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pfak  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pfak
    Pfak, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 343 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pfak+tyr925/Phospho-FAK+(Tyr925)+Antibody/pmc12432516__BNEO_NEO-2024-000479-mmc1-35-9-12
    Average 95 stars, based on 343 article reviews
    pfak - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Incubation:

    Article Title: Senescent immune cells release grancalcin to promote skeletal aging.
    Article Snippet: For Western blot analysis, total cell lysates were separated by SDS-PAGE and blotted on polyvinylidene difluoride membranes (Millipore). .. The membranes were incubated with specific antibodies to GCA(PA5-77127, 1:1000, Invitrogen), Plxnb2 (PA5-47880, 1:1000, Invitrogen), FAK (3285T, 1:1000, Cell Signaling Technology), pFAK-Tyr397 (8556T, 1:1000, Cell Signaling Technology), pFAK-Tyr576/ 577 (3281T, 1:1000, Cell Signaling Technology), pFAK-Tyr925 (3284T, 1:1000, Cell Signaling Technology), Runx2 (Abcam, 1:200, ab23981), SRC (2109T, 1:1000, Cell Signaling Technology), pSRC-Tyr416 (2101S, 1:1000, Cell Signaling Technology), YAP (14074S, 1:1000, Cell Signaling Technology), pYAP-Ser127 (13008S, 1:1000, Cell Signaling Technology), TAZ (4883, 1:1000, Cell Signaling Technology), pTAZ-Ser89 (59971S, 1:1000, Cell Signaling Technology), and GAPDH (5174, 1:2000, Cell Signaling Technology), then reprobed with appropriate horseradish peroxidase-conjugated secondary antibodies. .. Blots were visualized by enhanced chemiluminescence (ECL Kit; Amersham Biosciences).

    Article Title: Grancalcin in Immune Cells is Induced and Regulates Bone-Fat Imbalance During Skeletal Aging
    Article Snippet: 3 Chang-Jun Li1, 2, 3, , Ye Xiao1 , Yu-Chen Sun1, Tian Su1 , Qi Guo1, Yan Huang1, Mi Yang1, Xiang4 Hang Luo1,2, 3 * 5 6 1 Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South 7 University, Changsha, Hunan, 410008, China.. 8 2 National Clinical Research Center for Geriatric Disorders, Xiangya Hospital, Changsha, Hunan 9 410008, China.. 10 3 Key Laboratory of Organ Injury, Aging and Regenerative Medicine of Hunan Province, Hunan, 11 410008, China.

    Western Blot:

    Article Title: Src Kinase is a Novel Therapeutic Target in Lymphangio-leiomyomatosis
    Article Snippet: .. Reagents and antibodies The following antibodies were used for immunoblot analysis: pSrc(Tyr416), pStat3(Tyr705), Stat3, pErk1/2(Thr202/Tyr204), Erk1/2, S6, pS6(Ser235/236), pFAK(Tyr925), pFAK(Tyr397), mTOR, U0126 (all from Cell Signaling), tuberin, rabbit E-cadherin, MMP9, Snail (all from Santa Cruz), mouse E-cadherin (BD), Src (Millipore), pSrc(Tyr418) (LifeSpan Biosciences) and HMB45 (Enzo Life Sciences). .. Src kinase inhibitors PP2 and SU6656 were purchased from Calbiochem.



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    MPO inhibits prostate cancer metastasis. (A) The cell number of LNCaP cells was counted at different time points. (B, C) Cell cycle analysis through PI staining was detected by FACS (B) , and the cell cycle distribution was presented (C) . (D, E) LNCaP cells were analyzed for cell migration and invasion. Representative images of crystal violet-stained migrated (D) or invaded (E) cells are presented (scale bar, 100 μL). (F) The <t>Tyr925-phosphorylated</t> level of FAK and total FAK, E-Cadherin, and Snail in LNCaP cells were detected by Western blot analysis. Actin was used as a loading control. All data are presented as the mean ± SD of three independent experiments; ns, not significant.
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    Growth of GBM cells in fibrin clot and plasma clot depends on integrins β1 and β3. A, Integrins β1, β3, β5, and αV as well as total and activated FAK at Y397 and <t>Y925</t> were analyzed in subconfluent extracts from U87MG, U373MG, and U343MG GBM cells by immunoblotting. α-tubulin served as a loading control. B, Western blot analysis of integrin β1 and integrin β3 expression and total FAK and FAK activation at Y925 in extracts from U87MG and U373MG cells 3 days after transfection with siRNA against integrins β1 (siβ1) and β3 (siβ3) compared with treatment with control siRNA (siCtrl; B , top). FAK expression after transfection with siRNA against FAK (siFAK) compared with siCtrl ( B , bottom). C–F, Fold increase in cell proliferation was analyzed over time in fibrin clot–embedded ( C ) and plasma clot–embedded ( D ) U87MG cells and in fibrin clot–embedded ( E ) and plasma clot–embedded ( F ) U373MG cells following transfection with siβ1, siβ3, and siRNA against FAK compared with siCtrl by phase-contrast microscopy. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001 compared with siCtrl.
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    Growth of GBM cells in fibrin clot and plasma clot depends on integrins β1 and β3. A, Integrins β1, β3, β5, and αV as well as total and activated FAK at Y397 and <t>Y925</t> were analyzed in subconfluent extracts from U87MG, U373MG, and U343MG GBM cells by immunoblotting. α-tubulin served as a loading control. B, Western blot analysis of integrin β1 and integrin β3 expression and total FAK and FAK activation at Y925 in extracts from U87MG and U373MG cells 3 days after transfection with siRNA against integrins β1 (siβ1) and β3 (siβ3) compared with treatment with control siRNA (siCtrl; B , top). FAK expression after transfection with siRNA against FAK (siFAK) compared with siCtrl ( B , bottom). C–F, Fold increase in cell proliferation was analyzed over time in fibrin clot–embedded ( C ) and plasma clot–embedded ( D ) U87MG cells and in fibrin clot–embedded ( E ) and plasma clot–embedded ( F ) U373MG cells following transfection with siβ1, siβ3, and siRNA against FAK compared with siCtrl by phase-contrast microscopy. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001 compared with siCtrl.
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    Image Search Results


    MPO inhibits prostate cancer metastasis. (A) The cell number of LNCaP cells was counted at different time points. (B, C) Cell cycle analysis through PI staining was detected by FACS (B) , and the cell cycle distribution was presented (C) . (D, E) LNCaP cells were analyzed for cell migration and invasion. Representative images of crystal violet-stained migrated (D) or invaded (E) cells are presented (scale bar, 100 μL). (F) The Tyr925-phosphorylated level of FAK and total FAK, E-Cadherin, and Snail in LNCaP cells were detected by Western blot analysis. Actin was used as a loading control. All data are presented as the mean ± SD of three independent experiments; ns, not significant.

    Journal: Frontiers in Genetics

    Article Title: Exploring the prognostic significance of lactate-mitochondria-related genes in prostate cancer

    doi: 10.3389/fgene.2024.1515045

    Figure Lengend Snippet: MPO inhibits prostate cancer metastasis. (A) The cell number of LNCaP cells was counted at different time points. (B, C) Cell cycle analysis through PI staining was detected by FACS (B) , and the cell cycle distribution was presented (C) . (D, E) LNCaP cells were analyzed for cell migration and invasion. Representative images of crystal violet-stained migrated (D) or invaded (E) cells are presented (scale bar, 100 μL). (F) The Tyr925-phosphorylated level of FAK and total FAK, E-Cadherin, and Snail in LNCaP cells were detected by Western blot analysis. Actin was used as a loading control. All data are presented as the mean ± SD of three independent experiments; ns, not significant.

    Article Snippet: Anti- FAK (Cat# 3285), anti-pFAK Tyr925 (Cat# 3284), anti-Snail (Cat# 3879), anti-E-Cadherin (Cat# 3195) and anti-actin (Cat# 4970) antibodies were purchased from Cell Signaling Technology.

    Techniques: Cell Cycle Assay, Staining, Migration, Western Blot, Control

    Growth of GBM cells in fibrin clot and plasma clot depends on integrins β1 and β3. A, Integrins β1, β3, β5, and αV as well as total and activated FAK at Y397 and Y925 were analyzed in subconfluent extracts from U87MG, U373MG, and U343MG GBM cells by immunoblotting. α-tubulin served as a loading control. B, Western blot analysis of integrin β1 and integrin β3 expression and total FAK and FAK activation at Y925 in extracts from U87MG and U373MG cells 3 days after transfection with siRNA against integrins β1 (siβ1) and β3 (siβ3) compared with treatment with control siRNA (siCtrl; B , top). FAK expression after transfection with siRNA against FAK (siFAK) compared with siCtrl ( B , bottom). C–F, Fold increase in cell proliferation was analyzed over time in fibrin clot–embedded ( C ) and plasma clot–embedded ( D ) U87MG cells and in fibrin clot–embedded ( E ) and plasma clot–embedded ( F ) U373MG cells following transfection with siβ1, siβ3, and siRNA against FAK compared with siCtrl by phase-contrast microscopy. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001 compared with siCtrl.

    Journal: Cancer Research Communications

    Article Title: Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase

    doi: 10.1158/2767-9764.CRC-24-0164

    Figure Lengend Snippet: Growth of GBM cells in fibrin clot and plasma clot depends on integrins β1 and β3. A, Integrins β1, β3, β5, and αV as well as total and activated FAK at Y397 and Y925 were analyzed in subconfluent extracts from U87MG, U373MG, and U343MG GBM cells by immunoblotting. α-tubulin served as a loading control. B, Western blot analysis of integrin β1 and integrin β3 expression and total FAK and FAK activation at Y925 in extracts from U87MG and U373MG cells 3 days after transfection with siRNA against integrins β1 (siβ1) and β3 (siβ3) compared with treatment with control siRNA (siCtrl; B , top). FAK expression after transfection with siRNA against FAK (siFAK) compared with siCtrl ( B , bottom). C–F, Fold increase in cell proliferation was analyzed over time in fibrin clot–embedded ( C ) and plasma clot–embedded ( D ) U87MG cells and in fibrin clot–embedded ( E ) and plasma clot–embedded ( F ) U373MG cells following transfection with siβ1, siβ3, and siRNA against FAK compared with siCtrl by phase-contrast microscopy. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001 compared with siCtrl.

    Article Snippet: The membrane was blocked with 5% non-fat dry milk or 5% BSA in PBS containing 0.1% Tween 20 for 1 hour at room temperature and probed for anti-integrin β1 (Cell Signaling Technology, catalog # 9699, RRID: AB_11178800), anti-integrin β3 (BD Biosciences, catalog # 611140, RRID: AB_398451), anti-integrin β5 (Cell Signaling Technology, catalog # 3629, RRID: AB_2249358), anti-integrin αV (BD Biosciences, catalog # 611012, RRID: AB_398325), anti-FAK (Cell Signaling Technology, catalog # 3285, RRID: AB_2269034), anti-pFAK Y397 (Thermo Fisher Scientific, catalog # 700255, RRID: AB_2532307), anti-pFAK Y925 (Cell Signaling Technology, catalog # 3284, RRID: AB_10831810), or α-tubulin (Sigma-Aldrich, catalog # T-6199, RRID: AB_477583) overnight at 4°C.

    Techniques: Clinical Proteomics, Western Blot, Control, Expressing, Activation Assay, Transfection, Microscopy