This antibody is purified through a protein G column, followed by dialysis against PBS.
Immunogène
This RAD23B antibody is generated from a mouse immunized with a KLH conjugated synthetic peptide between 1-409 amino acids from the N-terminal region of human RAD23B.
RAD23B
Reactivité: Humain
WB, ELISA, IHC
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
WB: 1:1000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified monoclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C,-20 °C
Date de péremption
6 months
Huang, Wang, Xu, Lu, Xu, Li, Zhou, Sha: "Expression of a novel RAD23B mRNA splice variant in the human testis." dans: Journal of andrology, Vol. 25, Issue 3, pp. 363-8, (2004) (PubMed).
Humphray, Oliver, Hunt, Plumb, Loveland, Howe, Andrews, Searle, Hunt, Scott, Jones, Ainscough, Almeida, Ambrose, Ashwell, Babbage, Babbage, Bagguley, Bailey, Banerjee, Barker, Barlow, Bates, Beasley et al.: "DNA sequence and analysis of human chromosome 9. ..." dans: Nature, Vol. 429, Issue 6990, pp. 369-74, (2004) (PubMed).
Masutani, Sugasawa, Yanagisawa, Sonoyama, Ui, Enomoto, Takio, Tanaka, van der Spek, Bootsma: "Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23." dans: The EMBO journal, Vol. 13, Issue 8, pp. 1831-43, (1994) (PubMed).
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 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. May play a role in endoplasmic reticulum- associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. 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 stimulates the activity of DNA glycosylases TDG and SMUG1.