Introduction
The enzyme GSTK1 plays a crucial role in cellular detoxification. It resides in the peroxisome, an organelle within the cell, and facilitates the removal of harmful substances. Specifically, GSTK1 catalyzes the conjugation of glutathione (GSH), a naturally occurring antioxidant, to electrophilic compounds. This conjugation process makes these compounds more water-soluble, enabling their efficient elimination from the cells.
Description
Recombinant human GSTK1, expressed in E. coli, is available as a purified, non-glycosylated polypeptide chain. This protein consists of 226 amino acids (spanning positions 1 to 226) and exhibits a molecular weight of 25.5 kDa. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
The product is provided as a sterile, colorless solution that has been filtered for clarity.
Formulation
The GSTK1 solution is supplied in a buffer composed of 20mM Tris at pH 8, 1mM DTT (dithiothreitol), and 10% glycerol. These components help maintain protein stability and prevent degradation.
Stability
For short-term storage (2-4 weeks), the entire vial can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To further enhance long-term stability, the addition of a carrier protein like HSA (human serum albumin) or BSA (bovine serum albumin) at a concentration of 0.1% is advisable. Repeated freeze-thaw cycles should be avoided to preserve protein integrity.
Purity
The purity of the GSTK1 protein is greater than 90%, as assessed by SDS-PAGE analysis, ensuring a high-quality product for research purposes.
Synonyms
GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.
Amino Acid Sequence
MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL.
