Anti raf 1

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-Raf-1 is a primary antibody that recognizes the Raf-1 protein, also known as c-Raf. Raf-1 is a serine/threonine-protein kinase that plays a crucial role in the Ras-Raf-MEK-ERK signal transduction pathway, which is involved in cell growth, differentiation, and survival. The Anti-Raf-1 antibody can be used to detect and study the Raf-1 protein in various experimental techniques, such as Western blotting, immunoprecipitation, and immunohistochemistry.

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Close spelling variants of this product

Raf-1 (20 citations) Anti-phospho-Raf-1 (3 citations) Anti- p-Raf-1 (2 citations)

8 protocols using anti raf 1

Molecular Mechanisms of VEGF Signaling

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Anti-VEGFR2, anti-PLCγ, anti-HSP90, anti-Raf-1, anti-cyclin D1, anti-CDK4 and anti-p21 antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Anti-VEGFR2, anti-phospho-VEGFR2 (Y1175), anti-phospho-PLCγ (Y783), anti-phospho-Erk (T202/Y204), anti-Erk, antiphospho-Akt (S473) and anti-Akt antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA). Anti-eNOS and anti-phospho-eNOS (S1177) antibodies were purchased from BD Biosciences (San Diego, CA, USA). Anti-α-tubulin antibody was purchased from Sigma-Aldrich. Recombinant human VEGF165 and 4,5-diaminofluorescein diacetate (DAF2-DA) and DAPI (4′,6-diamidino-2-phenylindole dihydrochloride hydrate) were purchased from Sigma-Aldrich. DMAG (17-dimethylaminoethylamino-17-demethoxygeldanamycin) and NOC-18 was purchased from Santa Cruz Biotechnology.

Tae N., Hung T.M., Kim O., Kim N., Lee S., Na S., Min B.S, & Lee J.H. (2017). A cassaine diterpene alkaloid, 3β-acetyl-nor-erythrophlamide, suppresses VEGF-induced angiogenesis and tumor growth via inhibiting eNOS activation. Oncotarget, 8(54), 92346-92358.

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Characterization of Non-Hodgkin's T-cell Lymphoma

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Non-Hodgkin’s T cell human lymphoblastic lymphoma (SUP-T1) were obtained from Biological Materials Bank (ICLC)-CBA-Genoa. ³H palmytic acid, [³H] thymidine and [³H] UTP (41 Ci/mmol, 1.52 TBq/mmol) were obtained from Amersham Pharmacia Biotech (Rainham, Essex, UK); Ecoscint A was obtained from National Diagnostic (Atlanta, GA, USA); Thin layer chromatography (TLC) plates (silica Gel G60) were from Merck, Darmstadt, Germany; CHO, SM, Fetal bovine serum (FBS), RPMI 1640 Medium, PSF (penicillin, streptomycin and fungizone) were purchased from Sigma Aldrich Co. (St. Louis, MO, USA). Anti-actin, anti-Raf1, anti-phosphoRaf1 and anti-E-cadherin antibodies were obtained from Santa Cruz Biotechnology, Inc. (California, USA).

Codini M., Cataldi S., Lazzarini A., Tasegian A., Ceccarini M.R., Floridi A., Lazzarini R., Ambesi-Impiombato F.S., Curcio F., Beccari T, & Albi E. (2016). Why high cholesterol levels help hematological malignancies: role of nuclear lipid microdomains. Lipids in Health and Disease, 15, 4.

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Western Blot Analysis of Protein Markers

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Total protein was extracted from cells using RIPA buffer containing 10% protease inhibitor cocktail (Sigma, St. Louis, MO). Protein concentration was determined using Bradford (Bio-Rad Laboratories, Hercules, CA), and 40 μg of each sample was fractionated by 10–12% SDS-PAGE and blotted onto a nitrocellulose membrane (Hybond-ECL; Amersham Biosciences, Little Chalfont, UK). Non-specific binding sites were blocked with 5% non-fat dry milk in PBS−0.1% Tween-20. The following primary antibodies were used: anti-FAM83F (N17) (sc-102517), anti-p-ERK1/2 (sc-7393), anti-ERK1(sc-94), anti-BRAF (sc-166), anti-RAF-1 (sc-133), anti-Vimentin (sc-32322), anti-TTF-1 (sc-13040), anti PAX-8 (sc-81353), anti-β-actin (sc-47778) (Santa Cruz, Santa Cruz, CA, USA), anti-Myc-tag (TA100010) (OriGene Technologies), and anti-LIN28B (Cell Signaling). The anti-Nis antibody was kindly donated by Dr. Sissy Jhiang.
Immunoexpression was detected with horseradish peroxidase-conjugated secondary antibodies (GeHealthcare) and developed with luminol and p-cumaric acid (Sigma) reagents in the presence of H₂O₂. Chemoluminescence emission was visualized in an ImageQuant LAS4000 imaging system (GE Healthcare, Little Chalfont, UK).

Fuziwara C.S., Saito K.C., Leoni S.G., Waitzberg Â.F, & Kimura E.T. (2019). The Highly Expressed FAM83F Protein in Papillary Thyroid Cancer Exerts a Pro-Oncogenic Role in Thyroid Follicular Cells. Frontiers in Endocrinology, 10, 134.

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Immunofluorescence staining of HDLBP and RAF1

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Immunofluorescence staining was performed as previously described.¹⁹ (link) Anti-HDLBP (Proteintech, 15406-1-AP, 1:100) and Anti-RAF1 (Santa Cruz Biotechnology, sc-7267, Dallas, Tx, 1:50) were used.

Yuan J., Lv T., Yang J., Wu Z., Yan L., Yang J., Shi Y, & Jiang L. (2022). HDLBP Promotes Hepatocellular Carcinoma Proliferation and Sorafenib Resistance by Suppressing Trim71-dependent RAF1 Degradation. Cellular and Molecular Gastroenterology and Hepatology, 15(2), 307-325.

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Immunohistochemical Evaluation of HDLBP and RAF1

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Histology and IHC were performed as previously described.¹⁹ (link)^,³⁴ (link) Anti-HDLBP (Proteintech, 15406-1-AP, 1:100), Anti-RAF1 (Santa Cruz Biotechnology, sc-7267, 1:100), and Anti-Ki67 (Proteintech, 27309-1-AP, 1:2000) were used. The IHC results from human tissues were evaluated by 2 independent observers based on the percentage of positively stained cells (scored from 0–3 points) and intensity of staining (scored from 0–3 points), and a final immunoreactivity score (range 0–9 points) was obtained by multiplying the 2 scores. HDLBP and RAF1 expression levels were classified as low if the score was less than 5 and high if the score was ≥5.

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Immunoprecipitation of FAM83F Complexes

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For immunoprecipitation, PCCL3-FAM83F and Nthy-ori-FAM83F cells were lysed in RIPA buffer containing 10% protease inhibitor cocktail and incubated with agarose-protein A/G beads (Santa Cruz) for pre-clearing. Next, cell lysates were incubated overnight at 4°C under agitation with 20 μL of the complex of agarose-protein A/G beads + 1 μg of one of the following antibodies: anti-Myc tag (OriGene Technologies), anti-BRAF (Santa Cruz), anti-RAF1 (Santa Cruz), or anti-HuR (Invitrogen). After the incubation, beads were pelleted at 1,000 × g at 4°C and washed in RIPA buffer. Beads were resuspended in 1 × Western Blotting loading buffer and denaturated at 95°C for 5 min before loading into 10% SDS-PAGE. Immunodetection was performed as already described in WB section.

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Western Blot Analysis of Lung Cancer

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The Western blot analysis in this investigation was conducted according to the methods described earlier [26 (link),27 ]. RIPA lysis buffer (Santa Cruz) along with Protease and phosphatase inhibitor cocktail (Biotech Roche) were used to lyse cells or clinical samples of lung cancer. In this study, the antibodies used included anti-TCF19 (diluted 1:1000, YT5078, Immunoway), anti-MEK1/2 (diluted 1:500, sc-81,504, Santa Cruz, USA), anti-p-MEK1/2 (diluted 1:500, sc-81,503, Santa Cruz, USA), anti-ERK1/2 (diluted 1:1000, #4695, Cell Signaling Technology), anti-p-ERK1/2 (diluted 1:1000, #4370, Cell Signaling Technology), anti-Raf-1 (diluted 1:500, sc-7267, Santa Cruz, USA), anti-p-Raf-1 (diluted 1:500, sc-271,919, Santa Cruz, USA), anti-FLAG (diluted 1:1000, #14,793, Cell Signaling Technology), CyclinA1 (diluted 1:1000, CY1027, Abways), CyclinD1 (diluted 1:10,000, ab228528, Abcam), CyclinE1 (diluted 1:1000, #20,808, Cell Signaling Technology), CDK2 (diluted 1:10,000, ab228528, Abcam), anti-GAPDH (diluted 1:1000, #5174, Cell Signaling Technology), and anti-β-actin (diluted 1:1000, A5316, Sigma). We bought the anti-rabbit and anti-mouse IgG conjugated with horseradish peroxidase from sigma (A6154, 1 1000; A0168, 1 1000). The results were obtained using Western blotting substrate (Millipore).

Tian Y., Xin S., Wan Z., Dong H., Liu L., Fan Z., Li T., Peng F., Xiong Y, & Han Y. (2024). TCF19 promotes cell proliferation and tumor formation in lung cancer by activating the Raf/MEK/ERK signaling pathway. Translational Oncology, 45, 101978.

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Comprehensive Lipidomic and Proteomic Analysis of CHO Cells

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DMEM, bovine serum albumin (BSA), dithiothreitol (DTT), fetal bovine serum (FBS), phenylmethylsulfonylfluoride (PMSF), methanol, 3-(4,5-dimethyl-thiazol-2-yl)-2,5-diphenyltetrazolium bromide, 2-propanol, metyl-tert-butyl ether, formic acid, chloroform, and CHO were obtained from Sigma-Aldrich (St. Louis, MO); lipid standards 16:0 SM, 18:1 SM, 24:0 SM, 16:0 18:1 PC, 16:0 24:0 PC, 18:1 18:0 PC, 16:0 ceramide, 20:0 ceramide, and 24:0 ceramide were purchased from Avanti (Avanti Polar, Alabaster, AL); anti-giantin, anti-STAT3, anti-Raf1, anti-PKCζ, and anti-VDR were obtained from Santa Cruz Biotechnology (Santa Cruz, CA); anti-lamin B was obtained from Oncogene (Boston, MA)

Lazzarini A., Macchiarulo A., Floridi A., Coletti A., Cataldi S., Codini M., Lazzarini R., Bartoccini E., Cascianelli G., Ambesi-Impiombato F.S., Beccari T., Curcio F, & Albi E. (2015). Very-long-chain fatty acid sphingomyelin in nuclear lipid microdomains of hepatocytes and hepatoma cells: can the exchange from C24:0 to C16:0 affect signal proteins and vitamin D receptor?. Molecular Biology of the Cell, 26(13), 2418-2425.

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