E.coli DnaJ protein (Recombinant) (No-Tag) (STJP019608)
SPECIFICATIONS
HostE.coli
ImmunogenE.coli
General Information
| Short Description | Recombinant-E.coli DnaJ-No-Tag protein was developed from e.coli and has a target region of No-Tag. For use in research applications. |
| Applications | SDS-PAGE |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 1 mg/mL |
| Formulation | Liquid in 25mM Tris-HCl buffer (pH 8.8) containing 5mM DTT, 100mM NaCl, 10% Glycerol |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Accession Number | NP_414556 |
| Immunogen | E.coli |
| Immunogen Region | 1-376aa |
| Immunogen Sequence | MAKQDYYEIL GVSKTAEEHE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRL |
Additional Info
| Background | 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. DnaJ (amino acids 1-376) was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques. |
Information sourced from Uniprot.org