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| Product Name | DnaJ, Recombinant (HSP40) |
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| Description | Purity ≥ 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel. DnaJ, Heat shock protein, functions in association with DnaK(Hsp70) molecular chaperone to facilitate protein folding. p70 chaperone. DnaJ plays a key role in the chaperone reaction by stimulating the ATPase activity and activating the substrate binding of Hsp70. DnaJ consists of four domains that are N-terminal 76 amino acid J-domain, G/F domain, zinc-binding cystein rich CR-domain, C-terminal CTD-domain and they are conserved to various degrees among the homologues. Recombinant Dna-J produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids and having a molecular mass of 41.1kD. |
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| Size | 10ug, 50ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | D4015-10A |
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| Order / More Info | DnaJ, Recombinant (HSP40) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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