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Proteasome 19S Rpn10/S5a subunit (human), (recombinant) (GST-tag)

BML-UW8465-0100 100 µg 252.00 USD
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A subunit of the 26S proteasome, S5a, recognises and binds multi-ubiquitinylated proteins containing chains of at least four ubiquitin moieties. Purified recombinant S5a retains the ability to bind multi-ubiquitinylated proteins in isolation, when immobilised on glutathione-Sepharose, and after being eluted from glutathione-Sepharose, run on SDS-PAGE, and blotted onto nitrocellulose. Human S5a sequence, with an N-terminal fusion of glutathione S-transferase (Schistosoma japonicum), was expressed in E. coli with GST tag at amino terminus.

Product Specification

Alternative Name:26S proteasome non-ATPase regulatory subunit 4, Antisecretory factor 1, Multiubiquitin chain-binding protein
MW:~78kDa (observed)
Source:Produced in E. coli.
UniProt ID:P55036
Formulation:Liquid. In 20mM TRIS, pH 7.5, containing 500mM sodium chloride.
Purity:≥95% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Appearance:Colorless liquid.
Activity:Bound to mutliubiquitin chains of length >4 when conjugated to agarose (Prod. No. BML-UW8635).
Application Notes:Useful for the isolation of multi-ubiquitinylated proteins.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Scientific Background:S5a (RPN10), a subunit of the 19S regulator of the 26S proteasome, binds multi-ubiquitinylated proteins containing chains of at least four ubiquitin moieties.
SDS-PAGE Analysis of Rpn10/S5a. Lane 1: MW Marker, Lane 2: 1 µg.
Western Blot Analysis of Rpn10/S5a (Prod. No. BML-UW8465). Lane 1: MW Marker, Lane 2: Rpn10/S5a, Lane 3: Multiubiquitin chains (Prod. No. BML-UW8860), Lane 4: HeLa lysate (Prod. No. ADI-LYC-HL100). The blot on the left was probed with 10 µg/ml Rpn10, right with blocking buffer only. Rpn10 was detected by probing with GST polyclonal antibodies.
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Product Literature References

Quantitative Affinity Interaction of Ubiquitinated and Non-ubiquitinated Proteins with Proteasome Subunit Rpn10: O. A. Buneeva, et al.; Biochemistry (Moscow) 82, 1042 (2017), Abstract; Full Text

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