Anti ras

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-Ras is a reagent used in molecular biology research. It is designed to detect and study the Ras protein, which is a small GTPase involved in cellular signaling pathways. The core function of Anti-Ras is to provide a specific and sensitive tool for the identification and analysis of Ras proteins in various experimental settings.

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Lab products found in correlation

Anti β actin, by Merck Group (3 mentions) Anti h2ax s139p, by Cell Signaling Technology (2 mentions) Anti flag, by Merck Group (2 mentions) Anti chk1, by Santa Cruz Biotechnology (1 mentions) Anti h2a, by Cell Signaling Technology (1 mentions) Fitc conjugated anti mouse iga, by BD (1 mentions) Anti rad52, by Santa Cruz Biotechnology (1 mentions) Anti rpa32, by Fortis Life Sciences (1 mentions) Brca1, by Fortis Life Sciences (1 mentions) Anti fanca, by Fortis Life Sciences (1 mentions) Anti rad51, by Santa Cruz Biotechnology (1 mentions) Anti smad2 3, by Cell Signaling Technology (1 mentions) Anti smad2, by Thermo Fisher Scientific (1 mentions) Anti smad4, by Abcam (1 mentions) Mouse monoclonal anti β tubulin, by Merck Group (1 mentions) Anti phospho smad2, by Cell Signaling Technology (1 mentions) Anti blm, by Fortis Life Sciences (1 mentions) Anti ku70, by Santa Cruz Biotechnology (1 mentions) Anti c jun, by Santa Cruz Biotechnology (1 mentions) Anti tubulin, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

Anti-pan-Ras (4 citations) Anti-H-Ras antibody (3 citations) Mouse anti-H-Ras (2 citations) Mouse anti-N-ras (2 citations) Rabbit anti-H-RAS (2 citations)

5 protocols using anti ras

Immunoblotting analysis of DNA repair proteins

Cited 3 times

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Whole cell lysis and immunoblotting were performed as described^{63 (link),68 (link)}. Antibodies against FANCM and FAAP24, and antibody against BRCA2 were kindly provided by Dr. Weidong Wang^{38 (link)} and Dr. Jun Huang^{66 (link)}, respectively. Antibodies against Mre11 and CtIP were used previously^{10 (link),63 (link),69 (link)}. Commercial antibodies used were: Anti-FANCA (Bethyl Laboratories A301-980A,1:1000), anti-FANCD2 (Bethyl Laboratories A302-174A, 1:1000), anti-MHF1 (Abcam, ab169385, 1:1000), anti-Rad51 (Santa Cruz Biotechnology, sc-398587, 1:500), anti-H2AX-S139p (Cell Signaling, #2577, 1:1000), anti-H2A (Cell signaling, #2578, 1:1000), anti-FLAG (Sigma, F1804, 1:2000), anti-Rad52 (Santa Cruz Biotechnology, sc-365341, 1:1000), anti-Ras (Santa Cruz Biotechnology, sc-520, 1:1000), anti-β-actin (Sigma, A5441, 1:2000), anti-Chk1 (Santa Cruz Biotechnology, sc-8408, 1:500), anti-Chk1-S345p (Cell Signaling,#2348, 1:500), anti-RPA32 (Bethyl Laboratories A300-244A, 1:1000), BRCA1 (Bethyl Laboratories, A300–000A, 1:500) and FITC-conjugated anti-mouse IgA (BD, 559354).

Wang H., Li S., Oaks J., Ren J., Li L, & Wu X. (2018). The concerted roles of FANCM and Rad52 in the protection of common fragile sites. Nature Communications, 9, 2791.

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Western Blotting of SMAD and RAS Proteins

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Western blotting was performed as previously described.²⁹ (link) The primary antibodies used were anti-phospho-SMAD2 (Cell Signaling #3101), anti-SMAD2 (Invitrogen #51-1300; Carlsbad, CA), anti-SMAD2/3 (Cell Signaling #3102), anti-SMAD4 (Epitomics #1676-1; Burlingame, CA), anti-RAS (Santa Cruz Biotechnology), anti-β-actin (Sigma-Aldrich #A5441 Clone AC15), and anti-β-tubulin (mouse monoclonal; Sigma-Aldrich). Peroxidase-labeled anti-rabbit and anti-mouse secondary antibodies were purchased from Dako (mouse immunoglobulin G horseradish peroxidase–conjugated DAKO P0260, rabbit immunoglobulin G horseradish peroxidase–conjugated DAKO #P0448).

Chuvin N., Vincent D.F., Pommier R.M., Alcaraz L.B., Gout J., Caligaris C., Yacoub K., Cardot V., Roger E., Kaniewski B., Martel S., Cintas C., Goddard-Léon S., Colombe A., Valantin J., Gadot N., Servoz E., Morton J., Goddard I., Couvelard A., Rebours V., Guillermet J., Sansom O.J., Treilleux I., Valcourt U., Sentis S., Dubus P, & Bartholin L. (2017). Acinar-to-Ductal Metaplasia Induced by Transforming Growth Factor Beta Facilitates KRASG12D-driven Pancreatic Tumorigenesis. Cellular and Molecular Gastroenterology and Hepatology, 4(2), 263-282.

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Western Blot Analysis of DNA Damage Proteins

Cited 1 time

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Western blot analysis was performed as described [60 (link)]. Cells were lysed with NETN buffer (20 mM Tris, pH 8.0, 1 mM EDTA, 150 mM NaCl, and 0.5% Nonidet P-40) for 30 min. Cell lysates were boiled in 2xSDS loading buffer and subjected to SDS-PAGE.
Commercial antibodies used include anti-BLM (Bethyl Laboratories, A300), anti-H2AX-S139p (Cell Signaling, #2577), anti-Ras (Santa Cruz Biotechnology, sc-520), anti-FLAG (Sigma, F1804), anti-Ku70 (Santa Cruz Biotechnology, sc-17789), anti-β-actin (Sigma, A5441). Antibodies against FANCM was kindly provided by Dr. Weidong Wang [57 (link)].

Wang H., Li S., Zhang H., Wang Y., Hao S, & Wu X. (2018). BLM prevents instability of structure-forming DNA sequences at common fragile sites. PLoS Genetics, 14(11), e1007816.

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Antibody source and application

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Antibodies were obtained from Bethyl Laboratories, Montgomery, TX, USA: anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH), anti-DDX21; Cell Signaling, Danvers, MA, USA: anti-p53, anti-cyclin D1, anti-c-jun, anti-phospho-c-jun (S73), anti-phospho-c-jun (S63); and Santa Cruz Biotechnology, Dallas, TX, USA: anti-epithelial growth factor receptor (EGFR), anti-tubulin, anti-Ras.

Zhang Y., Baysac K.C., Yee L.F., Saporita A.J, & Weber J.D. (2014). Elevated DDX21 regulates c-Jun activity and rRNA processing in human breast cancers. Breast Cancer Research : BCR, 16, 449.

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Mitochondrial Dynamics Regulation by Co-IP

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GMC lysates from various groups were used for co-immunoprecipitation as described previously (Koshiba et al. 2004 (link), Zhang et al. 2009) (link). In brief, cell lysates were first cleared with 50% protein A-agarose (Santa Cruz Biotechnology) and were then incubated with rabbit polyclonal antibody against mfn2 protein (Thermo Scientific) for 1 h at 4°C, followed by incubation with protein A-agarose overnight at 4°C. The antigenantibody-protein A-agarose complex pellets were collected through centrifugation and washed with RIPA buffer. The bound proteins were separated using SDS-PAGE and were then transferred to PVDF membranes for Western blot analyses with anti-mfn2 (Thermo Scientific), anti-Ras (Santa Cruz Biotechnology) or non-specific IgG antibodies (Santa Cruz Biotechnology).

Mi X., Tang W., Chen X., Liu F, & Tang X. (2016). Mitofusin 2 attenuates the histone acetylation at collagen IV promoter in diabetic nephropathy. Journal of molecular endocrinology, 57(4).

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