RAD23B Antibody, Biotin conjugated

$210.00$377.00

Cat. No.: 44291 Categories: ,

Description

Aliases

UV excision repair protein RAD23 homolog B, HR23B, hHR23B, XP-C repair-complementing complex 58 kDa protein, p58, RAD23B

Antibody Type

Polyclonal Antibody

Species

Human

Uniprot ID

P54727

Immunogen

Recombinant human UV excision repair protein RAD23 homolog B protein (1-250AA)

Raised In

Rabbit

Species Reactivity

Human

Tested Applications

ELISA;Not yet tested in other applications.

Background / Function

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. 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 stimulates the activity of DNA glycosylases TDG and SMUG1.

Isotype

IgG

Conjugate

Biotin

Storage Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4

Form

Liquid

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze.

Purity

Caprylic Acid Ammonium Sulfate Precipitation purified

Literature

[1]”Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008). [2]”Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.”Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.Biochemistry 46:3553-3565(2007). [3]”Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B.”Chen L., Madura K.FEBS Lett. 580:3401-3408(2006).

Additional information

Size

50μg, 100μg

Certificate of Analysis