特徴
- 背景：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.
仕様
- サイズ：50ug
- 種由来：Human
- 発現宿主：E.coli
- 純度：> 97 % as determined by reducing SDS-PAGE.
- エンドトキシン濃度：Please contact us for more information.
- アクセッションＮｏ．：NP_003158.2
- タグ種類：N-His
- アミノ酸配列：Ser 2-Glu 285
- 遺伝子構造：A DNA sequence encoding the human SULT2A1 (NP_003158.2) (Ser 2-Glu 285) was expressed, with a polyhistide tag at the N-terminus.
- 別名（遺伝子名）：Bile Salt Sulfotransferase; Dehydroepiandrosterone Sulfotransferase; DHEA-ST; Hydroxysteroid Sulfotransferase; HST; ST2; ST2A3; Sulfotransferase 2A1; ST2A1; SULT2A1; HST; STD;DHEA-ST;DHEAS;ST2A3
- 分子量：
- 組成：Lyophilized from sterile 50mM Tris, 500mM NaCl, 20% glycerol, pH 8.0
- 保存条件：Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
- メーカーマニュアルリンク：https://www.elabscience.com/viewpdf-105542-Elabscience-PKSH031126.pdf
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- E-mail：[email protected]
商品のバリエーション （サイズ違い・スペック違い・オプション品など）
| 商品イメージ | アズワン品番 商品名 |
|---|---|
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89-7757-86
Recombinant Human SULT2A1 Protein (His Tag) 20ug
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89-7757-87
Recombinant Human SULT2A1 Protein (His Tag) 50ug
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