Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Storage bufferpH: 7.20
Preservative: 0.01% Sodium azide
Constituents: 0.42% Potassium phosphate, 0.87% Sodium chloride
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab3835 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500. Detects a band of approximately 58 kDa (predicted molecular weight: 43 kDa).
Block with milk.
FunctionMultiubiquitin 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 endoplasmatic 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.
Sequence similaritiesBelongs to the RAD23 family.
Contains 1 STI1 domain.
Contains 2 UBA domains.
Contains 1 ubiquitin-like domain.
DomainThe ubiquitin-like domain mediates interaction with ATXN3.
Cellular localizationNucleus. Cytoplasm. 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.
- Information by UniProt
- hHR 23b antibody
- hHR23B antibody
- HR 23B antibody
Anti-hHR23b antibody (ab3835) at 1/500 dilution + HeLa whole cell lysate at 33 µg
IRDye 800 conjugated Rabbit anti-Goat IgG [H&L] at 1/10000 dilution
Predicted band size: 43 kDa
Observed band size: 58 kDa why is the actual band size different from the predicted?
Blocked with 5% milk. The band can be completely blocked with the immunising peptide (data not shown).
This product has been referenced in:
- Bergink S et al. Recognition of DNA damage by XPC coincides with disruption of the XPC-RAD23 complex. J Cell Biol 196:681-8 (2012). WB . Read more (PubMed: 22431748) »
- Tsuda N et al. Taxol increases the amount and T cell activating ability of self-immune stimulatory multimolecular complexes found in ovarian cancer cells. Cancer Res 67:8378-87 (2007). Read more (PubMed: 17804754) »