DnaJ, Recombinant (HSP40)

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.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, add 0.1% HSA or BSA, aliquot and store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.\n

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SPECIFICATIONS

Catalog Number

D4015-10A

Size

20ug

Form

Supplied as a liquid in 25mM Tris-HCl, pH 7.5, 100mM sodium chloride, 5mM DTT and 10% glycerol.

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. Immunogenicity and protective efficacy of DnaJ (hsp40) of Streptococcus pneumoniae against lethal infection in mice.\n\nVaccine 2006 Jun 9;\n\n2. A new tumor suppressor DnaJ-like heat shock protein, HLJ1, and survival of patients with non-small-cell lung carcinoma.\n\nJ Natl Cancer Inst 2006 Jun 21;98(12):825-38\n\n3. Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins.\n\nJ Gen Virol 2006 Jul;87(Pt 7):1883-91\n\n4. Thermoprotection of synaptic transmission in a Drosophila heat shock factor mutant is accompanied by increased expression of Hsp83 and DnaJ-1.\n\nPhysiol Genomics 2006 May 16;25(3):493-501\n\n5. The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle.\n\nJ Biol Chem 2006 May 5;281(18):12436-44\n\n6. Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate.\n\nJ Biol Chem 2006 May 12;281(19):13150-8