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- hsp-043
- 2026年01月27日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
for future use below -18°C
- 保质期：
See instructions
- 英文名：
hchA
- 库存：
常规产品有备货
- 供应商：
上海经科化学科技有限公司
- CAS号：
无
- 规格：
5ug/20ug/1mg
| 规格： | 5ug | 产品价格： | ￥1080.0 |
|---|---|---|---|
| 规格： | 20ug | 产品价格： | ￥2415.0 |
| 规格： | 1mg | 产品价格： | ￥45885.0 |
CATALOGUE NUMBER
HSP-043
SYNONYMS
Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.
INTRODUCTION
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.
DESCRIPTION
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.
SOURCE
PHYSICAL APPEARANCE
FORMULATION
STABILITY
hchA E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C.
Please prevent freeze thaw cycles.
PURITY
AMINO ACID SEQUENCE
MG.S.SHHHHHH 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.
SAFETY DATA SHEET
SDS
USAGE
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文献和实验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.
of proteins in both normal and stressed cells. The rational manipulation of chaperone levels in a cell line engineered to produce a defined recombinant protein (rP) can significantly improve both the achievable steady-state levels and authenticity of a wide
Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression
Protein folding in the viscous and crowded environment of the cell is very different from in vitro processes in which a single protein is allowed to refold at low concentration in an optimized buffer. Although Anfinsen's observation
chaperone complexes of large HSPs and protein antigen may be exploited for augmentation of an antigen-specific immune response. The methods for the preparation of the recombinant protein antigen chaperone complex and characterization of its T-cell priming
技术资料
