p fak y397 rabbit ab Search Results


fak  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology fak
(a) Effect of simvastatin on expressions of β1‐integrin mRNA transcript and protein. Analysis of β1‐integrin mRNA expression using reverse transcription‐polymerase chain reaction (RT‐PCR). Head and neck squamous cell carcinoma cells were incubated for 48 h with 5 or 10 µM simvastatin and compared with untreated cells (incubated with vehicle). (b) Analysis of β1‐integrin, <t>FAK,</t> and <t>p‐FAK</t> <t>(Y397)</t> expressions using western blot. The condition of cell culture was identical with that of RT‐PCR analysis. The intensity of each band of western blot was determined using NIH Image program and the ratio of β1‐integrin and β‐actin was calculated for each treatment. The β1‐integrin/β‐actin ratio in untreated cells was set as 1. GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.
Fak, 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
https://www.bioz.com/product/p+fak+y397+rabbit+ab/p21/pmc11159053-106-43-45
Average 96 stars, based on 1 article reviews
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phospho fak tyr 397  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc phospho fak tyr 397
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Phospho Fak Tyr 397, 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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Average 96 stars, based on 1 article reviews
phospho fak tyr 397 - by Bioz Stars, 2026-10
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p fak y397  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc p fak y397
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
P Fak Y397, 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
https://www.bioz.com/product/p+fak+y397+rabbit+ab/Phospho-FAK+(Tyr397)+Rabbit+mAb/pmc04694986-164-16-19
Average 96 stars, based on 1 article reviews
p fak y397 - by Bioz Stars, 2026-10
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rabbit monoclonal anti phospho fak  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc rabbit monoclonal anti phospho fak
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Rabbit Monoclonal Anti Phospho Fak, supplied by Cell Signaling Technology Inc, 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/product/p+fak+y397+rabbit+ab/FAK+XP+Rabbit+mAb/pmc08990080-302-5-11
Average 90 stars, based on 1 article reviews
rabbit monoclonal anti phospho fak - by Bioz Stars, 2026-10
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rabbit polyclonal anti p fak y397  (Danaher Inc)
99
Danaher Inc rabbit polyclonal anti p fak y397
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Rabbit Polyclonal Anti P Fak Y397, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p+fak+y397+rabbit+ab/Rabbit+Polyclonal+Anti-JAK2+(phospho+Y1007)+antibody/pmc04090039-134-24-31
Average 99 stars, based on 1 article reviews
rabbit polyclonal anti p fak y397 - by Bioz Stars, 2026-10
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anti phospho fak y397  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc anti phospho fak y397
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Anti Phospho Fak Y397, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p+fak+y397+rabbit+ab/Phospho-FAK+(Tyr576%2F577)+Antibody/10__2147_slash_cmar__s196509-37-18-32
Average 95 stars, based on 1 article reviews
anti phospho fak y397 - by Bioz Stars, 2026-10
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p fak  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc p fak
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
P Fak, 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
https://www.bioz.com/product/p+fak+y397+rabbit+ab/FAK+Antibody/10__3390_slash_molecules24101928-201-16-40
Average 96 stars, based on 1 article reviews
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phosphorylation  (Boster Bio)
91
Boster Bio phosphorylation
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Phosphorylation, supplied by Boster Bio, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p+fak+y397+rabbit+ab/Anti-Phospho-FAK+(Y397)+PTK2+Rabbit+Monoclonal+Antibody/pmc06178139-96-18-23
Average 91 stars, based on 1 article reviews
phosphorylation - by Bioz Stars, 2026-10
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rabbit anti–phospho-fak (y397  (Becton Dickinson)
90
Becton Dickinson rabbit anti–phospho-fak (y397
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Rabbit Anti–Phospho Fak (Y397, supplied by Becton Dickinson, 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/product/p+fak+y397+rabbit+ab/p+fak++y397+antibody/pmc04258507-113-18-20
Average 90 stars, based on 1 article reviews
rabbit anti–phospho-fak (y397 - by Bioz Stars, 2026-10
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fak phosphospecific antibody  (Bethyl)
86
Bethyl fak phosphospecific antibody
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
Fak Phosphospecific Antibody, supplied by Bethyl, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 86 stars, based on 1 article reviews
fak phosphospecific antibody - by Bioz Stars, 2026-10
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phospho fak y397 p fak  (ABclonal Biotechnology)
94
ABclonal Biotechnology phospho fak y397 p fak
Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK <t>Tyr-397,</t> total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).
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(a) Effect of simvastatin on expressions of β1‐integrin mRNA transcript and protein. Analysis of β1‐integrin mRNA expression using reverse transcription‐polymerase chain reaction (RT‐PCR). Head and neck squamous cell carcinoma cells were incubated for 48 h with 5 or 10 µM simvastatin and compared with untreated cells (incubated with vehicle). (b) Analysis of β1‐integrin, FAK, and p‐FAK (Y397) expressions using western blot. The condition of cell culture was identical with that of RT‐PCR analysis. The intensity of each band of western blot was determined using NIH Image program and the ratio of β1‐integrin and β‐actin was calculated for each treatment. The β1‐integrin/β‐actin ratio in untreated cells was set as 1. GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.

Journal: Cancer Science

Article Title: Simvastatin inactivates β1‐integrin and extracellular signal‐related kinase signaling and inhibits cell proliferation in head and neck squamous cell carcinoma cells

doi: 10.1111/j.1349-7006.2007.00471.x

Figure Lengend Snippet: (a) Effect of simvastatin on expressions of β1‐integrin mRNA transcript and protein. Analysis of β1‐integrin mRNA expression using reverse transcription‐polymerase chain reaction (RT‐PCR). Head and neck squamous cell carcinoma cells were incubated for 48 h with 5 or 10 µM simvastatin and compared with untreated cells (incubated with vehicle). (b) Analysis of β1‐integrin, FAK, and p‐FAK (Y397) expressions using western blot. The condition of cell culture was identical with that of RT‐PCR analysis. The intensity of each band of western blot was determined using NIH Image program and the ratio of β1‐integrin and β‐actin was calculated for each treatment. The β1‐integrin/β‐actin ratio in untreated cells was set as 1. GAPDH, glyceraldehyde‐3‐phosphate dehydrogenase.

Article Snippet: Antibodies for immunoblotting were obtained from the following sources: rabbit polyclonal anti‐ERK1/2 (Santa Cruz Biotechnology, Santa Cruz, CA, USA); mouse monoclonal anti‐phospho‐ERK1/2 (Santa Cruz Biotechnology); rabbit polyclonal anti‐β1‐integrin (Chemicon International Inc., Temecula, CA, USA); rabbit polyclonal anti‐FAK (Santa Cruz Biotechnology); rabbit polyclonal anti‐phosphorylated FAK (Y397; Santa Cruz Biotechnology); mouse monoclonal anti‐p21 (Santa Cruz Biotechnology); mouse monoclonal anti‐p27 (Santa Cruz Biotechnology); mouse monoclonal anti‐thymidylate synthase (Chemicon); rabbit polyclonal anti‐active‐caspase‐3 (BioVision, Mountain View, CA, USA); and mouse monoclonal anti‐β‐actin (Abcam, Cambridge, MA, USA).

Techniques: Expressing, Reverse Transcription, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Incubation, Western Blot, Cell Culture

Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK Tyr-397, total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).

Journal: The Journal of Biological Chemistry

Article Title: Toxoplasma gondii disrupts β1 integrin signaling and focal adhesion formation during monocyte hypermotility

doi: 10.1074/jbc.M117.793281

Figure Lengend Snippet: Phosphorylation of FAK and Pyk2 in monocytes during cell adhesion. A, primary human monocytes were mock infected or infected with T. gondii for 4 h and either lysed in suspension or settled on fibronectin for 15, 30, or 60 min prior to lysis. Total lysates were separated by SDS-PAGE and examined by Western blotting for total FAK, p-FAK Tyr-397, total Pyk2, p-Pyk2 Tyr-402, and β-actin. Molecular weight markers (MW) are shown to the right of each blot. Representative blots from three independent experiments are shown. B and C, densitometry was performed on Western blots of FAK (B) and Pyk2 (C) by normalizing band intensities to β-actin. p-FAK Tyr-397 and p-Pyk2 Tyr-402 levels were normalized to total FAK or total Pyk2 band intensities, respectively. Error bars display the mean ± S.D. from three independent experiments (*, p < 0.05; one-way ANOVA with a Bonferroni post hoc test). D, transcript levels of PTK2 and PTK2B (the gene names for FAK and Pyk2, respectively) relative to GAPDH were quantified by qPCR. RNA was isolated from freshly elutriated primary human monocytes (0 h) or monocytes cultured for 4 h in mock conditions or with T. gondii. Error bars indicate the mean ± S.D. from three independent experiments. (*, p < 0.05; **, p < 0.01; one-way ANOVA with a Bonferroni post hoc test). E, primary human monocytes were mock treated or cultured with T. gondii of Type I (RH strain) or Type II (Prugniaud strain) lineage for 4 h or treated with LPS. Monocytes were then settled onto immobilized fibronectin, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, and β-actin. Representative blots from three independent experiments are shown. F, a simplified model of FAK phosphorylation and subsequent FAK-mediated signaling for cell adhesion is illustrated. Autophosphorylation at Tyr-397 induces FAK association with Src and signals for adhesome formation. The association results in Src phosphorylation of FAK at Tyr-925, located within the C-terminal focal adhesion targeting (FAT) domain. G, primary human monocytes were mock infected or cultured with T. gondii for 4 h, settled onto fibronectin for 30 min, lysed, and analyzed by Western blotting using antibodies for total FAK, p-FAK Tyr-397, p-FAK Tyr-925, and β-actin. Representative blots from four independent experiments are shown. H, quantification of p-FAK Tyr-925 levels relative to total FAK at 30 min post settling was performed by using densitometry of Western blots. Error bars display the mean ± S.D. from four independent experiments. (*, p < 0.05; Student's t-test).

Article Snippet: Gels were transferred to polyvinylidene difluoride (PVDF) (Bio-Rad, Hercules, CA) and probed using antibodies for FAK (D2R2E), phospho-FAK Tyr-397 (D20B1), or polyclonal antibodies against phospho-FAK Tyr-925, Pyk2 (H364), phospho-Pyk2 Tyr-402 from Cell Signaling Technology (Danvers, MA); vinculin (7F9) or talin (TA205) from EMD Millipore; or β-actin (AC-15, Sigma Aldrich).

Techniques: Infection, Lysis, SDS Page, Western Blot, Molecular Weight, Isolation, Cell Culture

Generation of eGFP-FAK THP-1 cells. A, eGFP-FAK was expressed in THP-1 monocytic cells by retroviral transduction, and the cells were imaged by live cell fluorescence microscopy. B, the transduced cells were single-cell cloned, and the clonal population was compared with the parental THP-1 cells by flow cytometry. Debris and dead cells were gated out based on a propidium iodide (PI) viability stain, and eGFP expression of the THP-1 and eGFP-FAK THP-1 cells was represented as histograms. C, eGFP-FAK THP-1 cells were mock infected or infected with T. gondii for 4 h and left unsettled or settled onto fibronectin for 30 min. Cells were lysed and analyzed by Western blotting using antibodies for total eGFP-FAK, phosphorylated eGFP-FAK at Tyr-397 (p-FAK Tyr-397), talin, vinculin, and β-actin. Representative blots from four independent experiments are shown. D, densitometry was performed on Western blots of p-FAK Tyr-397 by normalizing band intensities to total FAK. Error bars display the mean ± S.D. from four independent experiments (*, p < 0.05; Student's t-test).

Journal: The Journal of Biological Chemistry

Article Title: Toxoplasma gondii disrupts β1 integrin signaling and focal adhesion formation during monocyte hypermotility

doi: 10.1074/jbc.M117.793281

Figure Lengend Snippet: Generation of eGFP-FAK THP-1 cells. A, eGFP-FAK was expressed in THP-1 monocytic cells by retroviral transduction, and the cells were imaged by live cell fluorescence microscopy. B, the transduced cells were single-cell cloned, and the clonal population was compared with the parental THP-1 cells by flow cytometry. Debris and dead cells were gated out based on a propidium iodide (PI) viability stain, and eGFP expression of the THP-1 and eGFP-FAK THP-1 cells was represented as histograms. C, eGFP-FAK THP-1 cells were mock infected or infected with T. gondii for 4 h and left unsettled or settled onto fibronectin for 30 min. Cells were lysed and analyzed by Western blotting using antibodies for total eGFP-FAK, phosphorylated eGFP-FAK at Tyr-397 (p-FAK Tyr-397), talin, vinculin, and β-actin. Representative blots from four independent experiments are shown. D, densitometry was performed on Western blots of p-FAK Tyr-397 by normalizing band intensities to total FAK. Error bars display the mean ± S.D. from four independent experiments (*, p < 0.05; Student's t-test).

Article Snippet: Gels were transferred to polyvinylidene difluoride (PVDF) (Bio-Rad, Hercules, CA) and probed using antibodies for FAK (D2R2E), phospho-FAK Tyr-397 (D20B1), or polyclonal antibodies against phospho-FAK Tyr-925, Pyk2 (H364), phospho-Pyk2 Tyr-402 from Cell Signaling Technology (Danvers, MA); vinculin (7F9) or talin (TA205) from EMD Millipore; or β-actin (AC-15, Sigma Aldrich).

Techniques: Transduction, Fluorescence, Microscopy, Clone Assay, Flow Cytometry, Staining, Expressing, Infection, Western Blot