Analytical Data
-
Gene name
GSTO2
- Application
-
Alternative Names
GSTO2; Glutathione S-transferase omega-2; GSTO-2; EC 2.5.1.18; Glutathione S-transferase omega 2-2; GSTO 2-2; Glutathione-dependent dehydroascorbate reductase; EC 1.8.5.1; Monomethylarsonic acid reductase; MMA(V) reductase; EC 1.20.4.2
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9H4Y5
-
Expression Region
1-243aa
-
AA Sequence
MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDFGLC
-
Molecular Weight
54.7 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
GSTO2 (Glutathione S-transferase omega 2) is a member of the glutathione S-transferase (GST) superfamily, which plays a critical role in cellular detoxification and the metabolism of xenobiotics. GSTO2 is primarily known for its function in conjugating glutathione to various electrophilic compounds, thereby aiding in their removal from the body. Research has shown that GSTO2 is involved in several cellular processes, including apoptosis, cell proliferation, and response to oxidative stress. It is also associated with various diseases, including cancer, neurodegenerative disorders, and other conditions linked to oxidative damage. The study of GSTO2 recombinantly expressed proteins has gained significance in understanding its structure-function relationships and elucidating its role in disease mechanisms. By generating and characterizing GSTO2 recombinant proteins, researchers aim to explore their enzymatic activity, substrate specificity, and interactions with other cellular components. This research could lead to insights into the development of GSTO2-targeted therapies and the identification of biomarkers for diseases where GSTO2 is implicated. Furthermore, understanding the mechanisms by which GSTO2 contributes to detoxification processes may have broader implications for pharmacology and toxicology, potentially informing the design of drugs that modulate its activity. Overall, the investigation of GSTO2 recombinant proteins represents an important avenue for advancing our comprehension of this multifunctional enzyme and its potential therapeutic applications.
