lucidum of the CA3 region of the hippocampus. C: magnified view of mossy fiber axons. Arrows in A–C highlight anatomical landmarks that specify the regions magnified. D–E: double label immunofluorescence labeling of brain sections from wild-type (D, WT) and Slo1-deficient (E, KO) mice. Brain sections from these mice were stained with L6/60 (24 µg/ml) mAb in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the hilus of the dentate gyrus and CA3 stratum lucidum. Scale bars, A:, 500 µm; B, C: 100 µm; D: 50 µm.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Staining, Immunoperoxidase Staining, Immunofluorescence, Labeling

    Magnified view of stratum lucidum of CA3 region of hippocampus. A–C: somata and apical dendrites of CA3 pyramidal neurons were negatively stained with L6/60 (A, 24 µg/ml) as well as with anti-Kv1.4 antibody (B, K13/31 mouse mAb, TC supe 1:2), which overlapped in mossy fibers (C). D–F: in contrast, somatodendritic Kv2.1 (D, KC rabbit polyclonal antibody, 1:100) staining interdigitated with L6/60 staining (E), indicating the presence of Slo1 on synaptic terminals on the Kv2.1-positive apical dendrites of CA3 pyramidal neurons (F, overlay). Scale bars, 10 µm.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: Magnified view of stratum lucidum of CA3 region of hippocampus. A–C: somata and apical dendrites of CA3 pyramidal neurons were negatively stained with L6/60 (A, 24 µg/ml) as well as with anti-Kv1.4 antibody (B, K13/31 mouse mAb, TC supe 1:2), which overlapped in mossy fibers (C). D–F: in contrast, somatodendritic Kv2.1 (D, KC rabbit polyclonal antibody, 1:100) staining interdigitated with L6/60 staining (E), indicating the presence of Slo1 on synaptic terminals on the Kv2.1-positive apical dendrites of CA3 pyramidal neurons (F, overlay). Scale bars, 10 µm.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Staining

    These photomicrographs show the pattern of immunoreactivity for the indicated subunits in the unoperated, control hemisphere (A–E) and operated hemisphere (F–J) of an animal that sustained a circumscribed unilateral ibotenic acid lesion. This lesion destroyed cells in the distal CA1 subfield, prosubiculum and subiculum, and also destroyed a central portion of the dentate gyrus. The entire CA3 and proximal CA1 subfield was spared by this lesion. This lesion greatly reduced the density of Slo1 (A, F; L6/60 TC supe 1:10), and Kv1.4 (B, G; K13/31 TC supe 1:10) in stratum lucidum of CA3, but did not affect binding of secondary antibody alone (C, H), nor staining for Slo1 (D, I; L6/60 TC supe 1:10), and Kv1.4 (E, J; K13/31 TC supe 1:10) in the terminal fields of striatal effernts to globus pallidus.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: These photomicrographs show the pattern of immunoreactivity for the indicated subunits in the unoperated, control hemisphere (A–E) and operated hemisphere (F–J) of an animal that sustained a circumscribed unilateral ibotenic acid lesion. This lesion destroyed cells in the distal CA1 subfield, prosubiculum and subiculum, and also destroyed a central portion of the dentate gyrus. The entire CA3 and proximal CA1 subfield was spared by this lesion. This lesion greatly reduced the density of Slo1 (A, F; L6/60 TC supe 1:10), and Kv1.4 (B, G; K13/31 TC supe 1:10) in stratum lucidum of CA3, but did not affect binding of secondary antibody alone (C, H), nor staining for Slo1 (D, I; L6/60 TC supe 1:10), and Kv1.4 (E, J; K13/31 TC supe 1:10) in the terminal fields of striatal effernts to globus pallidus.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Control, Binding Assay, Staining

    A: low magnification view of L6/60 (0.6 µg/ml) immunoperoxidase staining near the primary fissure. Note moderate to high levels of staining in the molecular layer relative to the granule cell layer, and intense staining at/near the Purkinje cell layer. B: higher magnification view of the area boxed in A, showing intense L6/60 staining in the Purkinje cell layer. The arrowheads point to a Purkinje cell soma, while the arrow points to a basket cell pinceau terminal onto a Purkinje cell initial segment. C–D: Double label immunofluorescence staining of brain sections from wild-type (C: WT) and Slo1-deficient (D: KO) mice. Brain sections from these mice were stained with L6/60 mAb (24 µg/ml) in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the Purkinje cell layer and reveal that staining in Purkinje cell somata, basket cell terminals, and the molecular layer is eliminated in the Slo1 knockout. Scale bars, A:, 100 µm; B, C: 500 µm; D: 10 µm.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: A: low magnification view of L6/60 (0.6 µg/ml) immunoperoxidase staining near the primary fissure. Note moderate to high levels of staining in the molecular layer relative to the granule cell layer, and intense staining at/near the Purkinje cell layer. B: higher magnification view of the area boxed in A, showing intense L6/60 staining in the Purkinje cell layer. The arrowheads point to a Purkinje cell soma, while the arrow points to a basket cell pinceau terminal onto a Purkinje cell initial segment. C–D: Double label immunofluorescence staining of brain sections from wild-type (C: WT) and Slo1-deficient (D: KO) mice. Brain sections from these mice were stained with L6/60 mAb (24 µg/ml) in red, and anti-Kv2.1 (KC rabbit polyclonal, 1:100) antibody in green. Images were taken from the Purkinje cell layer and reveal that staining in Purkinje cell somata, basket cell terminals, and the molecular layer is eliminated in the Slo1 knockout. Scale bars, A:, 100 µm; B, C: 500 µm; D: 10 µm.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Immunoperoxidase Staining, Staining, Immunofluorescence, Knock-Out

    Confocal images of double label immunofluorescence staining. A–C: Slo1 and Kv1.2 localization in basket cell terminals. L6/60 (A: 24 µg/ml) staining overlaps with that for Kv1.2 (B: K14/16 mouse mAb, 16 µg/ml) in basket cell terminals (C: overlay); D–F: L6/60 (D: 24 µg/ml) staining encircles axon initial segments of Purkinje cells, stained with anti-NF-155/186 antibody (E: L11A/41 mouse mAb, TC supe 1:2; F: overlay). G–H: dendrites of multiple Purkinje cells, filled with anti-calbindin (H: Sigma mouse monoclonal, 16 µg/ml) staining, were associated with membrane-associated L6/60 staining (G: 24 µg/ml; I: overlay). J–L: localization of Slo1 in Purkinje cell somata. Slo1 staining (J: L6/60; 24 µg/ml) on the somata of Purkinje cells partially overlapped with Kv2.1 (K: KC rabbit polyclonal antibody, 1:100) surface clusters (L: overlay). Scale bars, 10 µm.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: Confocal images of double label immunofluorescence staining. A–C: Slo1 and Kv1.2 localization in basket cell terminals. L6/60 (A: 24 µg/ml) staining overlaps with that for Kv1.2 (B: K14/16 mouse mAb, 16 µg/ml) in basket cell terminals (C: overlay); D–F: L6/60 (D: 24 µg/ml) staining encircles axon initial segments of Purkinje cells, stained with anti-NF-155/186 antibody (E: L11A/41 mouse mAb, TC supe 1:2; F: overlay). G–H: dendrites of multiple Purkinje cells, filled with anti-calbindin (H: Sigma mouse monoclonal, 16 µg/ml) staining, were associated with membrane-associated L6/60 staining (G: 24 µg/ml; I: overlay). J–L: localization of Slo1 in Purkinje cell somata. Slo1 staining (J: L6/60; 24 µg/ml) on the somata of Purkinje cells partially overlapped with Kv2.1 (K: KC rabbit polyclonal antibody, 1:100) surface clusters (L: overlay). Scale bars, 10 µm.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Immunofluorescence, Staining, Membrane

    A–C: Localization of endogenous Slo1. Neurons at 24 DIV were fixed, permeabilized with 0.1% Triton X-100 and stained with anti-Slo1 antibody L6/60 (A: 24 µg/ml; green) to detect the total pool of endogenous rSlo1, and anti-MAP2 (B: Sigma mouse mAb, 1:1000; C: overlay). D–F: Localization of surface hSlo1. Neurons at 11 DIV were fixed, stained with anti-Myc antibody (E: mouse monoclonal 1-9E10, 1 µg/ml) for cell surface hSlo1 (green), and then permeabilized with 0.1% Triton X-100 for L6/60 (D: 5 µg/ml) staining (red) to detect the total pool of exogenous hSlo1 and endogenous rSlo1 (F: overlay). Arrow points to a presumably untransfected neuron in the culture. Panel D inset: hSlo in both axons and dendrites was detected on a longer exposure. G: Surface Myc-positive (mouse mAb 19E10, 1 µg/ml) processes overlap with axonal tau (Sigma mouse monoclonal antibody 1:2000) staining. H–J: Surface Myc-positive (H: mouse mAb 19E10, 1 µg/ml) processes do not overlap with dendritic MAP-2 (I: Sigma mouse mAb, 1:1000) staining (J: overlay). Scale bars, A–F:, 20 µm; D inset: 50 µm ; G: 10 µm; H–J: 10 µm.

    Journal:

    Article Title: Immunolocalization of the Ca 2+ -Activated K + Channel Slo1 in Axons and Nerve Terminals of Mammalian Brain and Cultured Neurons

    doi: 10.1002/cne.20931

    Figure Lengend Snippet: A–C: Localization of endogenous Slo1. Neurons at 24 DIV were fixed, permeabilized with 0.1% Triton X-100 and stained with anti-Slo1 antibody L6/60 (A: 24 µg/ml; green) to detect the total pool of endogenous rSlo1, and anti-MAP2 (B: Sigma mouse mAb, 1:1000; C: overlay). D–F: Localization of surface hSlo1. Neurons at 11 DIV were fixed, stained with anti-Myc antibody (E: mouse monoclonal 1-9E10, 1 µg/ml) for cell surface hSlo1 (green), and then permeabilized with 0.1% Triton X-100 for L6/60 (D: 5 µg/ml) staining (red) to detect the total pool of exogenous hSlo1 and endogenous rSlo1 (F: overlay). Arrow points to a presumably untransfected neuron in the culture. Panel D inset: hSlo in both axons and dendrites was detected on a longer exposure. G: Surface Myc-positive (mouse mAb 19E10, 1 µg/ml) processes overlap with axonal tau (Sigma mouse monoclonal antibody 1:2000) staining. H–J: Surface Myc-positive (H: mouse mAb 19E10, 1 µg/ml) processes do not overlap with dendritic MAP-2 (I: Sigma mouse mAb, 1:1000) staining (J: overlay). Scale bars, A–F:, 20 µm; D inset: 50 µm ; G: 10 µm; H–J: 10 µm.

    Article Snippet: We also characterize the localization of exogenously expressed Slo1 α subunits in hippocampal neurons developing in culture that exhibit a prominent localization of Slo1 in axons and presynaptic terminals. table ft1 table-wrap mode="anchored" t5 Table 1 caption a7 Anti-slo1 antibodies used in this study L6/60 mouse monoclonal IgG2a GST Fusion protein 690–1196 Mapped to within 690–891 Alomone APC-021, lot AN-04 Rabbit polyclonal GST Fusion protein 1098–1196 Chemicon AB5228, lot 22040170 Rabbit polyclonal GST Fusion protein 1098–1196 Anti-slo1 antibodies used in other studies Martin et al., 2004 .

    Techniques: Staining