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Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 μl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
Application References:
1. Maine GN, et al. 2007. EMBO 26:436. PubMed 2. Mao X, et al. 2009. Genes Dev. 23:849. PubMed 3. Mao, X., et al. 2011. J. Biol Chem. 16:32355. PubMed.
Hela cell nuclear extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-Elongin C antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Elongin C (also known as RNA polymerase II transcription factor SIII p15 subunit and transcription elongation factor B polypeptide 1) is a 12.5 kD member of the SKP1 family. Elongin functions as a regulatory subunit of a general transcription elongation factor that increases RNA polymerase II transcription elongation past template-encoded arresting sites in the nucleus. The Elongin BC complex acts as adaptor to link Elongin A, VHL, WSB1 or SOCS1 with a module of CUL2 or CUL5 and RBX1 to form E3 ubiquitin ligases. The Poly6131 antibody recognizes the human and mouse elongin C protein and has been shown to be useful for Western blotting.
Other Names:
RNA polymerase II transcription factor SIII p15 subunit, transcription elongation factor B polypeptide 1
Structure:
SKP1 family, heterotrimer; 12.5 kD
Distribution:
Nuclear
Function:
Regulatory subunit of a general transcription elongation factor that increases RNA polymerase II transcription elongation past template-encoded arresting sites
Interaction:
Elongin BC complex acts as adaptor to link Elongin A, VHL, WSB1 or SOCS1 with a module of CUL2 or CUL5 and RBX1 to form E3 ubiquitin ligases
Antigen References:
1. Garrett K, et al. 1994. P. Natl. Acad. Sci. USA 91:5237. 2. Stebbins C, et al. 1999. Science. 284:455. 3. Brower C, et al. 2002. P. Natl. Acad. Sci. USA 99:10353. 4. Haan S, et al. 2003. J. Biol. Chem. 278:31972.
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This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Purified anti-Elongin C
Hela cell nuclear extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-Elongin C antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
