GST, His
Greater than 90% as determined by SDS-PAGE.
Description
Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa.
The GST protein is fused to a 20 amino acids His-Tag at N-terminus.
The GST protein is purified by proprietary chromatographic techniques.
Product Specs
This recombinant Schistosoma japonicum GST protein is expressed in E.coli. It consists of the full-length protein sequence (218 amino acids) with an additional 20 amino acid His-Tag fused at the N-terminus, resulting in a total of 244 amino acids and a molecular weight of 28.3 kDa. The protein is purified using proprietary chromatographic techniques.
The purity of this GST protein is determined to be greater than 90% by SDS-PAGE analysis.
The biological activity of this GST protein is greater than 10 units/mg. One unit is defined as the amount of enzyme required to conjugate 1.0 µmol of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at a pH of 6.5 and a temperature of 25°C.
MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.
Product Science Overview
Glutathione S-Transferase (GST) is a crucial enzyme involved in the detoxification process in various organisms, including plants, animals, bacteria, and algae . Recombinant GST, often used as a fusion protein, is a 26 kDa protein originally derived from the parasitic helminth Schistosoma japonicum . The His Tag, a sequence of histidine residues, is commonly used in protein purification due to its affinity for nickel or cobalt ions .
GST is widely utilized in biotechnology for its ability to enhance the solubility and stability of recombinant proteins . When fused to a target protein, GST can facilitate the expression, folding, and purification of the protein in various host cells, including bacterial, fungal, and eukaryotic systems . This makes GST an invaluable tool in structural and functional proteomic studies .
The His Tag, typically consisting of six histidine residues, is another widely used affinity tag in protein purification . It binds strongly to nickel or cobalt ions immobilized on a support matrix, allowing for efficient purification of His-tagged proteins through affinity chromatography . This method is particularly advantageous for purifying recombinant proteins with both known and unknown biochemical properties .
Combining GST and His Tag in a single recombinant protein offers several benefits. The GST tag enhances the solubility and stability of the protein, while the His Tag facilitates its purification . This dual-tagging approach is especially useful in high-throughput protein purification, where the target proteins are fused to both affinity tags to streamline the purification process .
The use of GST and His Tag in recombinant protein production has revolutionized the field of biotechnology. These tags enable researchers to produce and purify proteins efficiently, aiding in the study of their biological functions . The methodology has become a widely used research tool for determining the biological function of uncharacterized proteins .
