DNAJ / HSP40 (1-376) Escherichia coli Protein

CAT#: SA6028X

DNAJ / HSP40 (1-376) e. coli protein, 0.5 mg

Product Images

Specifications

Product Data

• Species: Escherichia coli
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  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
• Predicted MW: 41 kDa
• Concentration: lot specific
• Purity: >95% by SDS-PAGE
• Presentation: Purified
• Buffer: Presentation State: Purified
  State: Liquid purified protein
  Buffer System: 25 mM Tris-HCl, pH 7.5, 100 mM NaCl, 5 mM DTT, 10% Glycerol
• Preparation: Liquid purified protein
• Protein Description: DnaJ(amino acids 1-376) was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques.
• Storage: Store (in aliquots) at -20°C. Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.

Reference Data

• Summary: 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.