DnaJ (E. coli), (recombinant) (His-tag) | Enzo Life Sciences ADI-SPP-640-D product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

protein

product name :

DnaJ (E. coli), (recombinant) (His-tag)

catalog :

ADI-SPP-640-D

quantity :

50 µg

citations: 5

Reference
Miyazaki Imamura C, Oohira K, Kitagawa R, Nakano H, Yamane T, Takahashi H. Improvement of H2O2 stability of manganese peroxidase by combinatorial mutagenesis and high-throughput screening using in vitro expression with protein disulfide isomerase. Protein Eng. 2003;16:423-8 pubmed
Maki J, Schnobrich D, Culver G. The DnaK chaperone system facilitates 30S ribosomal subunit assembly. Mol Cell. 2002;10:129-38 pubmed
Vial S, Lu H, Allen S, Savory P, Thornton D, Sheehan J, et al. Assembly of Tim9 and Tim10 into a functional chaperone. J Biol Chem. 2002;277:36100-8 pubmed
Martens E, Alloza I, Scott C, Billiau A, Vandenbroeck K. Protein disulfide isomerase-mediated cell-free assembly of recombinant interleukin-12 p40 homodimers. Eur J Biochem. 2000;267:6679-83 pubmed
Kudlicki W, Odom O, Kramer G, Hardesty B. Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomes. J Biol Chem. 1996;271:31160-5 pubmed

product information

Product ID :

ADI-SPP-640

Catalog Number :

ADI-SPP-640-D

Product Name :

DnaJ (E. coli), (recombinant) (His-tag)

Product Type :

Protein

Size :

50 µg

list of Pubmed id :

12874375, 12150913, 12138093, 11054122, 8940114

Background :

Escherichia coli heat shock protein DnaJ belongs to the molecular chaperone class of proteins. Located in an operon with dnaK, theE. coli dnaJ gene shares sequence identity with eukaryotic cytosolic and endoplasmic reticulum DnaJ homologs (Hsp40) involved in protein folding, membrane translocation of newly synthesized proteins, and initiation of translation. The N-terminal, highly-conserved "J" domain of the DnaJ protein supports interaction with the DnaK protein and represents the signature sequence of DnaJ family members. Bacterial DnaJ protein acts synergistically with bacterial chaperones DnaK (Hsp70 homolog) and GrpE in various functions, including suppressing eukaryotic and prokaryotic polypeptide aggregation to promote protein folding, facilitating protein translocation through intracellular compartments or protein secretion , and repairing and reactivating partially aggregated enzymes such asE. coli RNAP and luciferase. In these reactions, DnaJ protein facilitates the binding of DnaK to its substrate by accelerating DnaK-catalyzed ATP hydrolysis to produce a DnaK-ADP form with a higher affinity for certain protein substrates. Some eukaryotic homologues of DnaJ also display an ability to stimulate the ATPase activity of Hsp70 proteins, including DnaJ homologue S. cerevisiae YDJ1 which interacts with DnaK homologue Ssal to stimulate its ATPase activity. Data suggests that DnaJ protein acting alone possesses chaperone activity, demonstrating an ability to bind tightly to denatured proteins such as rhodanese or luciferase to prevent their aggregation or misfolding.

ALTnames :

DNAJB2, DnaJ HSJ1, HSPF3, HSP40

Purity :

≥90% (SDS-PAGE; Western blot)

Buffer :

Liquid. In 25mM HEPES, pH 7.5, containing 200mM potassium chloride, 10% glycerol, and 5mM DTT.

Uses :

Western blot control.

Application Summary :

WB, Protein refolding assay

Storage :

-80°C