Recombinant E.Coli Dnak Substrate Binding Domain
Source : Escherichia Coli. Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 14.6 kDa. DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. Dnak (residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK (amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
Product Specifications
Product Name Alternative
HSP-70||HSP70||DnaK||Chaperone protein dnaK||Heat shock protein 70||Heat shock 70 kDa protein||groP||grpF||seg||b0014||JW0013.
Purification
Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Components
The protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10%Glycerol.
Storage Conditions
Amino Acids
MNEDEIQKMV RDAEANAEAD RKFEELVQTR NQGDHLLHST RKQVEEAGDK LPADDKTAIESALTALETAL KGEDKAAIEA KMQELAQVSQ KLMEIAQQQH AQQQTAGADASANNAKDDDVVDAEFEEVKDKK.
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