Recombinant E.Coli DnaJ (HSP40)
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| Amount : | 50 µg |
| Purification : | Greater than 95.0% as determined by SDS-PAGE. |
| Content : | The DnaJ contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
| AA sequence : | MAKQDYYEIL GVSKTAEEHE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDSQKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYNMELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQQTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAPAGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRSKSFFDGVKKF FDDLTR. |
| Alternative Name : | HSP-40, HSP40, DnaJ, DNAJB1, HSPF1, Hdj1, Chaperone protein dnaJ, Heat shock protein J, groP, b0015, JW0014. |
Source : Escherichia Coli.
Recombinant Dna-J produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids and having a molecular mass of 41.1 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.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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