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| Product Name | GroES, Recombinant (Chaperonin 10, cpn10, Heat Shock Protein 10, HSP10) |
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| Description | Purity ≥95% (SDS-PAGE). The E.coli heat shock proteins GroEL and GroES are two of the most thoroughly characterized members of a class of proteins known collectively as ``molecular chaperones''. GroEL (cpn60; Hsp60 homolog) is an acidic 60kD E. coli heat shock protein which possesses a weak ATPase activity. In its native form, GroEL exists as a 14-mer consisting of two stacked rings each composed of seven identical subunits of Mr ~57,250. GroES (cpn10; Hsp10 homolog) consists of a single ring of seven identical subunits of Mr ~10,350 (2,3). Molecular chaperones, such as GroEL and GroES, are thought to function by interacting with transiently exposed interactive surfaces during their nascent synthesis, folding, transport and oligomerization. The net effect of chaperone participation in these processes is a reduction in inappropriate protein-protein interactions that might produce a nonfunctional structure. The GroEL and GroES genes, constituting the GroE operon, are members of the heat sh |
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| Size | 50ug, 200ug |
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| Concentration | n/a |
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| Applications | WB |
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| Other Names | n/a |
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| Gene, Accession, CAS # | SwissProt: P0A6F9 |
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| Catalog # | G8976-05 |
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| Order / More Info | GroES, Recombinant (Chaperonin 10, cpn10, Heat Shock Protein 10, HSP10) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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