ELISA RAD23B Antibody, FITC

Quantity :50µg Clone Number: Aliases:hHR 23b antibody; hHR23B antibody; HR 23B antibody; HR23B antibody; mHR 23B antibody; mHR23B antibody; p58 antibody; RAD 23B antibody; RAD23 (S. cerevisiae) homolog B antibody; RAD23 homolog B (S. cerevisiae) antibody; RAD23 homolog B antibody; RAD23 yeast homolog of B antibody; Rad23b antibody; RD23B_ antibody; UV excision repair protein RAD23 homolog B antibody; XP C repair complementing complex 58 kDa antibody; XP C repair complementing complex 58 kDa protein antibody; XP C repair complementing protein antibody; XP-C repair-complementing complex 58 kDa protein antibody; XPC repair complementing complex 58 kDa antibody; XPC repair complementing complex 58 kDa protein antibody; XPC repair complementing protein antibody Product Type:Polyclonal Antibody Immunogen Species:Homo sapiens () UniProt ID:P54727 Immunogen:Recombinant UV excision repair protein RAD23 homolog B protein (1-250AA) Raised in:Rabbit Reactivity: Tested Applications: Background:MµLtiubiquitin chain receptor involved in modµLation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simµLtaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticµLum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5\'-to-3\' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5\' and 3\' of a cisplatin lesion with a preference for the 5\' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimµLates the activity of DNA glycosylases TDG and SMµg1. Clonality:Polyclonal Isotype:IgG Purification Method:>95%, Protein G purified Conjµgate:FITC Buffer:Preservative: 0.03% Proclin 300 Constituents: 50% Glycerol, 0.01M PBS, PH 7.4 Form:Liquid Stroage:Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Target Names:RAD23B Research Areas:Epigenetics and Nuclear Signaling