Recombinant E.Coli DnaJ (HSP40)
Source : Escherichia Coli. Recombinant Dna-J produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids and having a molecular mass of 41.1 kDa. 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.
Product Specifications
Product Name Alternative
HSP-40||HSP40||DnaJ||DNAJB1||HSPF1||Hdj1||Chaperone protein dnaJ||Heat shock protein J||groP||b0015||JW0014.
Purification
Greater than 95.0% as determined by SDS-PAGE.
Components
The DnaJ contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Storage Conditions
Amino Acids
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