|Product Name:||E.Coli DnaJ Recombinant Protein|
|Synonyms:||HSP-40, HSP40, DnaJ, DNAJB1, HSPF1, Hdj1, Chaperone protein dnaJ, Heat shock protein J, groP, b0015, JW0014.|
|Physical Appearance:||Sterile filtered colorless solution.|
|Formulation:||The DnaJ contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.|
|Stability:||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.|
|Purity:||Greater than 95.0% as determined by SDS-PAGE.|
|Amino Acid Sequence:||MAKQ DYYE ILGV SKTA EEHE IRKA YKRL AMKY HPDR NQGD KEAE AKFK EIKE AYEV LTDS QKRA AYDQ YGHA AFEQ GGMG GGGF GGGA DFSD IFGD VFGD IFGG GRGR QRAA RGAD LRYN MELT LEEA VRGV TKEI RIPT LEEC DVCH GSGA KPGT QPQT CPTC HGSG QVQM RQGF FAVQ QTCP HCQG RGTL IKDP CNKC HGHG RVER SKTL SVKI PAGV DTGD RIRL AGEG EAGE HGAP AGDL YVQV QVKQ HPIF EREG NNLY CEVP INFA MAAL GGEI EVPT LDGR VKLK VPGE TQTG KLFR MRGK GVKS VRGG AQGD LLCR VVVE TPVG LNER QKQL LQEL QESF GGPT GEHN SPRS KSFF DGVK KFFD DLTR|
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 41.1 kDa.