Description
Recombinant Human AGO3/Argonaute 3/EIF2C3 Protein (His Tag) | PKSH031121 | Gentaur US, UK & Europe Disrtribition
Synonyms: EIF2C3
Active Protein: N/A
Activity: A DNA sequence encoding the human EIF2C3 (Q9H9G7-1) (Met 1-Ala 860) was expressed, with a polyhistidine tag at the N-terminus.
Protein Construction: A DNA sequence encoding the human EIF2C3 (Q9H9G7-1) (Met 1-Ala 860) was expressed, with a polyhistidine tag at the N-terminus.
Fusion Tag: N-His
Species: Human
Expressed Host: Baculovirus-Insect Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 88 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 99.6 kDa
Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly
Reconstitution: Please refer to the printed manual for detailed information.
Background: Hydroxysteroid sulfotransferase ( SULT2A1 ) is a key enzyme in the testicular and hepatic metabolism of 5alpha-androstenone, which is a major component of the off-odor and off-flavor in pork known as boar taint. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. SULT2A1 is a sulfo-conjugating phase II enzyme expressed at very high levels in the liver and intestine, the two major first-pass metabolic tissues, and in the steroidogenic adrenal tissue. SULT2A1 acts preferentially on the hydroxysteroids dehydroepiandrosterone, testosterone/dihydrotestosterone, and pregnenolone and on cholesterol-derived amphipathic sterol bile acids.
Research Area: N/A
