snaka51 Search Results


snaka51  (Novus Biologicals)
93
Novus Biologicals snaka51
Integrins are differentially activated by different flow patterns via Piezo1 and G q /G 11 . (A–C) HUAECs were transfected with scrambled siRNA (control) or siRNA directed against ITGA5 and ITGAV (A) or against Gα q and Gα 11 (Gα q/11 ; B and C) and were exposed to laminar or disturbed flow as described in . Activation of integrin signaling was determined by immunoblotting for phosphorylated focal adhesion kinase (pFAK, Y397; A) or by immunoprecipitation of activated α5 integrin (B and C). P65 activation was determined by anti–phospho-P65 (S536) antibodies (A). Bar diagrams show densitometric evaluation of immunoblots (quantification of three to five independent experiments). (D) Ldlr-KO mice without or with endothelium-specific Gα q /Gα 11 deficiency (Ldlr-KO;EC-Gα q/11 -KO) endothelium-specific Piezo1-deficiency (Ldlr-KO;EC-Piezo1-KO) were fed a high-fat diet for 4 wk ( n = 4–6 mice per genotype). Cross sections of the inner and outer curvatures of aortic arches were immunostained with antibodies against activated α5 integrin <t>(SNAKA51;</t> green), against the endothelial marker CD31 (red) or with DAPI (blue). Bar diagrams show percentage of area stained by anti-activated α5 integrin antibody of total endothelial cell area defined by staining by anti-CD31 antibody (based on analysis of at least five sections each from at least four different animals). Bars, 25 µm. Data represent mean ± SEM; *, P ≤ 0.05; **, P ≤ 0.01; ***, P ≤ 0.001 (two-tailed Student’s t test).
Snaka51, supplied by Novus Biologicals, 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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mouse mab anti-active α5 integrin clone snaka51  (Merck KGaA)
90
Merck KGaA mouse mab anti-active α5 integrin clone snaka51
(A, B, C) Representative confocal microscopy analysis of <t>SNAKA51</t> + active α5 integrin (A), β3 integrin (B), and soluble rhodamine-FN (C) localization in ECs that were incubated (bottom panels) or not (top panels) for 10 min with the anti-βI domain mAb 12G10. Scale bar 20 µ m; magnification scale bar 10 µ m. (A, C) When compared with untreated control (CTL) ECs, the mFD of SNAKA51 + fibrillar adhesions or rhodamine-FN + fibrils was significantly reduced in ECs treated with mAb 12G10. Data are mean ± S.D, n ≥ 34 cells per condition pooled from three independent experiments. Statistical analysis: unpaired t test, P ≤ 0.0001 ****. (B) The incubation of cultured ECs with mAb 12G10 did not influence number, mean area, or mFD of β3 integrin + focal adhesions. Data are mean ± S.D, n ≥ 32 cells per condition pooled from three independent experiments. Statistical analysis: unpaired t test. Source data are available for this figure.
Mouse Mab Anti Active α5 Integrin Clone Snaka51, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse mab anti-active α5 integrin clone snaka51/product/Merck KGaA
Average 90 stars, based on 1 article reviews
mouse mab anti-active α5 integrin clone snaka51 - by Bioz Stars, 2026-03
90/100 stars
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Image Search Results


Integrins are differentially activated by different flow patterns via Piezo1 and G q /G 11 . (A–C) HUAECs were transfected with scrambled siRNA (control) or siRNA directed against ITGA5 and ITGAV (A) or against Gα q and Gα 11 (Gα q/11 ; B and C) and were exposed to laminar or disturbed flow as described in . Activation of integrin signaling was determined by immunoblotting for phosphorylated focal adhesion kinase (pFAK, Y397; A) or by immunoprecipitation of activated α5 integrin (B and C). P65 activation was determined by anti–phospho-P65 (S536) antibodies (A). Bar diagrams show densitometric evaluation of immunoblots (quantification of three to five independent experiments). (D) Ldlr-KO mice without or with endothelium-specific Gα q /Gα 11 deficiency (Ldlr-KO;EC-Gα q/11 -KO) endothelium-specific Piezo1-deficiency (Ldlr-KO;EC-Piezo1-KO) were fed a high-fat diet for 4 wk ( n = 4–6 mice per genotype). Cross sections of the inner and outer curvatures of aortic arches were immunostained with antibodies against activated α5 integrin (SNAKA51; green), against the endothelial marker CD31 (red) or with DAPI (blue). Bar diagrams show percentage of area stained by anti-activated α5 integrin antibody of total endothelial cell area defined by staining by anti-CD31 antibody (based on analysis of at least five sections each from at least four different animals). Bars, 25 µm. Data represent mean ± SEM; *, P ≤ 0.05; **, P ≤ 0.01; ***, P ≤ 0.001 (two-tailed Student’s t test).

Journal: The Journal of Experimental Medicine

Article Title: Piezo1 and G q /G 11 promote endothelial inflammation depending on flow pattern and integrin activation

doi: 10.1084/jem.20180483

Figure Lengend Snippet: Integrins are differentially activated by different flow patterns via Piezo1 and G q /G 11 . (A–C) HUAECs were transfected with scrambled siRNA (control) or siRNA directed against ITGA5 and ITGAV (A) or against Gα q and Gα 11 (Gα q/11 ; B and C) and were exposed to laminar or disturbed flow as described in . Activation of integrin signaling was determined by immunoblotting for phosphorylated focal adhesion kinase (pFAK, Y397; A) or by immunoprecipitation of activated α5 integrin (B and C). P65 activation was determined by anti–phospho-P65 (S536) antibodies (A). Bar diagrams show densitometric evaluation of immunoblots (quantification of three to five independent experiments). (D) Ldlr-KO mice without or with endothelium-specific Gα q /Gα 11 deficiency (Ldlr-KO;EC-Gα q/11 -KO) endothelium-specific Piezo1-deficiency (Ldlr-KO;EC-Piezo1-KO) were fed a high-fat diet for 4 wk ( n = 4–6 mice per genotype). Cross sections of the inner and outer curvatures of aortic arches were immunostained with antibodies against activated α5 integrin (SNAKA51; green), against the endothelial marker CD31 (red) or with DAPI (blue). Bar diagrams show percentage of area stained by anti-activated α5 integrin antibody of total endothelial cell area defined by staining by anti-CD31 antibody (based on analysis of at least five sections each from at least four different animals). Bars, 25 µm. Data represent mean ± SEM; *, P ≤ 0.05; **, P ≤ 0.01; ***, P ≤ 0.001 (two-tailed Student’s t test).

Article Snippet: Cells were then incubated in flow chambers with primary antibody directed against activated integrin α5, SNAKA51 (Novus Biologicals, NBP2-50146), overnight at 4°C (1:100 dilution).

Techniques: Transfection, Control, Activation Assay, Western Blot, Immunoprecipitation, Marker, Staining, Two Tailed Test

(A, B, C) Representative confocal microscopy analysis of SNAKA51 + active α5 integrin (A), β3 integrin (B), and soluble rhodamine-FN (C) localization in ECs that were incubated (bottom panels) or not (top panels) for 10 min with the anti-βI domain mAb 12G10. Scale bar 20 µ m; magnification scale bar 10 µ m. (A, C) When compared with untreated control (CTL) ECs, the mFD of SNAKA51 + fibrillar adhesions or rhodamine-FN + fibrils was significantly reduced in ECs treated with mAb 12G10. Data are mean ± S.D, n ≥ 34 cells per condition pooled from three independent experiments. Statistical analysis: unpaired t test, P ≤ 0.0001 ****. (B) The incubation of cultured ECs with mAb 12G10 did not influence number, mean area, or mFD of β3 integrin + focal adhesions. Data are mean ± S.D, n ≥ 32 cells per condition pooled from three independent experiments. Statistical analysis: unpaired t test. Source data are available for this figure.

Journal: Life Science Alliance

Article Title: The βI domain promotes active β1 integrin clustering into mature adhesion sites

doi: 10.26508/lsa.202201388

Figure Lengend Snippet: (A, B, C) Representative confocal microscopy analysis of SNAKA51 + active α5 integrin (A), β3 integrin (B), and soluble rhodamine-FN (C) localization in ECs that were incubated (bottom panels) or not (top panels) for 10 min with the anti-βI domain mAb 12G10. Scale bar 20 µ m; magnification scale bar 10 µ m. (A, C) When compared with untreated control (CTL) ECs, the mFD of SNAKA51 + fibrillar adhesions or rhodamine-FN + fibrils was significantly reduced in ECs treated with mAb 12G10. Data are mean ± S.D, n ≥ 34 cells per condition pooled from three independent experiments. Statistical analysis: unpaired t test, P ≤ 0.0001 ****. (B) The incubation of cultured ECs with mAb 12G10 did not influence number, mean area, or mFD of β3 integrin + focal adhesions. Data are mean ± S.D, n ≥ 32 cells per condition pooled from three independent experiments. Statistical analysis: unpaired t test. Source data are available for this figure.

Article Snippet: Mouse mAbs anti-active β1 integrin clone 12G10 and clone HUTS4 and mouse mAb anti-active α5 integrin clone SNAKA51 were from Merck Millipore.

Techniques: Confocal Microscopy, Incubation, Control, Cell Culture

Confocal immunofluorescence microscopy analysis of ECs live treated with mAb SNAKA51 ( red ) alone or in combination with mAb 12G10 ( green ). The internalization of mAb SNAKA51–bound active α5 integrins in EEA1 + early endosomes ( blue ) was quantified by Pearson correlation coefficient. Treatment with the anti-βI domain mAb 12G10 promotes mAb SNAKA51–bound active α5 integrin endocytosis. Data are mean ± SD, n ≥ 26 cells per condition pooled from three independent experiments. Scale bar 20 µ m; magnification scale bar 10 µ m. Statistical analysis: unpaired t test; P ≤ 0.0001 ****. Source data are available for this figure.

Journal: Life Science Alliance

Article Title: The βI domain promotes active β1 integrin clustering into mature adhesion sites

doi: 10.26508/lsa.202201388

Figure Lengend Snippet: Confocal immunofluorescence microscopy analysis of ECs live treated with mAb SNAKA51 ( red ) alone or in combination with mAb 12G10 ( green ). The internalization of mAb SNAKA51–bound active α5 integrins in EEA1 + early endosomes ( blue ) was quantified by Pearson correlation coefficient. Treatment with the anti-βI domain mAb 12G10 promotes mAb SNAKA51–bound active α5 integrin endocytosis. Data are mean ± SD, n ≥ 26 cells per condition pooled from three independent experiments. Scale bar 20 µ m; magnification scale bar 10 µ m. Statistical analysis: unpaired t test; P ≤ 0.0001 ****. Source data are available for this figure.

Article Snippet: Mouse mAbs anti-active β1 integrin clone 12G10 and clone HUTS4 and mouse mAb anti-active α5 integrin clone SNAKA51 were from Merck Millipore.

Techniques: Immunofluorescence, Microscopy