DRAP1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q14919 |
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Clone Names | 100318203 |
Gene ID | 10589 |
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Other Names | Dr1-associated corepressor, Dr1-associated protein 1, Negative cofactor 2-alpha, NC2-alpha, DRAP1 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | DRAP1 |
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Function | The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. |
Cellular Location | Nucleus. |
Tissue Location | Ubiquitous. Highly expressed in adult testis, heart, skeletal muscle, pancreas and brain, and in fetal brain, liver and kidney. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Transcriptional repression is a general mechanism forregulating transcriptional initiation in organisms ranging fromyeast to humans. Accurate initiation of transcription fromeukaryotic protein-encoding genes requires the assembly of a largemultiprotein complex consisting of RNA polymerase II and generaltranscription factors such as TFIIA, TFIIB, and TFIID. DR1 is arepressor that interacts with the TATA-binding protein (TBP) ofTFIID and prevents the formation of an active transcription complexby precluding the entry of TFIIA and/or TFIIB into thepreinitiation complex. The protein encoded by this gene is acorepressor of transcription that interacts with DR1 to enhanceDR1-mediated repression. The interaction between this corepressorand DR1 is required for corepressor function and appears tostabilize the TBP-DR1-DNA complex.
References
Kahle, J., et al. J. Biol. Chem. 284(14):9382-9393(2009)Schluesche, P., et al. Nat. Struct. Mol. Biol. 14(12):1196-1201(2007)Albert, T.K., et al. Proc. Natl. Acad. Sci. U.S.A. 104(24):10000-10005(2007)Lim, J., et al. Cell 125(4):801-814(2006)Assmann, E.M., et al. J. Biol. Chem. 281(15):9869-9881(2006)
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