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human brain protein extract  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology human brain protein extract
    Human Brain Protein Extract, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+brain+protein+extract/pm31991880-149-16-20?v=Santa+Cruz+Biotechnology
    Average 91 stars, based on 7 article reviews
    human brain protein extract - by Bioz Stars, 2026-07
    91/100 stars

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    L-PGC-1α is recruited to PCK1 promoter and physically interacts with HNF4α. A, chromatin from HEK293 cells transfected with Halo-tagged expression plasmids as indicated was captured using HaloTag resin and analyzed by PCR amplifying a fragment spanning the predicted HNF4α binding site in the human PCK1 promoter. B, nuclear extracts from HEK293 cells transfected with Halo-tagged expression plasmids as indicated were subjected to pulldown with HaloTag resin followed by <t>immunoblotting</t> with a monoclonal HNF4α antibody. Histone-3 (H3) antibody was used as a loading control for nuclear extracts. WB, Western blot; neg., negative; IP, immunoprecipitation.
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    Expression of neuronal adaptor <t>protein</t> (AP)-3 mRNA and protein in INS-1 β-cells and pancreatic islet <t>extracts.</t> A: PCR analysis was performed to determine whether the neuronal AP-3 subunits β3B and μ3B are expressed in human islets (Isl). Human brain (Br) cDNA was used as a positive control. PCR products of the expected size were detected in brain and islets for both β3B and μ3B. A negative control (−) in which no reverse transcriptase was added during the reverse transcription reaction (no RT control) is shown to the right of the brain and islet lanes. cDNA from human tissues (shown) and from <t>rat</t> tissues (not shown) yielded identical results. B: to determine whether β3B protein is expressed in islets, Western blot analysis was performed using a β3B-specific monoclonal antibody. As expected, β3B was detected in human (H), rat (R), and mouse (M) Br. β3B protein was also present in cell lysates from the insulin-secreting β-cell lines β-TC3 (β), HIT-T15 (Hit), and INS-1 (Ins) and in tissue lysates from human and rat Isl. β3B was not detected in human <t>liver</t> or in brain from β3B-knockout mice (Ref. 43 and data not shown). As observed previously, immunoblot detection of β3B yielded 2 bands (Mr of ∼140 K). C, left, lanes 1 and 2: μ3B was detected in INS-1 cell lysate (Ins) but not in rat liver lysate (Liv). C, right: μ3B produced by in vitro transcription and translation (lane 4) and analyzed by immunoblotting with the μ3B antibody ran at the expected Mr of ∼47,000. This band comigrated precisely with the band that was observed in INS-1 cells (lane 3). 35S-met was included in the in vitro translation reaction. Autoradiographic detection of the radiolabeled μ3B (lane 4) yielded a band that precisely aligned with the band detected by immunoblot analysis. This confirms that the μ3B antibody detected μ3B synthesized de novo in the in vitro transcription and translation reaction.
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    SLITRK1 protein expression in fetal and adult rhesus monkey and human brain. Immunolocalization of SLITRK1 with DAB staining. A,D,G,J: In monkey, as in human, SLITRK1 is expressed in prospective and mature cortical layers 3, 5, and 6 in both fetal (A,G) and adult (D,J) stages. B,H: SLITRK1 is expressed in cortical apical dendrites in fetal monkey and human brain. E,K: In adult monkey and human brain, SLITRK1 localization shifts toward the cell body of cortical pyramidal neurons. C,I: In fetal monkey and human striatum, SLITRK1 is highly expressed in striosomes. F,L: In adult monkey and human striatum, expression is significantly diminished, with no real presence in striosomes. CP, cortical plate; MZ, marginal zone; SP, subplate; 3, 5, 6, cortical layers 3, 5, and 6. Scale bars = 1 mm in A,C,D,F,G,I,J,L; 100 µm in B,E,H,K.

    Journal: The Journal of Comparative Neurology

    Article Title: Developmentally Regulated and Evolutionarily Conserved Expression of SLITRK1 in Brain Circuits Implicated in Tourette Syndrome

    doi: 10.1002/cne.21919

    Figure Lengend Snippet: SLITRK1 protein expression in fetal and adult rhesus monkey and human brain. Immunolocalization of SLITRK1 with DAB staining. A,D,G,J: In monkey, as in human, SLITRK1 is expressed in prospective and mature cortical layers 3, 5, and 6 in both fetal (A,G) and adult (D,J) stages. B,H: SLITRK1 is expressed in cortical apical dendrites in fetal monkey and human brain. E,K: In adult monkey and human brain, SLITRK1 localization shifts toward the cell body of cortical pyramidal neurons. C,I: In fetal monkey and human striatum, SLITRK1 is highly expressed in striosomes. F,L: In adult monkey and human striatum, expression is significantly diminished, with no real presence in striosomes. CP, cortical plate; MZ, marginal zone; SP, subplate; 3, 5, 6, cortical layers 3, 5, and 6. Scale bars = 1 mm in A,C,D,F,G,I,J,L; 100 µm in B,E,H,K.

    Article Snippet: Western blotting Adult human brain protein extracts (Human Brain Protein Medley) were obtained from Clontech Laboratories (Mountain View, CA).

    Techniques: Expressing, Staining

    SLITRK1 protein expression is maintained in cholinergic interneurons of adult striatum. Sections of adult mouse, monkey, and human striatum immunolabeled with anti-SLITRK1 (black) and anti-ChAT (red). A–C: Representative SLITRK1-positive neurons in adult mouse (A), monkey (B), and human (C) striatum. D–F: SLITRK1-positive neurons in adult mouse (D), monkey (E), and human (F) striatum also express ChAT. Cholinergic interneurons are the only cells that express SLITRK1 in the adult striatum. Scale bar = 100 µm.

    Journal: The Journal of Comparative Neurology

    Article Title: Developmentally Regulated and Evolutionarily Conserved Expression of SLITRK1 in Brain Circuits Implicated in Tourette Syndrome

    doi: 10.1002/cne.21919

    Figure Lengend Snippet: SLITRK1 protein expression is maintained in cholinergic interneurons of adult striatum. Sections of adult mouse, monkey, and human striatum immunolabeled with anti-SLITRK1 (black) and anti-ChAT (red). A–C: Representative SLITRK1-positive neurons in adult mouse (A), monkey (B), and human (C) striatum. D–F: SLITRK1-positive neurons in adult mouse (D), monkey (E), and human (F) striatum also express ChAT. Cholinergic interneurons are the only cells that express SLITRK1 in the adult striatum. Scale bar = 100 µm.

    Article Snippet: Adult human brain protein extracts (Human Brain Protein Medley) were obtained from Clontech Laboratories (Mountain View, CA).

    Techniques: Expressing, Immunolabeling

    SLITRK1 protein expression in mouse brain. A,D,G,J: Right coronal hemisection views of E17.5, P2, P7, and adult brain immunostained with an antibody against the extracellular domain of SLITRK1. B,E: In late embryonic and early postnatal stages, SLITRK1 is predominantly expressed in apical dendrites. H,K: At later postnatal stages and in adult, SLITRK1 is localized predominantly to the cell body outlining a pyramidal shape. C,F,I: SLITRK1 is found in patch-like regions in the striatum. L: SLITRK1 expression is virtually undetectable in adult striatum, with only a few cells maintaining expression. SP, subplate. Scale bars = 25 µm in B,E,H,K; 100 µm in C,F,I,L.

    Journal: The Journal of Comparative Neurology

    Article Title: Developmentally Regulated and Evolutionarily Conserved Expression of SLITRK1 in Brain Circuits Implicated in Tourette Syndrome

    doi: 10.1002/cne.21919

    Figure Lengend Snippet: SLITRK1 protein expression in mouse brain. A,D,G,J: Right coronal hemisection views of E17.5, P2, P7, and adult brain immunostained with an antibody against the extracellular domain of SLITRK1. B,E: In late embryonic and early postnatal stages, SLITRK1 is predominantly expressed in apical dendrites. H,K: At later postnatal stages and in adult, SLITRK1 is localized predominantly to the cell body outlining a pyramidal shape. C,F,I: SLITRK1 is found in patch-like regions in the striatum. L: SLITRK1 expression is virtually undetectable in adult striatum, with only a few cells maintaining expression. SP, subplate. Scale bars = 25 µm in B,E,H,K; 100 µm in C,F,I,L.

    Article Snippet: Adult human brain protein extracts (Human Brain Protein Medley) were obtained from Clontech Laboratories (Mountain View, CA).

    Techniques: Expressing

    SLITRK1 protein expression in fetal and adult rhesus monkey and human brain. Immunolocalization of SLITRK1 with DAB staining. A,D,G,J: In monkey, as in human, SLITRK1 is expressed in prospective and mature cortical layers 3, 5, and 6 in both fetal (A,G) and adult (D,J) stages. B,H: SLITRK1 is expressed in cortical apical dendrites in fetal monkey and human brain. E,K: In adult monkey and human brain, SLITRK1 localization shifts toward the cell body of cortical pyramidal neurons. C,I: In fetal monkey and human striatum, SLITRK1 is highly expressed in striosomes. F,L: In adult monkey and human striatum, expression is significantly diminished, with no real presence in striosomes. CP, cortical plate; MZ, marginal zone; SP, subplate; 3, 5, 6, cortical layers 3, 5, and 6. Scale bars = 1 mm in A,C,D,F,G,I,J,L; 100 µm in B,E,H,K.

    Journal: The Journal of Comparative Neurology

    Article Title: Developmentally Regulated and Evolutionarily Conserved Expression of SLITRK1 in Brain Circuits Implicated in Tourette Syndrome

    doi: 10.1002/cne.21919

    Figure Lengend Snippet: SLITRK1 protein expression in fetal and adult rhesus monkey and human brain. Immunolocalization of SLITRK1 with DAB staining. A,D,G,J: In monkey, as in human, SLITRK1 is expressed in prospective and mature cortical layers 3, 5, and 6 in both fetal (A,G) and adult (D,J) stages. B,H: SLITRK1 is expressed in cortical apical dendrites in fetal monkey and human brain. E,K: In adult monkey and human brain, SLITRK1 localization shifts toward the cell body of cortical pyramidal neurons. C,I: In fetal monkey and human striatum, SLITRK1 is highly expressed in striosomes. F,L: In adult monkey and human striatum, expression is significantly diminished, with no real presence in striosomes. CP, cortical plate; MZ, marginal zone; SP, subplate; 3, 5, 6, cortical layers 3, 5, and 6. Scale bars = 1 mm in A,C,D,F,G,I,J,L; 100 µm in B,E,H,K.

    Article Snippet: Adult human brain protein extracts (Human Brain Protein Medley) were obtained from Clontech Laboratories (Mountain View, CA).

    Techniques: Expressing, Staining

    L-PGC-1α is recruited to PCK1 promoter and physically interacts with HNF4α. A, chromatin from HEK293 cells transfected with Halo-tagged expression plasmids as indicated was captured using HaloTag resin and analyzed by PCR amplifying a fragment spanning the predicted HNF4α binding site in the human PCK1 promoter. B, nuclear extracts from HEK293 cells transfected with Halo-tagged expression plasmids as indicated were subjected to pulldown with HaloTag resin followed by immunoblotting with a monoclonal HNF4α antibody. Histone-3 (H3) antibody was used as a loading control for nuclear extracts. WB, Western blot; neg., negative; IP, immunoprecipitation.

    Journal: The Journal of Biological Chemistry

    Article Title: Characterization of Novel Peroxisome Proliferator-activated Receptor ? Coactivator-1? (PGC-1?) Isoform in Human Liver *

    doi: 10.1074/jbc.M111.227496

    Figure Lengend Snippet: L-PGC-1α is recruited to PCK1 promoter and physically interacts with HNF4α. A, chromatin from HEK293 cells transfected with Halo-tagged expression plasmids as indicated was captured using HaloTag resin and analyzed by PCR amplifying a fragment spanning the predicted HNF4α binding site in the human PCK1 promoter. B, nuclear extracts from HEK293 cells transfected with Halo-tagged expression plasmids as indicated were subjected to pulldown with HaloTag resin followed by immunoblotting with a monoclonal HNF4α antibody. Histone-3 (H3) antibody was used as a loading control for nuclear extracts. WB, Western blot; neg., negative; IP, immunoprecipitation.

    Article Snippet: Immunoblotting Human brain tissue protein extract (Millipore, catalogue number CL302) and liver nuclear extract (Active Motif, catalogue number 36042) were used for immunoblotting.

    Techniques: Transfection, Expressing, Binding Assay, Western Blot, Immunoprecipitation

    Expression of neuronal adaptor protein (AP)-3 mRNA and protein in INS-1 β-cells and pancreatic islet extracts. A: PCR analysis was performed to determine whether the neuronal AP-3 subunits β3B and μ3B are expressed in human islets (Isl). Human brain (Br) cDNA was used as a positive control. PCR products of the expected size were detected in brain and islets for both β3B and μ3B. A negative control (−) in which no reverse transcriptase was added during the reverse transcription reaction (no RT control) is shown to the right of the brain and islet lanes. cDNA from human tissues (shown) and from rat tissues (not shown) yielded identical results. B: to determine whether β3B protein is expressed in islets, Western blot analysis was performed using a β3B-specific monoclonal antibody. As expected, β3B was detected in human (H), rat (R), and mouse (M) Br. β3B protein was also present in cell lysates from the insulin-secreting β-cell lines β-TC3 (β), HIT-T15 (Hit), and INS-1 (Ins) and in tissue lysates from human and rat Isl. β3B was not detected in human liver or in brain from β3B-knockout mice (Ref. 43 and data not shown). As observed previously, immunoblot detection of β3B yielded 2 bands (Mr of ∼140 K). C, left, lanes 1 and 2: μ3B was detected in INS-1 cell lysate (Ins) but not in rat liver lysate (Liv). C, right: μ3B produced by in vitro transcription and translation (lane 4) and analyzed by immunoblotting with the μ3B antibody ran at the expected Mr of ∼47,000. This band comigrated precisely with the band that was observed in INS-1 cells (lane 3). 35S-met was included in the in vitro translation reaction. Autoradiographic detection of the radiolabeled μ3B (lane 4) yielded a band that precisely aligned with the band detected by immunoblot analysis. This confirms that the μ3B antibody detected μ3B synthesized de novo in the in vitro transcription and translation reaction.

    Journal: American Journal of Physiology - Endocrinology and Metabolism

    Article Title: An AP-3-dependent mechanism drives synaptic-like microvesicle biogenesis in pancreatic islet ?-cells

    doi: 10.1152/ajpendo.00664.2009

    Figure Lengend Snippet: Expression of neuronal adaptor protein (AP)-3 mRNA and protein in INS-1 β-cells and pancreatic islet extracts. A: PCR analysis was performed to determine whether the neuronal AP-3 subunits β3B and μ3B are expressed in human islets (Isl). Human brain (Br) cDNA was used as a positive control. PCR products of the expected size were detected in brain and islets for both β3B and μ3B. A negative control (−) in which no reverse transcriptase was added during the reverse transcription reaction (no RT control) is shown to the right of the brain and islet lanes. cDNA from human tissues (shown) and from rat tissues (not shown) yielded identical results. B: to determine whether β3B protein is expressed in islets, Western blot analysis was performed using a β3B-specific monoclonal antibody. As expected, β3B was detected in human (H), rat (R), and mouse (M) Br. β3B protein was also present in cell lysates from the insulin-secreting β-cell lines β-TC3 (β), HIT-T15 (Hit), and INS-1 (Ins) and in tissue lysates from human and rat Isl. β3B was not detected in human liver or in brain from β3B-knockout mice (Ref. 43 and data not shown). As observed previously, immunoblot detection of β3B yielded 2 bands (Mr of ∼140 K). C, left, lanes 1 and 2: μ3B was detected in INS-1 cell lysate (Ins) but not in rat liver lysate (Liv). C, right: μ3B produced by in vitro transcription and translation (lane 4) and analyzed by immunoblotting with the μ3B antibody ran at the expected Mr of ∼47,000. This band comigrated precisely with the band that was observed in INS-1 cells (lane 3). 35S-met was included in the in vitro translation reaction. Autoradiographic detection of the radiolabeled μ3B (lane 4) yielded a band that precisely aligned with the band detected by immunoblot analysis. This confirms that the μ3B antibody detected μ3B synthesized de novo in the in vitro transcription and translation reaction.

    Article Snippet: Human brain and human and rat liver protein extracts were obtained commercially (Biochain, Hayward, CA, and ProSci, Poway, CA).

    Techniques: Expressing, Positive Control, Negative Control, Reverse Transcription, Control, Western Blot, Knock-Out, Produced, In Vitro, Synthesized