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 Details
| Alternative Name: | 26S proteasome non-ATPase regulatory subunit 4, Antisecretory factor 1, Multiubiquitin chain-binding protein |
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| MW: | ~78kDa (observed) |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P55036 |
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| Formulation: | Liquid. In 20mM TRIS, pH 7.5, containing 500mM sodium chloride. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Appearance: | Colorless liquid. |
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| Activity: | Bound to mutliubiquitin chains of length >4 when conjugated to agarose (Prod. No. BML-UW8635). |
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| Application Notes: | Useful for the isolation of multi-ubiquitinylated proteins. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| 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. |
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| Regulatory Status: | RUO - Research Use Only |
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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.
SDS-PAGE Analysis of Rpn10/S5a. Lane 1: MW Marker, Lane 2: 1 µg.
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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
