Purity: > 95% by SDS - PAGE Format: Liquid. In 25 mM Tris-HCl buffer (pH 8.8) containing 5 mM DTT, 100 mM NaCl, 10% glycerol. 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. DnaJ(amino acids 1-376) was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques.
Size
0.5mg, 100ug, 20ug
Concentration
n/a
Applications
SDS-PAGE
Other Names
DNAJA1, DNAJ2, HDJ2, HSJ2, HSPF4, DnaJ (1-376aa), Heat shock 40 kDa protein 4, DnaJ protein homolog 2, HDJ-2, HSJ-2, HSDJ, DnaJ homolog subfamily A member 1,