RAD23B antibody

Catalog No. ABIN6241895

Product Details anti-RAD23B Antibody

Target: RAD23B (RAD23 Homolog B (RAD23B))

Reactivity: Human, Mouse

Host: Mouse

Clonality: Monoclonal

Conjugate: This RAD23B antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC)

Immunogen: Recombinant Protein

Application Details

Application Notes: WB: 1:1000. IHC: 1:100. ICC: 1:100

Restrictions: For Research Use only

Handling

Format: Liquid

Storage: 4 °C,-20 °C

Target Details for RAD23B

Target: RAD23B (RAD23 Homolog B (RAD23B))

Alternative Name: hHR23b (RAD23B Products)

Synonyms: HHR23B antibody, HR23B antibody, P58 antibody, 0610007D13Rik antibody, AV001138 antibody, mHR23B antibody, p58 antibody, MGC107846 antibody, zgc:65951 antibody, RAD23 homolog B, nucleotide excision repair protein antibody, UV excision repair protein RAD23 homolog B antibody, RAD23 homolog B, nucleotide excision repair protein S homeolog antibody, RAD23B antibody, Rad23b antibody, rd23b antibody, rad23b antibody, rad23b.S antibody

Background: 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.

UniProt: P54727

Pathways: DNA Damage Repair