GSTM1 Human, Sf9
Sf9, Insect cells.
Greater than 90.0% as determined by SDS-PAGE.
Description
|
GSTM1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (1-218a.a.) fused to a 9 aa His Tag at C-terminus containing 227 amino acids and having a molecular mass of 26.8kDa. GSTM1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques. |
Product Specs
|
Recombinant GSTM1 protein, expressed in Sf9 insect cells, is a single polypeptide chain with a molecular weight of 26.8 kDa. It comprises 227 amino acids, including the 1-218 amino acid sequence of GSTM1 and a 9 amino acid Histidine tag fused at the C-terminus. The protein is glycosylated, meaning it has sugar molecules attached. On SDS-PAGE analysis under reducing conditions, GSTM1 appears as multiple bands between 28-40 kDa. The protein has been purified using proprietary chromatographic techniques. |
|
The GSTM1 protein solution is provided at a concentration of 0.5 mg/ml and contains the following components: 40% glycerol, 0.2M NaCl, 2mM DTT, and 0.1mM PMSF. |
For short-term storage (up to 2-4 weeks), the GSTM1 protein should be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. To ensure stability during long-term storage, it is advisable to add a carrier protein such as HSA or BSA to a final concentration of 0.1%. Avoid repeated freeze-thaw cycles to maintain protein integrity.
The purity of GSTM1 protein is determined to be greater than 90% using SDS-PAGE analysis.
Sf9, Insect cells.
|
ADPMPMILGY WDIRGLAHAI RLLLEYTDSS YEEKKYTMGD APDYDRSQWL NEKFKLGLDF PNLPYLIDGA HKITQSNAIL CYIARKHNLC GETEEEKIRV DILENQTMDN HMQLGMICYN PEFEKLKPKY LEELPEKLKL YSEFLGKRPW FAGNKITFVD FLVYDVLDLH RIFEPKCLDA FPNLKDFISR FEGLEKISAY MKSSRFLPRP VFSKMAVWGN KHHHHHH. |
Product Science Overview
Glutathione S-Transferase M1 (GST M1) is a member of the glutathione S-transferase family, which plays a crucial role in the detoxification of endogenous and exogenous compounds. The recombinant form of GST M1, expressed in Sf9 cells, is used extensively in research to study its biochemical properties and potential therapeutic applications.
GST M1 is an enzyme that catalyzes the conjugation of reduced glutathione (GSH) to a variety of hydrophobic and electrophilic compounds. This reaction is essential for the detoxification of harmful substances, including carcinogens, therapeutic drugs, and products of oxidative stress. The enzyme’s activity is critical in protecting cells from damage and maintaining cellular homeostasis.
The recombinant form of GST M1 is often expressed in Spodoptera frugiperda (Sf9) insect cells using the baculovirus expression system. This system is advantageous due to its high expression levels, proper protein folding, and post-translational modifications that are similar to those in mammalian cells. The use of Sf9 cells ensures that the recombinant protein retains its functional and structural integrity, making it suitable for various biochemical and pharmacological studies.
GST M1 has a molecular weight of approximately 25 kDa and exhibits high specificity for its substrates. The enzyme’s activity can be measured using spectrophotometric assays that detect the formation of conjugates between GSH and electrophilic compounds. The recombinant GST M1 expressed in Sf9 cells is typically purified to high homogeneity, ensuring its suitability for detailed biochemical analyses.
The GST M1 gene is known to exhibit genetic polymorphisms, with a significant portion of the population lacking the functional gene (GST M1 null genotype). This genetic variability can influence an individual’s susceptibility to various diseases, including cancer, due to differences in detoxification capacity. Studies have shown that individuals with the GST M1 null genotype may have an increased risk of developing certain types of cancer, particularly those related to environmental and occupational exposures.
Recombinant GST M1 is widely used in research to investigate its role in detoxification processes and its potential as a therapeutic target. The enzyme is also employed in drug development to screen for compounds that can modulate its activity. Additionally, GST M1 is used as a fusion tag in protein purification, taking advantage of its strong affinity for GSH, which allows for efficient purification of recombinant proteins.
