Recombinant E.Coli Chaperone Protein hchA
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| Amount : | 20 µg |
| Purification : | Greater than 95.0% as determined by SDS-PAGE. |
| Content : | The hchA contains (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT. |
| Storage condition : | hchA E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles. |
| AA sequence : | MGSSHHHHHH SSGLVPRGSH MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG. |
| Alternative Name : | Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950. |
Source : Escherichia Coli.
hchA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-283 a.a.) and having a molecular mass of 33.3kDa.hchA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Escherichia coli Hsp31 (HchA) is a homodimeric member of the ThiI/DJ-1/PfpI superfamily which combines molecular chaperone and aminopeptidase activities. HchA uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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