Anti myc mab

Manufactured by Santa Cruz Biotechnology

Sourced in United States

The Anti-Myc mAb is a monoclonal antibody that specifically binds to the Myc protein, which is a transcription factor involved in various cellular processes. This antibody can be used for the detection and analysis of Myc-tagged proteins in various applications, such as Western blotting, immunoprecipitation, and immunohistochemistry.

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Lab products found in correlation

Anti flag mab, by Genomics Plc (2 mentions) Anti actin pab, by Merck Group (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (2 mentions) Formaldehyde, by Merck Group (1 mentions) X tremegene, by Merck Group (1 mentions) Nucblue reagent, by Thermo Fisher Scientific (1 mentions) Axiovision software, by Zeiss (1 mentions) Axiovision version 4, by Zeiss (1 mentions) X tremegene transfection reagent, by Roche (1 mentions)

5 protocols using anti myc mab

Stat5a Dimerization Assay Protocol

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The dimer formation of Stat5a was analyzed as described previously (4 (link)) and in the Supplementary Methods. Cells were serum-starved for 16 h, followed by pre-treatment with IST5-002 or the control compound (Ctrl) for 2 h at indicated concentrations, and stimulated with hPrl (10 nM) in serum-free medium for 30 min. Whole cell lysates were immunoprecipitated with anti-Myc mAb (2 μg/sample; Santa Cruz Biotechnology) and immunoblotted with anti-Flag mAb (1:1000; Genomics), anti-Myc mAb (1:1000; Santa Cruz Biotechnology) and anti-actin pAb (1:4000, Sigma-Aldrich).

Liao Z., Gu L., Vergalli J., Mariani S.A., De Dominici M., Lokareddy R.K., Dagvadorj A., Purushottamachar P., McCue P.A., Trabulsi E., Lallas C.D., Gupta S., Ellsworth E., Blackmon S., Ertel A., Fortina P., Leiby B., Xia G., Rui H., Hoang D.T., Gomella L.G., Cingolani G., Njar V., Pattabiraman N., Calabretta B, & Nevalainen M.T. (2015). Structure-based screen identifies a potent small-molecule inhibitor of Stat5a/b with therapeutic potential for prostate cancer and chronic myeloid leukemia. Molecular cancer therapeutics, 14(8), 1777-1793.

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Stat5 Dimerization Assay with FLAG-Stat5a and MYC-Stat5a

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FLAG-tagged Stat5a and MYC-tagged Stat5a constructs were generated for the analysis of Stat5 dimer formation. Full-length Stat5a was amplified by PCR and subcloned to pCMV-3FLAG and pCMV-3MYC vectors (Genomics, Santa Clara, CA, USA) with EcoR1 and SalI sites, and both constructs were sequenced. PC-3 cells were serum-starved for 16 h, followed by pretreatment with IST5, IST5-M or vehicle (DMSO) for 2 h at indicated concentrations, and stimulated with Prl (10 nM) in serum-free medium for 30 min. Whole-cell lysates were immunoprecipitated with anti-MYC mAb (2 μg/sample; Santa Cruz Biotechnology, Dallas, TX, USA) and immunoblotted with anti-FLAG mAb (1:1000; Genomics), anti-MYC mAb (1:1000; Santa Cruz Biotechnology, Dallas, TX, USA), and anti-actin pAb (1:4000; Sigma-Aldrich, St. Louis, MO, USA).

Maranto C., Udhane V., Jia J., Verma R., Müller-Newen G., LaViolette P.S., Pereckas M., Sabharwal L., Terhune S., Pattabiraman N., Njar V.C., Imig J.D., Wang L, & Nevalainen M.T. (2020). Prospects for Clinical Development of Stat5 Inhibitor IST5-002: High Transcriptomic Specificity in Prostate Cancer and Low Toxicity In Vivo. Cancers, 12(11), 3412.

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Detecting Tsg101 Colocalization in Transfected HeLa Cells

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Cells were prepared and analyzed as previously described (Strickland et al., 2017 (link)). HeLa cells were transfected (Sigma, X-treme GENE) with pCMV-Gag-EGFP with pLLEXP1-hTsg101-Myc. Cells were fixed in 4% formaldehyde (Sigma) and permeabilized in 0.1% Triton X-100. Tsg101 was detected in the samples by indirect immunofluorescence using anti-Myc Mab (Santa Cruz Biotechnology, 9E10) and Texas Red anti-mouse IgG (Molecular Probes). Nuclei were stained with DAPI (Thermo Scientific). Cells were fixed with anti-fade mountant (Molecular Probes). Images were captured on an inverted fluorescence/differential-interference contrast (dic) Zeiss Axiovert 200M deconvolving fluorescence microscope operated by Zeiss AxioVision Version 4.5 software and deconvolved by using the constrained iterative method. Protein co-localization was assessed in the entire co-transfected cell with Pearson’s coefficient of correlation using NIH Image J, JACoP plugin software (Bolte and Cordelieres, 2006 (link)). Pearson’s values were analyzed using Prism7’s t-test statistical software (GraphPad.com).

Ryabov E.V., Robinson D.J, & Taliansky M.E. (1999). A plant virus-encoded protein facilitates long-distance movement of heterologous viral RNA. Proceedings of the National Academy of Sciences of the United States of America, 96(4), 1212-1217.

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Visualizing Tsg101 Localization in HeLa Cells

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HeLa cells (ATCC CCL-2) grown on poly-l-lysine treated cover slips were transfected with pCMV-Gag-EGFP alone or together with pLLEXP1-hTsg101-myc using Roche X-tremeGene transfection reagent. After 48 h, cells were fixed in 4% formaldehyde (Thermo-Fisher, Waltham, MA, USA) and permeabilized in 0.1% Triton X-100/PBS. Tsg101 was detected in samples by indirect immunofluorescence using anti-myc Mab (Santa Cruz, CA, USA, SC-40, 1:100) and Texas Red tagged goat anti-mouse IgG (Molecular Probes, Eugene, OR, USA, 1:400). Nuclei were stained with NucBlue reagent (Thermo Fisher). Z-stack images were captured on an inverted fluorescence/differential-interference contrast (dic) Zeiss Axiovert 200M deconvolving fluorescence microscope operated by AxioVision Version 4.5 software (Zeiss, Jena, Germany). Deconvolution image processing used the constrained iterative method (Zeiss AxioVision software). Protein co-localization was assessed in cells by determination of Pearson’s coefficient of correlation of the entire cell using Image J software (National Institutes of Health).

Watanabe S.M., Strickland M., Tjandra N, & Carter C.A. (2020). RNA Binding Suppresses Tsg101 Recognition of Ub-Modified Gag and Facilitates Recruitment to the Plasma Membrane. Viruses, 12(4), 447.

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Detecting Recombinant chIL-7 in Cells

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The recombinant chIL-7 in the culture medium was detected with Western blot as previously described (Wen et al., 2013 (link)) using Anti-Myc mAb (Santa Cruz Biotechnologies). For the intracellular chIL-7 detection, the transfected cells were lysed with lysis buffer (5 mM Tris-HCl, 25 mM KCl, 2 mM EGTA, 2 mM EDTA, 1% NP-40, 150 mM NaCl and protease inhibitors) and then subjected to Western blot described as above.

Huo S., Wang L., Zhang Y., Zhang J., Zuo Y., Xu J., Cui D., Li X, & Zhong F. (2016). Molecular cloning of chicken IL-7 and characterization of its antiviral activity against IBDV in vivo. Poultry Science, 95(11), 2647-2654.

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