R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Rad23B (D4W7F) Rabbit mAb #13525
Filter:
- WB
Supporting Data
REACTIVITY | H Mk |
SENSITIVITY | Endogenous |
MW (kDa) | 53 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Rad23B (D4W7F) Rabbit mAb recognizes endogenous levels of total Rad23B protein. This antibody does not cross-react with Rad23A protein.
Species Reactivity:
Human, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala140 of human Rad23B protein.
Background
The yeast nucleotide excision repair (NER) radiation sensitive protein 23 (rad23) and its human homologs Rad23A (hHR23A) and Rad23B (hHR23B) are critical components of the cellular machinery that recognize DNA lesions and serve as receptors that target ubiquitinated substrates to the proteasome for degradation (1).
The UV excision repair protein Rad23B is a multi-domain scaffold protein that plays an important role in ubiquitin-dependent proteasomal degradation. Rad23B contains an amino-terminal ubiquitin-like (UbL) domain that facilitates interaction with the S5a/PSMD4 subunit of the proteasome 19S regulatory complex (2,3). In addition, Rad23B contains a central ubiquitin-associated domain (UBA1) and a carboxy-terminal UBA2 domain, which bind mono- and polyubiquitin with distinct specificities (4). Research studies demonstrate that Rad23B binds specifically to K48-ubiquitinated proteins to facilitate recruitment of target proteins to the proteasome (5). Between the paired UBA domains, Rad23B contains an XPC-binding domain that facilitates binding to XPC and recruitment to DNA lesions (6), as well as the binding of peptide:N-glycanase that is critical for recruitment of ubiquitinated ERAD substrates to the proteasome (7). Research studies have shown that targeted deletion of the murine Rad23b locus impairs embryonic development, suggesting that Rad23B is essential for mammalian development (8).
The UV excision repair protein Rad23B is a multi-domain scaffold protein that plays an important role in ubiquitin-dependent proteasomal degradation. Rad23B contains an amino-terminal ubiquitin-like (UbL) domain that facilitates interaction with the S5a/PSMD4 subunit of the proteasome 19S regulatory complex (2,3). In addition, Rad23B contains a central ubiquitin-associated domain (UBA1) and a carboxy-terminal UBA2 domain, which bind mono- and polyubiquitin with distinct specificities (4). Research studies demonstrate that Rad23B binds specifically to K48-ubiquitinated proteins to facilitate recruitment of target proteins to the proteasome (5). Between the paired UBA domains, Rad23B contains an XPC-binding domain that facilitates binding to XPC and recruitment to DNA lesions (6), as well as the binding of peptide:N-glycanase that is critical for recruitment of ubiquitinated ERAD substrates to the proteasome (7). Research studies have shown that targeted deletion of the murine Rad23b locus impairs embryonic development, suggesting that Rad23B is essential for mammalian development (8).
- Verma, R. et al. (2004) Cell 118, 99-110.
- Ryu, K.S. et al. (2003) J Biol Chem 278, 36621-7.
- Walters, K.J. et al. (2003) Proc Natl Acad Sci U S A 100, 12694-9.
- Raasi, S. et al. (2005) Nat Struct Mol Biol 12, 708-14.
- Nathan, J.A. et al. (2013) EMBO J 32, 552-65.
- Masutani, C. et al. (1994) EMBO J 13, 1831-43.
- Lee, J.H. et al. (2005) Proc Natl Acad Sci U S A 102, 9144-9.
- Ng, J.M. et al. (2002) Mol Cell Biol 22, 1233-45.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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