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Mouse Anti-RAD23B antibody
Mouse Anti-RAD23B antibody
hHR 23b; hHR23B; HR 23B; HR23B; mHR 23B; mHR23B; P58; RAD 23B; RAD23 (S. cerevisiae) homolog B; RAD23 homolog B (S. cerevisiae); RAD23 homolog B; RAD23 yeast homolog of B; RD23B_HUMAN; UV excision repair protein RAD23 homolog B; XP C repair complementing
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Details

Product Name RAD23B
Chinese Name 紫外切除修复蛋白RAD23B单克隆抗体
Alias hHR 23b; hHR23B; HR 23B; HR23B; mHR 23B; mHR23B; P58; RAD 23B; RAD23 (S. cerevisiae) homolog B; RAD23 homolog B (S. cerevisiae); RAD23 homolog B; RAD23 yeast homolog of B; RD23B_HUMAN; UV excision repair protein RAD23 homolog B; XP C repair complementing complex 58 kDa; XP C repair complementing complex 58 kDa protein; XP C repair complementing protein; XP-C repair-complementing complex 58 kDa protein; XPC repair complementing complex 58 kDa; XPC repair complementing complex 58 kDa protein; XPC repair complementing protein.   
Research Area Chromatin and nuclear signals  Epigenetics  
Immunogen Species Mouse
Clonality Monoclonal
Clone NO. H13G1
React Species Human, Mouse, Rat, 
Applications WB=1:500-1000 
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
Theoretical molecular weight 43kDa
Cellular localization The nucleus cytoplasmic 
Form Liquid
Concentration 1mg/ml
immunogen KLH conjugated synthetic peptide derived from human RAD23B 
Lsotype IgG1,κ
Purification affinity purified by Protein G
Buffer Solution 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Storage Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Attention This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
PubMed PubMed
Product Detail 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. [provided by RefSeq, Sep 2011]

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.

Subunit:
Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3. Interacts with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1.

Subcellular Location:
Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.

Post-translational modifications:
Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation.
Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.

Similarity:
Belongs to the RAD23 family.
Contains 1 STI1 domain.
Contains 2 UBA domains.
Contains 1 ubiquitin-like domain.

SWISS:
P54727

Gene ID:
5887

Database links:

Entrez Gene: 5887 Human

Entrez Gene: 19359 Mouse

Entrez Gene: 298012 Rat

Omim: 600062 Human

SwissProt: P54727 Human

SwissProt: P54728 Mouse

SwissProt: Q4KMA2 Rat



Product Picture
Sample:
Lane 1: Jurkat cell lysates
Lane 2: A549 cell lysates
Lane 3: Huvec cell lysates
Lane 4: NIH/3T3 cell lysates
Lane 5: Mouse brain tissue lysates
Lane 6: Rat brain tissue lysates
Primary: Anti-RAD23B (SLM-51580M) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Mouse IgG at 1/20000 dilution
Predicted band size: 43 kD
Observed band size: 57 kD

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