rabbit anti-β3-integrin Search Results


rabbit anti β3 integrin  (Cell Signaling Technology Inc)
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mouse monoclonal anti β3 integrin  (Abcam)
98
Abcam mouse monoclonal anti β3 integrin
Mouse Monoclonal Anti β3 Integrin, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti β3 integrin  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology anti β3 integrin
Anti β3 Integrin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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β3 integrin (rabbit polyclonal clone h-96) antibody  (Santa Cruz Biotechnology)
90
Santa Cruz Biotechnology β3 integrin (rabbit polyclonal clone h-96) antibody
β3 Integrin (Rabbit Polyclonal Clone H 96) Antibody, supplied by Santa Cruz Biotechnology, 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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anti β3 integrin  (Proteintech)
94
Proteintech anti β3 integrin
Anti β3 Integrin, supplied by Proteintech, 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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anti β3 integrin 4702p  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc anti β3 integrin 4702p
Anti β3 Integrin 4702p, supplied by Cell Signaling Technology Inc, 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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chemicals armenian hamster antibody anti β3 integrin  (Santa Cruz Biotechnology)
92
Santa Cruz Biotechnology chemicals armenian hamster antibody anti β3 integrin
Chemicals Armenian Hamster Antibody Anti β3 Integrin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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β3-integrin  (Millipore)
90
Millipore β3-integrin
SPARC regulates <t>β3-integrin</t> complexes to control surface AMPARs. A, Representative images of surface β3-integrin expression showing increased intensity of surface β3-integrin puncta in SPARC-deficient cultures compared to WT cultures. Recombinant SPARC application (0.5 μg/ml, 48 h) restores surface β3-integrin levels in SPARC-deficient cultures. The boxed region is magnified below each image. B, Quantification of surface β3-integrin expression [ANOVA with post hoc Holm–Sidak test, *p = 0.000158 (n = 4)]. C, Surface β1-integrin levels are similar in WT and SPARC-deficient cultures [27.405 arbitrary units for WT versus 27.794 arbitrary units for SPARC-deficient cultures; 2-tailed t test, p = 0.845 (n = 3)]. D, HEK 293T cells expressing β3-integrin have reduced attachment to vitronectin in the presence of SPARC [ANOVA with post hoc Holm–Sidak test, *p = 0.0036, (n = 4)]. E, Diagram illustrating the domain structure of SPARC and location of Peptide 2.3. Peptide 2.3 reduces surface β3-integrin (F), GluR2 (G), and GluR1 (H) levels in SPARC-deficient cultures to a similar extent as the full-length protein [ANOVA with post hoc Holm–Sidak test, *p = 0.0081 for β3-integrin (n = 5), *p = 0.0127 for GluR2 (n = 5), and *p = 0.00511 for GluR1 (n = 4) vs control]. A peptide containing a scrambled sequence (scPep2.3) had no effect. I, Coapplication of the disintegrin Echistatin (300 nm) prevents SPARC rescue (0.5 μg/ml, 48 h) of surface GluR1 levels in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.003, SPARC-treated vs SPARC-treated and Echistatin condition). J, The β3-integrin function-blocking antibody Clone 2C9.G2 (10 μg/ml, 48 h) blocks SPARC-mediated rescue of surface GluR1 in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.006). An isotype-matched control antibody had no effect. Error bars indicate SEM. Scale bars, 20 μm.
β3 Integrin, supplied by Millipore, 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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rabbit monoclonal anti-β3 integrin antibody sj19-09  (Novus Biologicals)
90
Novus Biologicals rabbit monoclonal anti-β3 integrin antibody sj19-09
SPARC regulates <t>β3-integrin</t> complexes to control surface AMPARs. A, Representative images of surface β3-integrin expression showing increased intensity of surface β3-integrin puncta in SPARC-deficient cultures compared to WT cultures. Recombinant SPARC application (0.5 μg/ml, 48 h) restores surface β3-integrin levels in SPARC-deficient cultures. The boxed region is magnified below each image. B, Quantification of surface β3-integrin expression [ANOVA with post hoc Holm–Sidak test, *p = 0.000158 (n = 4)]. C, Surface β1-integrin levels are similar in WT and SPARC-deficient cultures [27.405 arbitrary units for WT versus 27.794 arbitrary units for SPARC-deficient cultures; 2-tailed t test, p = 0.845 (n = 3)]. D, HEK 293T cells expressing β3-integrin have reduced attachment to vitronectin in the presence of SPARC [ANOVA with post hoc Holm–Sidak test, *p = 0.0036, (n = 4)]. E, Diagram illustrating the domain structure of SPARC and location of Peptide 2.3. Peptide 2.3 reduces surface β3-integrin (F), GluR2 (G), and GluR1 (H) levels in SPARC-deficient cultures to a similar extent as the full-length protein [ANOVA with post hoc Holm–Sidak test, *p = 0.0081 for β3-integrin (n = 5), *p = 0.0127 for GluR2 (n = 5), and *p = 0.00511 for GluR1 (n = 4) vs control]. A peptide containing a scrambled sequence (scPep2.3) had no effect. I, Coapplication of the disintegrin Echistatin (300 nm) prevents SPARC rescue (0.5 μg/ml, 48 h) of surface GluR1 levels in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.003, SPARC-treated vs SPARC-treated and Echistatin condition). J, The β3-integrin function-blocking antibody Clone 2C9.G2 (10 μg/ml, 48 h) blocks SPARC-mediated rescue of surface GluR1 in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.006). An isotype-matched control antibody had no effect. Error bars indicate SEM. Scale bars, 20 μm.
Rabbit Monoclonal Anti β3 Integrin Antibody Sj19 09, supplied by Novus Biologicals, 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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rabbit anti-β3-integrin antibody  (Thermo Fisher)
90
Thermo Fisher rabbit anti-β3-integrin antibody
SPARC regulates <t>β3-integrin</t> complexes to control surface AMPARs. A, Representative images of surface β3-integrin expression showing increased intensity of surface β3-integrin puncta in SPARC-deficient cultures compared to WT cultures. Recombinant SPARC application (0.5 μg/ml, 48 h) restores surface β3-integrin levels in SPARC-deficient cultures. The boxed region is magnified below each image. B, Quantification of surface β3-integrin expression [ANOVA with post hoc Holm–Sidak test, *p = 0.000158 (n = 4)]. C, Surface β1-integrin levels are similar in WT and SPARC-deficient cultures [27.405 arbitrary units for WT versus 27.794 arbitrary units for SPARC-deficient cultures; 2-tailed t test, p = 0.845 (n = 3)]. D, HEK 293T cells expressing β3-integrin have reduced attachment to vitronectin in the presence of SPARC [ANOVA with post hoc Holm–Sidak test, *p = 0.0036, (n = 4)]. E, Diagram illustrating the domain structure of SPARC and location of Peptide 2.3. Peptide 2.3 reduces surface β3-integrin (F), GluR2 (G), and GluR1 (H) levels in SPARC-deficient cultures to a similar extent as the full-length protein [ANOVA with post hoc Holm–Sidak test, *p = 0.0081 for β3-integrin (n = 5), *p = 0.0127 for GluR2 (n = 5), and *p = 0.00511 for GluR1 (n = 4) vs control]. A peptide containing a scrambled sequence (scPep2.3) had no effect. I, Coapplication of the disintegrin Echistatin (300 nm) prevents SPARC rescue (0.5 μg/ml, 48 h) of surface GluR1 levels in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.003, SPARC-treated vs SPARC-treated and Echistatin condition). J, The β3-integrin function-blocking antibody Clone 2C9.G2 (10 μg/ml, 48 h) blocks SPARC-mediated rescue of surface GluR1 in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.006). An isotype-matched control antibody had no effect. Error bars indicate SEM. Scale bars, 20 μm.
Rabbit Anti β3 Integrin Antibody, supplied by Thermo Fisher, 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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mouse anti-αv integrin  (Millipore)
90
Millipore mouse anti-αv integrin
SPARC regulates <t>β3-integrin</t> complexes to control surface AMPARs. A, Representative images of surface β3-integrin expression showing increased intensity of surface β3-integrin puncta in SPARC-deficient cultures compared to WT cultures. Recombinant SPARC application (0.5 μg/ml, 48 h) restores surface β3-integrin levels in SPARC-deficient cultures. The boxed region is magnified below each image. B, Quantification of surface β3-integrin expression [ANOVA with post hoc Holm–Sidak test, *p = 0.000158 (n = 4)]. C, Surface β1-integrin levels are similar in WT and SPARC-deficient cultures [27.405 arbitrary units for WT versus 27.794 arbitrary units for SPARC-deficient cultures; 2-tailed t test, p = 0.845 (n = 3)]. D, HEK 293T cells expressing β3-integrin have reduced attachment to vitronectin in the presence of SPARC [ANOVA with post hoc Holm–Sidak test, *p = 0.0036, (n = 4)]. E, Diagram illustrating the domain structure of SPARC and location of Peptide 2.3. Peptide 2.3 reduces surface β3-integrin (F), GluR2 (G), and GluR1 (H) levels in SPARC-deficient cultures to a similar extent as the full-length protein [ANOVA with post hoc Holm–Sidak test, *p = 0.0081 for β3-integrin (n = 5), *p = 0.0127 for GluR2 (n = 5), and *p = 0.00511 for GluR1 (n = 4) vs control]. A peptide containing a scrambled sequence (scPep2.3) had no effect. I, Coapplication of the disintegrin Echistatin (300 nm) prevents SPARC rescue (0.5 μg/ml, 48 h) of surface GluR1 levels in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.003, SPARC-treated vs SPARC-treated and Echistatin condition). J, The β3-integrin function-blocking antibody Clone 2C9.G2 (10 μg/ml, 48 h) blocks SPARC-mediated rescue of surface GluR1 in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.006). An isotype-matched control antibody had no effect. Error bars indicate SEM. Scale bars, 20 μm.
Mouse Anti αv Integrin, supplied by Millipore, 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


SPARC regulates β3-integrin complexes to control surface AMPARs. A, Representative images of surface β3-integrin expression showing increased intensity of surface β3-integrin puncta in SPARC-deficient cultures compared to WT cultures. Recombinant SPARC application (0.5 μg/ml, 48 h) restores surface β3-integrin levels in SPARC-deficient cultures. The boxed region is magnified below each image. B, Quantification of surface β3-integrin expression [ANOVA with post hoc Holm–Sidak test, *p = 0.000158 (n = 4)]. C, Surface β1-integrin levels are similar in WT and SPARC-deficient cultures [27.405 arbitrary units for WT versus 27.794 arbitrary units for SPARC-deficient cultures; 2-tailed t test, p = 0.845 (n = 3)]. D, HEK 293T cells expressing β3-integrin have reduced attachment to vitronectin in the presence of SPARC [ANOVA with post hoc Holm–Sidak test, *p = 0.0036, (n = 4)]. E, Diagram illustrating the domain structure of SPARC and location of Peptide 2.3. Peptide 2.3 reduces surface β3-integrin (F), GluR2 (G), and GluR1 (H) levels in SPARC-deficient cultures to a similar extent as the full-length protein [ANOVA with post hoc Holm–Sidak test, *p = 0.0081 for β3-integrin (n = 5), *p = 0.0127 for GluR2 (n = 5), and *p = 0.00511 for GluR1 (n = 4) vs control]. A peptide containing a scrambled sequence (scPep2.3) had no effect. I, Coapplication of the disintegrin Echistatin (300 nm) prevents SPARC rescue (0.5 μg/ml, 48 h) of surface GluR1 levels in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.003, SPARC-treated vs SPARC-treated and Echistatin condition). J, The β3-integrin function-blocking antibody Clone 2C9.G2 (10 μg/ml, 48 h) blocks SPARC-mediated rescue of surface GluR1 in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.006). An isotype-matched control antibody had no effect. Error bars indicate SEM. Scale bars, 20 μm.

Journal: The Journal of Neuroscience

Article Title: Astrocytes Control Glutamate Receptor Levels at Developing Synapses through SPARC–β-Integrin Interactions

doi: 10.1523/JNEUROSCI.4757-10.2011

Figure Lengend Snippet: SPARC regulates β3-integrin complexes to control surface AMPARs. A, Representative images of surface β3-integrin expression showing increased intensity of surface β3-integrin puncta in SPARC-deficient cultures compared to WT cultures. Recombinant SPARC application (0.5 μg/ml, 48 h) restores surface β3-integrin levels in SPARC-deficient cultures. The boxed region is magnified below each image. B, Quantification of surface β3-integrin expression [ANOVA with post hoc Holm–Sidak test, *p = 0.000158 (n = 4)]. C, Surface β1-integrin levels are similar in WT and SPARC-deficient cultures [27.405 arbitrary units for WT versus 27.794 arbitrary units for SPARC-deficient cultures; 2-tailed t test, p = 0.845 (n = 3)]. D, HEK 293T cells expressing β3-integrin have reduced attachment to vitronectin in the presence of SPARC [ANOVA with post hoc Holm–Sidak test, *p = 0.0036, (n = 4)]. E, Diagram illustrating the domain structure of SPARC and location of Peptide 2.3. Peptide 2.3 reduces surface β3-integrin (F), GluR2 (G), and GluR1 (H) levels in SPARC-deficient cultures to a similar extent as the full-length protein [ANOVA with post hoc Holm–Sidak test, *p = 0.0081 for β3-integrin (n = 5), *p = 0.0127 for GluR2 (n = 5), and *p = 0.00511 for GluR1 (n = 4) vs control]. A peptide containing a scrambled sequence (scPep2.3) had no effect. I, Coapplication of the disintegrin Echistatin (300 nm) prevents SPARC rescue (0.5 μg/ml, 48 h) of surface GluR1 levels in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.003, SPARC-treated vs SPARC-treated and Echistatin condition). J, The β3-integrin function-blocking antibody Clone 2C9.G2 (10 μg/ml, 48 h) blocks SPARC-mediated rescue of surface GluR1 in SPARC-deficient cultures (ANOVA with post hoc Holm–Sidak test, *p = 0.006). An isotype-matched control antibody had no effect. Error bars indicate SEM. Scale bars, 20 μm.

Article Snippet: The following antibodies were used in this study: mouse SPARC AF942 (goat polyclonal, R and D Systems), Hevin/SC1 (rat polyclonal, R and D Systems), GFAP (mouse monoclonal, Sigma), GFAP (rabbit polyclonal, Millipore), glutamine synthetase (mouse monoclonal, Millipore), IBA-1 (rabbit polyclonal, Wako), GluR1 N-terminal (rabbit polyclonal, Calbiochem), GluR1 C-terminal CT3 (rabbit monoclonal, Millipore), GluR1 N-terminal RH95 (mouse monoclonal, Millipore), GluR2 N-terminal (mouse monoclonal, Millipore), β3-integrin (rabbit polyclonal AB1932, Millipore), NeuN (mouse monoclonal, Millipore), MAP2 clone HM-2 (mouse monoclonal, Sigma), PSD-95 (mouse monoclonal, NeuroMab/Antibodies), Synapsin (rabbit polyclonal, Synaptic Systems), NR1 (mouse monoclonal clone 54.1, Millipore), GAPDH (Abcam), hamster anti-mouse β3-integrin clone 2C9.G2 (BD Biosciences), hamster IgG1 κ isotype control (BD Biosciences), and anti-goat and rat HRP (GE Healthcare).

Techniques: Expressing, Recombinant, Sequencing, Blocking Assay