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Conditions of optimal DnaJ Protein performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
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Introduction
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.
Human HSP40 (heat shock protein with molecular size of 40kDa) is one of the mammalian homologues of bacterial DnaJ heat shock protein and regulates cellular processes by aiding in the folding, transport and assembly. HSP40 protein contains the J-domain which controls interaction with the ATPase domain of DnaK.
BP001984-HSP-007: Recombinant E.Coli DnaJ (HSP40) Protein
Source: E. coli-derived.
Recombinant Dna-J protein is a single, non-glycosylated polypeptide chain containing 376 amino acids and having a molecular mass of 41.1 kDa.
Purity: > 95.0% as determined by SDS-PAGE.
Formulation: The DnaJ contains 25 mM Tris-HCl buffer (pH 7.5), 100 mM NaCl, 5 mM DTT and 10% Glycerol.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
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