|Application ||WB, E|
|Other Accession||A3KMV2, NP_005044.1|
|Calculated MW||39609 Da|
|Antigen Region||42-70 aa|
|Other Names||UV excision repair protein RAD23 homolog A, HR23A, hHR23A, RAD23A|
|Target/Specificity||This RAD23A antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 42-70 amino acids from the N-terminal region of human RAD23A.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RAD23A Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. Involved in vpr-dependent replication of HIV-1 in non- proliferating cells and primary macrophages. Required for the association of HIV-1 vpr with the host proteasome.|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, as well as with ubiquitin protein ligase E6AP, and thus suggests that this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. [provided by RefSeq].
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Briggs, F.B., et al. Am. J. Epidemiol. 172(2):217-224(2010)
Monsees, G.M., et al. Breast Cancer Res. Treat. (2010) In press :
Li, G., et al. PLoS ONE 5 (6), E11371 (2010) :
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
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