Analytical Data
-
Gene name
SULT1A3
- Application
-
Alternative Names
Aryl sulfotransferase 1A3/1A4 Catecholamine-sulfating phenol sulfotransferase HAST3 M-PST Monoamine-sulfating phenol sulfotransferase Placental estrogen sulfotransferase Sulfotransferase 1A3/1A4 Sulfotransferase, monoamine-preferring Thermolabile phenol sulfotransferase Short name: TL-PST
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0DMM9
-
Expression Region
1-295aa
-
Molecular Weight
50.2 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
SULT1A3, a member of the sulfotransferase enzyme family, plays a critical role in the metabolism of various endogenous and exogenous compounds by catalyzing the sulfonation process. This enzymatic activity is crucial for the detoxification and elimination of drugs, hormones, and environmental toxins, which underscores the importance of SULT1A3 in pharmacology and toxicology. Research has shown that variations in SULT1A3 can influence drug response and susceptibility to certain diseases, including cancer, due to altered metabolic pathways. Additionally, SULT1A3 is involved in the biotransformation of catecholamines and estrogens, pointing to its potential implications in neurodegenerative diseases and hormonal disorders. Given its diverse substrate specificity and biological relevance, the recombinant expression of SULT1A3 is essential for characterizing its enzymatic properties, identifying substrates, and studying drug interactions. By producing a recombinant form of this enzyme, researchers aim to elucidate its structure-function relationship, assess its kinetic parameters, and explore its role in drug metabolism. This knowledge is vital for the development of safer therapeutic agents and personalized medicine approaches, as it can lead to better predictions of drug efficacy and toxicity in different populations. Overall, the study of SULT1A3 recombinant protein is a key area of research that bridges biochemistry, pharmacology, and clinical applications, contributing to our understanding of metabolic processes and their implications for human health.
