Trip12

Manufactured by Abcam

TRIP12 is a gene that encodes the E3 ubiquitin-protein ligase TRIP12. This enzyme is involved in the ubiquitination and degradation of target proteins.

Automatically generated - may contain errors

Lab products found in correlation

Gapdh, by Merck Group (1 mentions) Smarce1 baf57, by Fortis Life Sciences (1 mentions) Smarcb1 snf5, by Fortis Life Sciences (1 mentions) Eif4e, by BD (1 mentions) Prmt5, by Merck Group (1 mentions) Cdc42, by BD (1 mentions) Horseradish peroxidase conjugated secondary antibody, by GE Healthcare (1 mentions) Trans blot turbo, by Bio-Rad (1 mentions) Gradient polyacrylamide gel, by Bio-Rad (1 mentions)

2 protocols using trip12

Protein Expression Analysis in Prostate Cancer

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Procedures were previously described (Mounir et al., 2015 (link)) and the following antibodies were used at 1:1000 dilutions and incubated overnight at 4°C: ERG (Epitomics# 2805–1), PRMT5 (CST# 2252; SIGMA#P0493), GAPDH (Millipore#MAB374), H4 (CST#2592), AR (Santa Cruz#sc-7305), HA (Roche#11815016001), Symmetric Di-methyl arginine (SDMA, CST#13222), Mono-methyl arginine (MMA, CST#8711), TRIP12 (Abcam#ab86220), EIF4E (CST#9742), CDC42 (BD Transduction Laboratories#610929), HDAC1 (CST#2062), SMARCB1/SNF5 (Bethyl Laboratories# A301-087A), SMARCE1/BAF57 (Bethyl Laboratories# A300–810A).

Mounir Z., Korn J.M., Westerling T., Lin F., Kirby C.A., Schirle M., McAllister G., Hoffman G., Ramadan N., Hartung A., Feng Y., Kipp D.R., Quinn C., Fodor M., Baird J., Schoumacher M., Meyer R., Deeds J., Buchwalter G., Stams T., Keen N., Sellers W.R., Brown M, & Pagliarini R.A. (2016). ERG signaling in prostate cancer is driven through PRMT5-dependent methylation of the Androgen Receptor. eLife, 5, e13964.

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Western Blot Analysis of Cellular Proteins

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Following treatment, cells were lysed with extraction buffer containing 20mM Hepes, pH 7.9, 400mM NaCl, 0.1mM EDTA pH 8.0, 0.1mM EGTA pH 7.0 and XPert protease and phosphatase inhibitors were added at 1:100 dilution (GenDepot) then sonicated. Equal amounts of protein were loaded into 4–15% gradient polyacrylamide gels (Bio-Rad) then transferred to PVDF membranes for 10min at 25V using Trans-Blot Turbo (Bio-Rad). Membranes were incubated in 5% dry milk for 1h then incubated in primary antibody p16 1:1000 (BD Biosciences), Trip12 1:10,000 (Abcam) or Actin 1:2000 (Cell Signaling Technologies) overnight at 4°C. Immunoblots were detected using horseradish peroxidase-conjugated secondary antibodies (GE) and ECL2 chemiluminescent substrate (Pierce).

Molkentine J.M., Molkentine D.P., Bridges K.A., Xie T., Yang L., Sheth A., Heffernan T.P., Clump D.A., Faust A.Z., Ferris R., Myers J.N., Frederick M.J., Mason K.A., Meyn R.E., Pickering C.R, & Skinner H.D. (2020). Targeting DNA damage response in head and neck cancers through abrogation of cell cycle checkpoints. International journal of radiation biology, 97(8), 1121-1128.

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