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This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide at 0.5 mg/ml.
Preparation:
The antibody was purified by affinity chromatography, and conjugated with biotin under optimal conditions. The solution is free of unconjugated biotin.
Concentration:
0.5 mg/ml
Storage & Handling:
The antibody solution should be stored undiluted at 4°C. Do not freeze.
Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 5 μg 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:
Hela cell nuclear extracts were resolved by electrophoresis, transferred to nitrocellulose and probed with monoclonal anti-elongin B (clone 10C4). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
Elongin B (also known as RNA polymerase II transcription factor SIII p18 subunit and transcription elongation factor B polypeptide 2) is an 18 kD member of the UbH family containing a ubiquitin-like domain. Elongin functions as a 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 10C4 monoclonal antibody recognizes the human elongin B protein and has been shown to be useful for Western blotting.
Other Names:
RNA polymerase II transcription factor SIII p18 subunit, transcription elongation factor B polypeptide 2
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. Duan D, et al. 1995. Science. 269:1402. 2. Stebbins C, et al. 1999. Science. 284:455. 3. Brower C, et al. 2002. P. Natl. Acad. Sci. USA 99:10353. 4. DeRenzo C, et al. 2003. Nature. 424:685.
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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 B
Hela cell nuclear extracts were resolved by electrophoresis, transferred to nitrocellulose and probed with monoclonal anti-elongin B (clone 10C4). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
Biotin anti-Elongin B
Hela cell nuclear extracts were resolved by electrophoresis, transferred to nitrocellulose and probed with monoclonal anti-elongin B (clone 10C4). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
