RAD23 homolog B Peptide 2


Background

Catalog Number:

CPTC-RAD23B-2

RRID:

AB_2888971

Target Antigen:

RAD23 homolog B Peptide 2

Isotype:

IgG

Species:

Rabbit Monoclonal Antibody

Last Updated:

07/14/2022

Antigen Recognition(s):

Peptide

Thematic Panel(s):

DNA Damage Response (DDR) Pathway

External Links
Purchase
Publications
Characterization Data [Compare Characterization Data]
  Immuno-MRM
Click to enlarge image Immuno-MRM chromatogram of CPTC-RAD23B-2 antibody (see CPTAC assay portal for details: https://assays.cancer.gov/CPTAC-3248) 

Data provided by the Paulovich Lab, Fred Hutch (https://research.fredhutch.org/paulovich/en.html) Click image to enlarge

CPTC-RAD23B-2 IMRM

Result: Positive

Immuno-MRM chromatogram of CPTC-RAD23B-2 antibody (see CPTAC assay portal for details: https://assays.cancer.gov/CPTAC-3248)

Data provided by the Paulovich Lab, Fred Hutch (https://research.fredhutch.org/paulovich/en.html)


  Indirect ELISA
Click to enlarge image Indirect peptide ELISA (ie, binding of Antibody to biotinylated peptide coated on a NeutrAvidin plate). Note: B50% represents the concentration of Ab required to generate 50% of maximum binding. Click image to enlarge

CPTC-RAD23B-2 Indirect peptide ELISA

Result: Positive

Indirect peptide ELISA (ie, binding of Antibody to biotinylated peptide coated on a NeutrAvidin plate). Note: B50% represents the concentration of Ab required to generate 50% of maximum binding.


Characterization SOP Files

Background

NCI Identification Number:

00037

Antigen Name:

RAD23 homolog B Peptide 2

CPTC Name:

CPTC-RAD23B Peptide 2

Aliases:

HR23B; HHR23B; P58; XP-C Repair-Complementing Complex 58 KDa Protein; RAD23; RAD23, Yeast Homolog Of, B; UV Excision Repair Protein RAD23 Homolog B; XP-C Repair Complementing Complex 58 KDa; XP-C Repair Complementing Protein; HHR23B

Function:

The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in the nucleotide excision repair (NER). This protein was found to be a component of the protein complex that
specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro. This protein was also 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, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

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

Function: 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 Function: 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.

Chromosomal Localization:

9q31.2

Accession Number:

NP_002865.1

UniProt Accession Number:

P54727

DNA Source:

N/A

Immunogen:

Synthetic Peptide

Vector Name:

N/A

Extinction Coefficient:

Buffers:

Expressed Sequence:

IDIDPEETVK

Native Sequence:

Calculated Isoelectric Point:

0

Molecular Weight:

1100

Last Updated:

06/11/2013

Links

Characterization Data

SOPs

No SOPs available.

Don't have Adobe Reader™?

Get it for free at Adobe.com