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total src  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc total src
    Total Src, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 227 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+total+src/Src+Mouse+mAb/pmc12925544-188-7-23
    Average 95 stars, based on 227 article reviews
    total src - by Bioz Stars, 2026-09
    95/100 stars

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    other:

    Article Title: Dietary palmitate cooperates with Src kinase to promote prostate tumor progression
    Article Snippet: Antibodies against total Src, phospho-Src(Y416), FAK, pFAK(Y925), GAPDH, and Caveolin-1 were purchased from Cell Signaling Technology (Beverly, MA).

    Membrane:

    Article Title: Pericytes Modulate Third-Generation Tyrosine Kinase Inhibitor Sensitivity in EGFR-Mutated Lung Cancer Cells Through IL32-β5-Integrin Paracrine Signaling.
    Article Snippet: .. Subsequently, the membrane was probed with the following primary antibodies (diluted 1:1000) overnight at 4 °C: anti-IL32 (Abcam-#ab37158), anti-β5-integrin (Cell Signaling Technology-#3629S), anti-p-Src (Cell Signaling Technology-#2101S), anti-total Src (Cell Signaling Technology-#2109S), anti-total Akt (Cell Signaling Technology#4691S), anti-p-Akt (Cell Signaling Technology-#4060S), anti-YY1 antibodies (Cell Signaling Technology-#46395), anti-total ERK (Cell Signaling Technology-#9102S), anti-p-ERK (Cell Signaling Technology-#4370S), anti-HSC70 (Santa Cruz-#sc-7298) and β-actin (Santa Cruz-#sc-47778) Adv. ..

    Article Title: Pericytes Modulate Third‐Generation Tyrosine Kinase Inhibitor Sensitivity in EGFR‐Mutated Lung Cancer Cells Through IL32‐β5‐Integrin Paracrine Signaling
    Article Snippet: .. Subsequently, the membrane was probed with the following primary antibodies (diluted 1:1000) overnight at 4 °C: anti‐IL32 (Abcam‐#ab37158), anti‐β5‐integrin (Cell Signaling Technology‐#3629S), anti‐p‐Src (Cell Signaling Technology‐#2101S), anti‐total Src (Cell Signaling Technology‐#2109S), anti‐total Akt (Cell Signaling Technology‐#4691S), anti‐p‐Akt (Cell Signaling Technology‐#4060S), anti‐YY1 antibodies (Cell Signaling Technology‐#46395), anti‐total ERK (Cell Signaling Technology‐#9102S), anti‐p‐ERK (Cell Signaling Technology‐#4370S), anti‐HSC70 (Santa Cruz‐#sc‐7298) and β‐actin (Santa Cruz‐#sc‐47778) (used as a loading control). .. After washing with TBST, the membrane was incubated with horseradish peroxidase‐conjugated anti‐rabbit secondary antibodies (Cell Signaling Technology‐#7074) for 1 h at room temperature, followed by three washes with TBST.

    Staining:

    Article Title: Sialyl Lewis X/A and Cytokeratin Crosstalk in Triple Negative Breast Cancer
    Article Snippet: To analyse the expression of intracellular markers by flow cytometry, cells were first permeabilised using Fixation/Permeabilization Solution Kit (BD Biosciences, Franklin Lakes, NJ, USA). .. Cells were stained with 1:1000 dilution of anti-phosphorylated (p)-Src (Tyr416), anti-total Src, anti-p-AKT (Ser473), anti-AKT1/2, anti-p-Erk1/2, anti- Erk1/2, anti-p-p38 MAPK and p38 MAPK mAbs, all from Cell Signalling Technology at 4 °C for 30 min. For cell surface α6 integrin staining, the anti-CD49f antibody was used (BD Biosciences, Franklin Lakes, NJ, USA). .. A FITC-conjugated anti-mouse IgG (Dako, Santa Clara, CA, USA) was used for secondary detection at 4 °C for 20 min.

    Article Title: Sialyl Lewis X/A and Cytokeratin Crosstalk in Triple Negative Breast Cancer.
    Article Snippet: To analyse the expression of intracellular markers by flow cytometry, cells were first permeabilised using Fixation/Permeabilization Solution Kit (BD Biosciences, Franklin Lakes, NJ, USA). .. Cells were stained with 1:1000 dilution of anti-phosphorylated (p)-Src (Tyr416), anti-total Src, anti-p-AKT (Ser473), anti-AKT1/2, anti-p-Erk1/2, anti- Erk1/2, anti-p-p38 MAPK and p38 MAPK mAbs, all from Cell Signalling Technology at 4 ◦C for 30 min. For cell surface α6 integrin staining, the anti-CD49f antibody was used (BD Biosciences, Franklin Lakes, NJ, USA). .. A FITC-conjugated anti-mouse IgG (Dako, Santa Clara, CA, USA) was used for secondary detection at 4 ◦C for 20 min.

    Control:

    Article Title: Pericytes Modulate Third‐Generation Tyrosine Kinase Inhibitor Sensitivity in EGFR‐Mutated Lung Cancer Cells Through IL32‐β5‐Integrin Paracrine Signaling
    Article Snippet: .. Subsequently, the membrane was probed with the following primary antibodies (diluted 1:1000) overnight at 4 °C: anti‐IL32 (Abcam‐#ab37158), anti‐β5‐integrin (Cell Signaling Technology‐#3629S), anti‐p‐Src (Cell Signaling Technology‐#2101S), anti‐total Src (Cell Signaling Technology‐#2109S), anti‐total Akt (Cell Signaling Technology‐#4691S), anti‐p‐Akt (Cell Signaling Technology‐#4060S), anti‐YY1 antibodies (Cell Signaling Technology‐#46395), anti‐total ERK (Cell Signaling Technology‐#9102S), anti‐p‐ERK (Cell Signaling Technology‐#4370S), anti‐HSC70 (Santa Cruz‐#sc‐7298) and β‐actin (Santa Cruz‐#sc‐47778) (used as a loading control). .. After washing with TBST, the membrane was incubated with horseradish peroxidase‐conjugated anti‐rabbit secondary antibodies (Cell Signaling Technology‐#7074) for 1 h at room temperature, followed by three washes with TBST.



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    FIGURE 6 SARS-CoV-2 Omicron BA.1 induces FAK/Src and ERK signaling after avb3 interaction. HL-mECs were not infected (NI) or infected with Omicron SARS-CoV-2 belonging to BA.1 and only XBB.1.5 sublineages (Omicron BA.1 and Omicron XBB.1.5, respectively) at a MOI of 1 for 1 h at 37°C. After 1 h p.i., cell lysates were analyzed by western blotting with anti-pFAK, anti-pSRC and anti-pERK antibodies (A-C, respectively). Blots are representative of three independent experiments with similar results. Quantification was carried out by densitometric analysis and plotting of the pFAK, pSrc and pERK normalized on GAPDH, <t>tSrc</t> or tERK as indicated in the graph. Values reported are the means ± the SD of three independent experiments. Statistical analysis was performed by one-way ANOVA, and the Bonferroni post-test was used to compare data (*p = 0.05, **p = 0.022, ***p = 0.0008). When indicated HL-mECs were pretreated with a mAb against avb3 integrin (mAb anti- avb3) or HSPGs inhibitors and analyzed for FAK/Src and ERK phosphorylation status (D-F).
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    FIGURE 6 SARS-CoV-2 Omicron BA.1 induces FAK/Src and ERK signaling after avb3 interaction. HL-mECs were not infected (NI) or infected with Omicron SARS-CoV-2 belonging to BA.1 and only XBB.1.5 sublineages (Omicron BA.1 and Omicron XBB.1.5, respectively) at a MOI of 1 for 1 h at 37°C. After 1 h p.i., cell lysates were analyzed by western blotting with anti-pFAK, anti-pSRC and anti-pERK antibodies (A-C, respectively). Blots are representative of three independent experiments with similar results. Quantification was carried out by densitometric analysis and plotting of the pFAK, pSrc and pERK normalized on GAPDH, <t>tSrc</t> or tERK as indicated in the graph. Values reported are the means ± the SD of three independent experiments. Statistical analysis was performed by one-way ANOVA, and the Bonferroni post-test was used to compare data (*p = 0.05, **p = 0.022, ***p = 0.0008). When indicated HL-mECs were pretreated with a mAb against avb3 integrin (mAb anti- avb3) or HSPGs inhibitors and analyzed for FAK/Src and ERK phosphorylation status (D-F).
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    FIGURE 6 SARS-CoV-2 Omicron BA.1 induces FAK/Src and ERK signaling after avb3 interaction. HL-mECs were not infected (NI) or infected with Omicron SARS-CoV-2 belonging to BA.1 and only XBB.1.5 sublineages (Omicron BA.1 and Omicron XBB.1.5, respectively) at a MOI of 1 for 1 h at 37°C. After 1 h p.i., cell lysates were analyzed by western blotting with anti-pFAK, anti-pSRC and anti-pERK antibodies (A-C, respectively). Blots are representative of three independent experiments with similar results. Quantification was carried out by densitometric analysis and plotting of the pFAK, pSrc and pERK normalized on GAPDH, <t>tSrc</t> or tERK as indicated in the graph. Values reported are the means ± the SD of three independent experiments. Statistical analysis was performed by one-way ANOVA, and the Bonferroni post-test was used to compare data (*p = 0.05, **p = 0.022, ***p = 0.0008). When indicated HL-mECs were pretreated with a mAb against avb3 integrin (mAb anti- avb3) or HSPGs inhibitors and analyzed for FAK/Src and ERK phosphorylation status (D-F).
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    Image Search Results


    FIGURE 6 SARS-CoV-2 Omicron BA.1 induces FAK/Src and ERK signaling after avb3 interaction. HL-mECs were not infected (NI) or infected with Omicron SARS-CoV-2 belonging to BA.1 and only XBB.1.5 sublineages (Omicron BA.1 and Omicron XBB.1.5, respectively) at a MOI of 1 for 1 h at 37°C. After 1 h p.i., cell lysates were analyzed by western blotting with anti-pFAK, anti-pSRC and anti-pERK antibodies (A-C, respectively). Blots are representative of three independent experiments with similar results. Quantification was carried out by densitometric analysis and plotting of the pFAK, pSrc and pERK normalized on GAPDH, tSrc or tERK as indicated in the graph. Values reported are the means ± the SD of three independent experiments. Statistical analysis was performed by one-way ANOVA, and the Bonferroni post-test was used to compare data (*p = 0.05, **p = 0.022, ***p = 0.0008). When indicated HL-mECs were pretreated with a mAb against avb3 integrin (mAb anti- avb3) or HSPGs inhibitors and analyzed for FAK/Src and ERK phosphorylation status (D-F).

    Journal: Frontiers in cellular and infection microbiology

    Article Title: Heparan sulfate proteoglycans remodel SARS-CoV-2 spike conformation to allow integrin interaction and infection of endothelial cells.

    doi: 10.3389/fcimb.2025.1552116

    Figure Lengend Snippet: FIGURE 6 SARS-CoV-2 Omicron BA.1 induces FAK/Src and ERK signaling after avb3 interaction. HL-mECs were not infected (NI) or infected with Omicron SARS-CoV-2 belonging to BA.1 and only XBB.1.5 sublineages (Omicron BA.1 and Omicron XBB.1.5, respectively) at a MOI of 1 for 1 h at 37°C. After 1 h p.i., cell lysates were analyzed by western blotting with anti-pFAK, anti-pSRC and anti-pERK antibodies (A-C, respectively). Blots are representative of three independent experiments with similar results. Quantification was carried out by densitometric analysis and plotting of the pFAK, pSrc and pERK normalized on GAPDH, tSrc or tERK as indicated in the graph. Values reported are the means ± the SD of three independent experiments. Statistical analysis was performed by one-way ANOVA, and the Bonferroni post-test was used to compare data (*p = 0.05, **p = 0.022, ***p = 0.0008). When indicated HL-mECs were pretreated with a mAb against avb3 integrin (mAb anti- avb3) or HSPGs inhibitors and analyzed for FAK/Src and ERK phosphorylation status (D-F).

    Article Snippet: The proteins were purified from HEK293 cells with a purity ≥ 90% and run at a higher molecular weight by SDS-PAGE due to glycosylation; anti-phospho-extracellular signal-regulated kinase 1/ 2 (pERK) and anti-total ERK1/2 (tERK) antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA); antiphospho-focal adhesion kinase (pFAK), anti phospho-Src (pSrc), anti-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and anti-total Src (tSrc) were purchased from Cell Signaling Technology (Danvers, MA, USA); recombinant human integrin alphaV beta3 (avb3), sodium chlorate, Heparinase III and heparin sodium salt from porcine intestinal mucosa were purchased from Merck (Darmstadt, Germany).

    Techniques: Infection, Western Blot, Phospho-proteomics