anti βiii spectrin Search Results


90
ICN Biomedicals monoclonal anti- -fodrin
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Enzo Biochem mouse monoclonal anti α-fodrin (αii-spectrin
Mouse Monoclonal Anti α Fodrin (αii Spectrin, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ProSci Incorporated fodrin
Fodrin, supplied by ProSci Incorporated, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cell Signaling Technology Inc anti fodrin
Anti Fodrin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Becton Dickinson mouse anti-βii-spectrin 1:2000
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Enzo Biochem mouse a-fodrin
Mouse A Fodrin, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology mouse monoclonal anti spectrin βii antibody
FIGURE 2 Two-colored dSTORM images revealing the organization of actin and <t>spectrin</t> in the LSEC cytoskeleton. Intact control cells (first row) and LSECs treated with 21 μM CB for 30 minutes before fixation (second row). Spectrin (red, spectrin β <t>II</t> Antibody conjugated with Alexa Fluor 647) and actin (green, phalloidin Atto488) distribution at the interconnection of several LSECs are shown in the left panels. The right panels present the magnifications of the selected areas (white squares) where independent and merged channels are shown. In the control samples, the encircled areas indicate sieve plates. The individual fenestrae are identified only in CB-treated samples in TIRF mode as black (eg, arrowheads)
Mouse Monoclonal Anti Spectrin βii Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cell Signaling Technology Inc cleaved fodrin
Fig. 7 Effect of sPLA2 III on the expression of cleaved <t>a-Fodrin</t> in neuronal cultures. (a1) Representative western blots showing cleaved a-Fodrin (upper panel), and b-actin protein expression (lower panel). (a2) Quantitative analysis of cleaved a-Fodrin protein expression after sPLA2 III (0.1 lg/mL) treatment for 10 h and 20 h, and pre-treatment by hypoxic pre-conditioning (HPC) (2 h) with or without rapamycin (40 nM) <t>and</t> <t>STAT3</t> shRNA (2.0 lg). The levels of cleaved a-Fodrin protein decreased by HPC and this decline was counteracted partly by pre-treatment with rapamycin and STAT3 shRNA, compared with sPLA2 III treatment (0.1 lg/mL) for 20 h. The data shown are pre- sented as the means ± SE of three separate experiments (n = 3). *p < 0.05 versus the normal control (time 0); ^p < 0.05 versus sPLA2 III group (time 20 h); and #p < 0.05 versus HPC group (time 20 h).
Cleaved Fodrin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology anti βiii spectrin
Fig. 1 A Cell-autonomous role of <t>βIII</t> <t>spectrin</t> in the planar dendrite formation in vivo
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Santa Cruz Biotechnology anti spectrin βiii
Fig. 1 A Cell-autonomous role of <t>βIII</t> <t>spectrin</t> in the planar dendrite formation in vivo
Anti Spectrin βiii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology spectrin βii
Fig. 1 A Cell-autonomous role of <t>βIII</t> <t>spectrin</t> in the planar dendrite formation in vivo
Spectrin βii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Biomol GmbH mouse anti-fodrin
Fig. 1 A Cell-autonomous role of <t>βIII</t> <t>spectrin</t> in the planar dendrite formation in vivo
Mouse Anti Fodrin, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


FIGURE 2 Two-colored dSTORM images revealing the organization of actin and spectrin in the LSEC cytoskeleton. Intact control cells (first row) and LSECs treated with 21 μM CB for 30 minutes before fixation (second row). Spectrin (red, spectrin β II Antibody conjugated with Alexa Fluor 647) and actin (green, phalloidin Atto488) distribution at the interconnection of several LSECs are shown in the left panels. The right panels present the magnifications of the selected areas (white squares) where independent and merged channels are shown. In the control samples, the encircled areas indicate sieve plates. The individual fenestrae are identified only in CB-treated samples in TIRF mode as black (eg, arrowheads)

Journal: Traffic (Copenhagen, Denmark)

Article Title: Actin-spectrin scaffold supports open fenestrae in liver sinusoidal endothelial cells.

doi: 10.1111/tra.12700

Figure Lengend Snippet: FIGURE 2 Two-colored dSTORM images revealing the organization of actin and spectrin in the LSEC cytoskeleton. Intact control cells (first row) and LSECs treated with 21 μM CB for 30 minutes before fixation (second row). Spectrin (red, spectrin β II Antibody conjugated with Alexa Fluor 647) and actin (green, phalloidin Atto488) distribution at the interconnection of several LSECs are shown in the left panels. The right panels present the magnifications of the selected areas (white squares) where independent and merged channels are shown. In the control samples, the encircled areas indicate sieve plates. The individual fenestrae are identified only in CB-treated samples in TIRF mode as black (eg, arrowheads)

Article Snippet: The membranes were blocked in a 1x Tris-buffered saline (TBS; pH 7.5) containing 5% wt/vol nonfat dry milk, incubated with a primary mouse monoclonal Anti-Spectrin βII antibody (Santa Cruz Biotechnology) 1:1000 in TBS buffer for 1.5 hours at room temperature, and with mouse IgG kappa binding protein (m-IgGκ BP) conjugated to horseradish peroxidase (Santa Cruz Biotechnology), 1:5000 for 45 minutes.

Techniques: Control

FIGURE 3 High-magnification dSTORM image of the cytoskeleton of CB-treated LSECs. A, The cytoplasmic distributions of actin (green, phalloidin Atto 488) and spectrin (red, spectrin β II antibody conjugated with Alexa Fluor 647). Arrowheads indicate individual fenestrae. B, Magnification of the selected white line indicating the cross section presented in C. D, Magnification of the single fenestrae marked in C. Separated channels show spectrin and actin distribution around the fenestra

Journal: Traffic (Copenhagen, Denmark)

Article Title: Actin-spectrin scaffold supports open fenestrae in liver sinusoidal endothelial cells.

doi: 10.1111/tra.12700

Figure Lengend Snippet: FIGURE 3 High-magnification dSTORM image of the cytoskeleton of CB-treated LSECs. A, The cytoplasmic distributions of actin (green, phalloidin Atto 488) and spectrin (red, spectrin β II antibody conjugated with Alexa Fluor 647). Arrowheads indicate individual fenestrae. B, Magnification of the selected white line indicating the cross section presented in C. D, Magnification of the single fenestrae marked in C. Separated channels show spectrin and actin distribution around the fenestra

Article Snippet: The membranes were blocked in a 1x Tris-buffered saline (TBS; pH 7.5) containing 5% wt/vol nonfat dry milk, incubated with a primary mouse monoclonal Anti-Spectrin βII antibody (Santa Cruz Biotechnology) 1:1000 in TBS buffer for 1.5 hours at room temperature, and with mouse IgG kappa binding protein (m-IgGκ BP) conjugated to horseradish peroxidase (Santa Cruz Biotechnology), 1:5000 for 45 minutes.

Techniques:

FIGURE 4 Western blot of spectrin in control and DIA-treated LSECs (500 μM, 5 minutes) (top). Elasticity parameter (effective Young's modulus) calculated from Hertz-Sneddon model fit to the force-distance curves taken at the nuclear part of live LSECs, both untreated and treated with DIA (500 μM), CB (21 μM) or IAA (10 μM) (bottom). The boxes indicate SD (SD), with a line and black dot indicating the median and mean value, respectively. *P < .001

Journal: Traffic (Copenhagen, Denmark)

Article Title: Actin-spectrin scaffold supports open fenestrae in liver sinusoidal endothelial cells.

doi: 10.1111/tra.12700

Figure Lengend Snippet: FIGURE 4 Western blot of spectrin in control and DIA-treated LSECs (500 μM, 5 minutes) (top). Elasticity parameter (effective Young's modulus) calculated from Hertz-Sneddon model fit to the force-distance curves taken at the nuclear part of live LSECs, both untreated and treated with DIA (500 μM), CB (21 μM) or IAA (10 μM) (bottom). The boxes indicate SD (SD), with a line and black dot indicating the median and mean value, respectively. *P < .001

Article Snippet: The membranes were blocked in a 1x Tris-buffered saline (TBS; pH 7.5) containing 5% wt/vol nonfat dry milk, incubated with a primary mouse monoclonal Anti-Spectrin βII antibody (Santa Cruz Biotechnology) 1:1000 in TBS buffer for 1.5 hours at room temperature, and with mouse IgG kappa binding protein (m-IgGκ BP) conjugated to horseradish peroxidase (Santa Cruz Biotechnology), 1:5000 for 45 minutes.

Techniques: Western Blot, Control

Fig. 7 Effect of sPLA2 III on the expression of cleaved a-Fodrin in neuronal cultures. (a1) Representative western blots showing cleaved a-Fodrin (upper panel), and b-actin protein expression (lower panel). (a2) Quantitative analysis of cleaved a-Fodrin protein expression after sPLA2 III (0.1 lg/mL) treatment for 10 h and 20 h, and pre-treatment by hypoxic pre-conditioning (HPC) (2 h) with or without rapamycin (40 nM) and STAT3 shRNA (2.0 lg). The levels of cleaved a-Fodrin protein decreased by HPC and this decline was counteracted partly by pre-treatment with rapamycin and STAT3 shRNA, compared with sPLA2 III treatment (0.1 lg/mL) for 20 h. The data shown are pre- sented as the means ± SE of three separate experiments (n = 3). *p < 0.05 versus the normal control (time 0); ^p < 0.05 versus sPLA2 III group (time 20 h); and #p < 0.05 versus HPC group (time 20 h).

Journal: Journal of neurochemistry

Article Title: Hypoxic preconditioning suppresses group III secreted phospholipase A2-induced apoptosis via JAK2-STAT3 activation in cortical neurons.

doi: 10.1111/j.1471-4159.2010.06817.x

Figure Lengend Snippet: Fig. 7 Effect of sPLA2 III on the expression of cleaved a-Fodrin in neuronal cultures. (a1) Representative western blots showing cleaved a-Fodrin (upper panel), and b-actin protein expression (lower panel). (a2) Quantitative analysis of cleaved a-Fodrin protein expression after sPLA2 III (0.1 lg/mL) treatment for 10 h and 20 h, and pre-treatment by hypoxic pre-conditioning (HPC) (2 h) with or without rapamycin (40 nM) and STAT3 shRNA (2.0 lg). The levels of cleaved a-Fodrin protein decreased by HPC and this decline was counteracted partly by pre-treatment with rapamycin and STAT3 shRNA, compared with sPLA2 III treatment (0.1 lg/mL) for 20 h. The data shown are pre- sented as the means ± SE of three separate experiments (n = 3). *p < 0.05 versus the normal control (time 0); ^p < 0.05 versus sPLA2 III group (time 20 h); and #p < 0.05 versus HPC group (time 20 h).

Article Snippet: Antibodies against phospho-JAK2, and phospho-STAT3, caspase 3, cleaved caspase 3, cleaved fodrin, Bax, and Bcl-xl were purchased from Cell Signaling Technology (Beverly, MA, USA).

Techniques: Expressing, Western Blot, shRNA, Control

Fig. 1 A Cell-autonomous role of βIII spectrin in the planar dendrite formation in vivo

Journal: Development (Cambridge, England)

Article Title: βIII spectrin controls the planarity of Purkinje cell dendrites by modulating perpendicular axon-dendrite interactions.

doi: 10.1242/dev.194530

Figure Lengend Snippet: Fig. 1 A Cell-autonomous role of βIII spectrin in the planar dendrite formation in vivo

Article Snippet: The protein was labeled with anti-βIII spectrin (Santa Cruz, SC-28273) and a secondary antibody conjugated with Alexa555 (Thermo Fisher).

Techniques: In Vivo