||Recombinant DnaJ was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques (376 aa, 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.
||Liquid. In 25 mM Tris-HCl buffer (pH 7.5) containing 5 mM DTT, 100 mM NaCl, 10% glycerol.
||41.1 kDa (376aa).
||> 95% by SDS – PAGE.
||1 mg/ml (determined by Bradford assay).
||MAKQDYYEIL GVSKTAEEHE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRS KSFFDGVKKF FDDLTR
||Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.