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Rpn10 (S5a) (human), (recombinant) (His-tag)

 
BML-UW1065-0050 50 µg 118.00 USD
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Product Specification

Alternative Name:26S Proteasome regulatory subunit S5A, 26S proteasome non-ATPase regulatory subunit 4, Antisecrectory factor 1, Multiubiquitin chain-binding protein
 
MW:~42.9kDa
 
Source:Produced in E. coli.
 
UniProt ID:P55036
 
Formulation:Liquid. In PBS containing 1mM DTT.
 
Purity:≥95% (SDS-PAGE)
 
Shipping:Shipped on Dry Ice
 
Short Term Storage:-80°C
 
Long Term Storage:-80°C
 
Use/Stability:Stable for at least 12 months after receipt when stored at -80ºC.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
Scientific Background:S5a/Rpn10 is a major ubiquitin binding protein that binds preferentially to polyubiquitin chains. It is found as a non-ATPase subunit of the 19S regulatory complex of the 26S proteasome where it functions as a receptor for proteins destined for proteolytic degradation. In yeast, the homologue of S5a, Rpn10, is required for degradation of a subset of cellular proteins by the proteasome. Unlike other proteasome subunits, S5a exists predominantly as a free protein in the cytosol (i.e. not incorporated into the proteasome), though its precise role in the cytosol has yet to be fully elucidated.

S5a contains two approximately 15 amino acid ubiquitin interacting motifs (UIM) which are responsible for its binding to polyubiquitin chains. In vitro S5a binds predominantly to chains of at least four ubiquitins in length and can act as a substrate for a wide range of ubiquitin E3 ligases, which, it has been suggested, occurs by a novel mechanism involving the association of S5a with growing poly-Ub chains.
 
BML-UW1065
SDS-PAGE image (coomassie stained) of His6-S5a (5µg, BML-UW1065).
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BML-UW1065

General Literature References

The ubiquitin-interacting motif protein, S5a, is ubiquitinated by all types of ubiquitin ligases by a mechanism different from typical substrate recognition: T. Uchiki, et al.; J. Biol. Chem. 284, 12622 (2009), Abstract;
Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system: R. Verma, et al.; Cell 118, 99 (2004), Abstract;
ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells: Q. Mao, et al.; Biochim. Biophys. Acta 1461, 69 (1999), Abstract;
Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a: P. Young, et al.; J. Biol. Chem. 273, 5461 (1998), Abstract;
ATPase and ubiquitin-binding proteins of the yeast proteasome: D.M. Rubin, et al.; Mol. Biol. Rep. 24, 17 (1997), Abstract;
The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover: S. van Nocker, et al.; Mol. Cell Biol. 16, 6020 (1996),
A 26 S protease subunit that binds ubiquitin conjugates: Q. Deveraux, et al.; J. Biol. Chem. 269, 7059 (1994), Abstract;

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