Analytical Data
-
Gene name
GSTZ1
- Application
-
Alternative Names
GSTZ1-1 Glutathione S-transferase zeta 1 (EC:2.5.1.18)
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43708
-
Expression Region
1-216aa
-
Molecular Weight
51.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
GSTZ1, or glutathione S-transferase Zeta 1, is a member of the glutathione S-transferase superfamily, which plays a crucial role in the detoxification of harmful substances and the metabolism of xenobiotics. Research into GSTZ1 has gained significant attention due to its involvement in various physiological processes, including antioxidant defense and cellular stress response. This enzyme is particularly notable for its ability to catalyze the conjugation of glutathione to a variety of electrophilic compounds, thereby facilitating their excretion and reducing cellular toxicity. Additionally, GSTZ1 has been implicated in the metabolism of specific drugs and environmental toxins, making it a critical focus in pharmacogenomics and toxicology research. Abnormalities in GSTZ1 function are linked to various diseases, including certain cancers and metabolic disorders, prompting further investigation into its structural and functional properties. The recombinant expression and purification of GSTZ1 have become essential for understanding its enzymatic mechanisms and for developing therapeutic strategies aimed at enhancing its activity or compensating for its dysfunction. Studying GSTZ1 through recombinant protein technology allows researchers to explore its biochemical characteristics and interactions with potential substrates, ultimately contributing valuable insights into its role in health and disease. This body of research not only advances our understanding of GSTZ1's biological significance but also offers potential avenues for novel therapeutic interventions targeting GSTZ1-related conditions.
