hchA E.Coli
Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.
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.
Product Specs
Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.
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.
Product Science Overview
Chaperone proteins play a crucial role in the cellular machinery by assisting the folding of newly synthesized proteins, preventing aggregation, and refolding misfolded proteins. One such chaperone protein is hchA, found in Escherichia coli (E. coli). The recombinant form of this protein has been extensively studied for its potential applications in biotechnology and medicine.
The hchA protein, also known as heat shock protein Hsp31, belongs to the DJ-1/ThiJ/PfpI superfamily. It is a small molecular chaperone that is upregulated in response to heat shock and other stress conditions. The primary function of hchA is to prevent the aggregation of proteins under stress conditions, thereby maintaining cellular homeostasis.
The recombinant production of hchA involves the insertion of the hchA gene into an expression vector, which is then introduced into E. coli cells. The cells are cultured under conditions that induce the expression of the recombinant protein. The protein is then purified using techniques such as affinity chromatography, which exploits the specific binding properties of the protein to isolate it from other cellular components.
The activity of hchA can be analyzed through various biochemical assays that measure its ability to prevent protein aggregation. One common method is the use of a model substrate protein that tends to aggregate under stress conditions. The presence of hchA can significantly reduce the aggregation of this substrate, demonstrating its chaperone activity.
Additionally, structural analysis techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy can be employed to determine the three-dimensional structure of hchA. These studies provide insights into the molecular mechanisms by which hchA interacts with substrate proteins and prevents their aggregation.
The recombinant hchA protein has potential applications in various fields. In biotechnology, it can be used to improve the yield and solubility of other recombinant proteins by co-expressing it with target proteins. In medicine, hchA and other chaperone proteins are being explored for their potential to treat diseases associated with protein misfolding and aggregation, such as neurodegenerative disorders.
