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primary antibodies against srf  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology primary antibodies against srf
    Serum response factor promotes OSCC cell epithelial-to-mesenchymal transition. Serum-starved OSCC cells (SAS and HSC3) were transfected with <t>pCGN-SRF</t> or Ctrl vectors. At 72 h post-transfection, the protein levels <t>of</t> <t>E-cadherin</t> and N-cadherin were detected via western blotting. GAPDH served as a protein loading control ( A ). Original western blots are shown in . The relative band intensity was determined through densitometric analysis ( B ). Data are presented as the mean ± SD of three independent experiments. ** p < 0.01 vs. control vector. ( C ) Immunofluorescence staining of E-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or Ctrl vectors. ( D ) Immunofluorescence staining of N-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or control (Ctrl) vector. Scale bar: 50μm. Data are representative of three independent experiments. Ctrl, control; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma.
    Primary Antibodies Against Srf, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 522 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary antibodies against srf/product/Santa Cruz Biotechnology
    Average 95 stars, based on 522 article reviews
    primary antibodies against srf - by Bioz Stars, 2026-03
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    Images

    1) Product Images from "Serum Response Factor-Regulated IDO1/Kyn-Ahr Pathway Promotes Tumorigenesis of Oral Squamous Cell Carcinoma"

    Article Title: Serum Response Factor-Regulated IDO1/Kyn-Ahr Pathway Promotes Tumorigenesis of Oral Squamous Cell Carcinoma

    Journal: Cancers

    doi: 10.3390/cancers15041319

    Serum response factor promotes OSCC cell epithelial-to-mesenchymal transition. Serum-starved OSCC cells (SAS and HSC3) were transfected with pCGN-SRF or Ctrl vectors. At 72 h post-transfection, the protein levels of E-cadherin and N-cadherin were detected via western blotting. GAPDH served as a protein loading control ( A ). Original western blots are shown in . The relative band intensity was determined through densitometric analysis ( B ). Data are presented as the mean ± SD of three independent experiments. ** p < 0.01 vs. control vector. ( C ) Immunofluorescence staining of E-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or Ctrl vectors. ( D ) Immunofluorescence staining of N-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or control (Ctrl) vector. Scale bar: 50μm. Data are representative of three independent experiments. Ctrl, control; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma.
    Figure Legend Snippet: Serum response factor promotes OSCC cell epithelial-to-mesenchymal transition. Serum-starved OSCC cells (SAS and HSC3) were transfected with pCGN-SRF or Ctrl vectors. At 72 h post-transfection, the protein levels of E-cadherin and N-cadherin were detected via western blotting. GAPDH served as a protein loading control ( A ). Original western blots are shown in . The relative band intensity was determined through densitometric analysis ( B ). Data are presented as the mean ± SD of three independent experiments. ** p < 0.01 vs. control vector. ( C ) Immunofluorescence staining of E-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or Ctrl vectors. ( D ) Immunofluorescence staining of N-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or control (Ctrl) vector. Scale bar: 50μm. Data are representative of three independent experiments. Ctrl, control; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma.

    Techniques Used: Transfection, Western Blot, Control, Plasmid Preparation, Immunofluorescence, Staining

    SRF overexpression promotes OSCC tumorigenesis in vivo. Xenografted nude mice ( n = 6/group) were injected with HSC3 cells stably overexpressing SRF. The mice were euthanized, and tumors were excised from nude mice 40 days after HSC-3 cell injection ( A ). Tumor volumes were measured using calipers ( B ), and tumors were weighed at the end of the experiment ( C ). Statistical data were derived from three independent measurements and are shown as means ± SDs. Infiltration of HSC-3-SRF tumor cells ( D ). Representative immunohistochemical images of E-cadherin and N-cadherin expression in samples from HSC-3-NC and HSC-3-SRF cells ( E ). The scale bar is shown in lower-right corner. Mean optical density of E-cadherin and N-cadherin in tumor samples from HSC-3-NC and HSC-3-SRF cells ( F ). * p < 0.05, ** p < 0.01, *** p < 0.001, tumor samples from HSC-3-NC cells compared with HSC-3-SRF cells. NC, negative control; OSCC, oral squamous cell carcinoma; SRF, serum response factor.
    Figure Legend Snippet: SRF overexpression promotes OSCC tumorigenesis in vivo. Xenografted nude mice ( n = 6/group) were injected with HSC3 cells stably overexpressing SRF. The mice were euthanized, and tumors were excised from nude mice 40 days after HSC-3 cell injection ( A ). Tumor volumes were measured using calipers ( B ), and tumors were weighed at the end of the experiment ( C ). Statistical data were derived from three independent measurements and are shown as means ± SDs. Infiltration of HSC-3-SRF tumor cells ( D ). Representative immunohistochemical images of E-cadherin and N-cadherin expression in samples from HSC-3-NC and HSC-3-SRF cells ( E ). The scale bar is shown in lower-right corner. Mean optical density of E-cadherin and N-cadherin in tumor samples from HSC-3-NC and HSC-3-SRF cells ( F ). * p < 0.05, ** p < 0.01, *** p < 0.001, tumor samples from HSC-3-NC cells compared with HSC-3-SRF cells. NC, negative control; OSCC, oral squamous cell carcinoma; SRF, serum response factor.

    Techniques Used: Over Expression, In Vivo, Injection, Stable Transfection, Derivative Assay, Immunohistochemical staining, Expressing, Negative Control

    SRF facilitates the migration and invasion of OSCC by upregulating IDO1 transcription. ( A ) Migration and invasion assays on SAS and HSC-3 cells incubated with the IDO1 inhibitor PC. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PC. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PC. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; IDO1, indoleamine 2,3-dioxygenase 1; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PC, palmatine chloride; SRF, serum response factor.
    Figure Legend Snippet: SRF facilitates the migration and invasion of OSCC by upregulating IDO1 transcription. ( A ) Migration and invasion assays on SAS and HSC-3 cells incubated with the IDO1 inhibitor PC. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PC. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PC. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; IDO1, indoleamine 2,3-dioxygenase 1; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PC, palmatine chloride; SRF, serum response factor.

    Techniques Used: Migration, Incubation, Immunofluorescence, Staining, Western Blot

    AhR is involved in the function of SRF in carcinogenesis. ( A ) Migration and invasion assays on SAS and HSC-3 cells after adding the AhR inhibitor PDM2. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PDM2. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PDM2. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PDM2, AhR inhibitor; SRF, serum response factor.
    Figure Legend Snippet: AhR is involved in the function of SRF in carcinogenesis. ( A ) Migration and invasion assays on SAS and HSC-3 cells after adding the AhR inhibitor PDM2. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PDM2. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PDM2. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PDM2, AhR inhibitor; SRF, serum response factor.

    Techniques Used: Migration, Immunofluorescence, Staining, Western Blot



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    Average 90 stars, based on 1 article reviews
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    Image Search Results


    Serum response factor promotes OSCC cell epithelial-to-mesenchymal transition. Serum-starved OSCC cells (SAS and HSC3) were transfected with pCGN-SRF or Ctrl vectors. At 72 h post-transfection, the protein levels of E-cadherin and N-cadherin were detected via western blotting. GAPDH served as a protein loading control ( A ). Original western blots are shown in . The relative band intensity was determined through densitometric analysis ( B ). Data are presented as the mean ± SD of three independent experiments. ** p < 0.01 vs. control vector. ( C ) Immunofluorescence staining of E-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or Ctrl vectors. ( D ) Immunofluorescence staining of N-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or control (Ctrl) vector. Scale bar: 50μm. Data are representative of three independent experiments. Ctrl, control; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma.

    Journal: Cancers

    Article Title: Serum Response Factor-Regulated IDO1/Kyn-Ahr Pathway Promotes Tumorigenesis of Oral Squamous Cell Carcinoma

    doi: 10.3390/cancers15041319

    Figure Lengend Snippet: Serum response factor promotes OSCC cell epithelial-to-mesenchymal transition. Serum-starved OSCC cells (SAS and HSC3) were transfected with pCGN-SRF or Ctrl vectors. At 72 h post-transfection, the protein levels of E-cadherin and N-cadherin were detected via western blotting. GAPDH served as a protein loading control ( A ). Original western blots are shown in . The relative band intensity was determined through densitometric analysis ( B ). Data are presented as the mean ± SD of three independent experiments. ** p < 0.01 vs. control vector. ( C ) Immunofluorescence staining of E-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or Ctrl vectors. ( D ) Immunofluorescence staining of N-cadherin in SAS and HSC3 cells transfected with pCGN-SRF or control (Ctrl) vector. Scale bar: 50μm. Data are representative of three independent experiments. Ctrl, control; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma.

    Article Snippet: Primary antibodies against SRF (sc-335, Santa Cruz Biotechnology, Dallas, TX, USA), E-cadherin (ab76055; Abcam, Cambridge, UK), and N-cadherin (13769-1-AP, Proteintech, Wuhan, Hubei, China) were applied.

    Techniques: Transfection, Western Blot, Control, Plasmid Preparation, Immunofluorescence, Staining

    SRF overexpression promotes OSCC tumorigenesis in vivo. Xenografted nude mice ( n = 6/group) were injected with HSC3 cells stably overexpressing SRF. The mice were euthanized, and tumors were excised from nude mice 40 days after HSC-3 cell injection ( A ). Tumor volumes were measured using calipers ( B ), and tumors were weighed at the end of the experiment ( C ). Statistical data were derived from three independent measurements and are shown as means ± SDs. Infiltration of HSC-3-SRF tumor cells ( D ). Representative immunohistochemical images of E-cadherin and N-cadherin expression in samples from HSC-3-NC and HSC-3-SRF cells ( E ). The scale bar is shown in lower-right corner. Mean optical density of E-cadherin and N-cadherin in tumor samples from HSC-3-NC and HSC-3-SRF cells ( F ). * p < 0.05, ** p < 0.01, *** p < 0.001, tumor samples from HSC-3-NC cells compared with HSC-3-SRF cells. NC, negative control; OSCC, oral squamous cell carcinoma; SRF, serum response factor.

    Journal: Cancers

    Article Title: Serum Response Factor-Regulated IDO1/Kyn-Ahr Pathway Promotes Tumorigenesis of Oral Squamous Cell Carcinoma

    doi: 10.3390/cancers15041319

    Figure Lengend Snippet: SRF overexpression promotes OSCC tumorigenesis in vivo. Xenografted nude mice ( n = 6/group) were injected with HSC3 cells stably overexpressing SRF. The mice were euthanized, and tumors were excised from nude mice 40 days after HSC-3 cell injection ( A ). Tumor volumes were measured using calipers ( B ), and tumors were weighed at the end of the experiment ( C ). Statistical data were derived from three independent measurements and are shown as means ± SDs. Infiltration of HSC-3-SRF tumor cells ( D ). Representative immunohistochemical images of E-cadherin and N-cadherin expression in samples from HSC-3-NC and HSC-3-SRF cells ( E ). The scale bar is shown in lower-right corner. Mean optical density of E-cadherin and N-cadherin in tumor samples from HSC-3-NC and HSC-3-SRF cells ( F ). * p < 0.05, ** p < 0.01, *** p < 0.001, tumor samples from HSC-3-NC cells compared with HSC-3-SRF cells. NC, negative control; OSCC, oral squamous cell carcinoma; SRF, serum response factor.

    Article Snippet: Primary antibodies against SRF (sc-335, Santa Cruz Biotechnology, Dallas, TX, USA), E-cadherin (ab76055; Abcam, Cambridge, UK), and N-cadherin (13769-1-AP, Proteintech, Wuhan, Hubei, China) were applied.

    Techniques: Over Expression, In Vivo, Injection, Stable Transfection, Derivative Assay, Immunohistochemical staining, Expressing, Negative Control

    SRF facilitates the migration and invasion of OSCC by upregulating IDO1 transcription. ( A ) Migration and invasion assays on SAS and HSC-3 cells incubated with the IDO1 inhibitor PC. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PC. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PC. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; IDO1, indoleamine 2,3-dioxygenase 1; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PC, palmatine chloride; SRF, serum response factor.

    Journal: Cancers

    Article Title: Serum Response Factor-Regulated IDO1/Kyn-Ahr Pathway Promotes Tumorigenesis of Oral Squamous Cell Carcinoma

    doi: 10.3390/cancers15041319

    Figure Lengend Snippet: SRF facilitates the migration and invasion of OSCC by upregulating IDO1 transcription. ( A ) Migration and invasion assays on SAS and HSC-3 cells incubated with the IDO1 inhibitor PC. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PC. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PC. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; IDO1, indoleamine 2,3-dioxygenase 1; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PC, palmatine chloride; SRF, serum response factor.

    Article Snippet: Primary antibodies against SRF (sc-335, Santa Cruz Biotechnology, Dallas, TX, USA), E-cadherin (ab76055; Abcam, Cambridge, UK), and N-cadherin (13769-1-AP, Proteintech, Wuhan, Hubei, China) were applied.

    Techniques: Migration, Incubation, Immunofluorescence, Staining, Western Blot

    AhR is involved in the function of SRF in carcinogenesis. ( A ) Migration and invasion assays on SAS and HSC-3 cells after adding the AhR inhibitor PDM2. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PDM2. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PDM2. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PDM2, AhR inhibitor; SRF, serum response factor.

    Journal: Cancers

    Article Title: Serum Response Factor-Regulated IDO1/Kyn-Ahr Pathway Promotes Tumorigenesis of Oral Squamous Cell Carcinoma

    doi: 10.3390/cancers15041319

    Figure Lengend Snippet: AhR is involved in the function of SRF in carcinogenesis. ( A ) Migration and invasion assays on SAS and HSC-3 cells after adding the AhR inhibitor PDM2. Immunofluorescence staining of AhR ( B ), E-cadherin ( C ), and N-cadherin ( D ) in SAS and HSC-3 cells after adding PDM2. The scale bar is shown in lower-right corner. ( E ) Western blotting results of AhR, E-cadherin, and N-cadherin in SAS and HSC-3 cells after adding PDM2. Original western blots are shown in . AhR, aryl hydrocarbon receptor; E-cad, E-cadherin; N-cad, N-cadherin; OSCC, oral squamous cell carcinoma; PDM2, AhR inhibitor; SRF, serum response factor.

    Article Snippet: Primary antibodies against SRF (sc-335, Santa Cruz Biotechnology, Dallas, TX, USA), E-cadherin (ab76055; Abcam, Cambridge, UK), and N-cadherin (13769-1-AP, Proteintech, Wuhan, Hubei, China) were applied.

    Techniques: Migration, Immunofluorescence, Staining, Western Blot