Recombinant Human SULT1A1/STP protein is a Human Full Length protein, in the 1 to 295 aa range, expressed in Escherichia coli, with >95% purity, = 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
>95% SDS-PAGE
= 1 EU/µg
Escherichia coli
His tag N-Terminus
SDS-PAGE, HPLC
No
M N H K V H H H H H H M E L I Q D T S R P P L E Y V K G V P L I K Y F A E A L G P L Q S F Q A R P D D L L I S T Y P K S G T T W V S Q I L D M I Y Q G G D L E K C H R A P I F M R V P F L E F K A P G I P S G M E T L K D T P A P R L L K T H L P L A L L P Q T L L D Q K V K V V Y V A R N A K D V A V S Y Y H F Y H M A K V H P E P G T W D S F L E K F M V G E V S Y G S W Y Q H V Q E W W E L S R T H P V L Y L F Y E D M K E N P K R E I Q K I L E F V G H S L P E E T V D F V V Q H T S F K E M K K N P M T N Y T T V P Q E F M D H S I S P F M R K G M A G D W K T T F T V A Q N E R F D A D Y A E K M A G C S L S F R S E L
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (PubMed:16221673, PubMed:12471039, PubMed:22069470, PubMed:21723874, PubMed:10199779, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621).
Sulfotransferase 1A1, ST1A1, Aryl sulfotransferase 1, HAST1/HAST2, Phenol sulfotransferase 1, Phenol-sulfating phenol sulfotransferase 1, ST1A3, Thermostable phenol sulfotransferase, P-PST 1, Ts-PST, STP1, OK/SW-cl.88, STP, SULT1A1
Recombinant Human SULT1A1/STP protein is a Human Full Length protein, in the 1 to 295 aa range, expressed in Escherichia coli, with >95% purity, = 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
Sulfotransferase 1A1, ST1A1, Aryl sulfotransferase 1, HAST1/HAST2, Phenol sulfotransferase 1, Phenol-sulfating phenol sulfotransferase 1, ST1A3, Thermostable phenol sulfotransferase, P-PST 1, Ts-PST, STP1, OK/SW-cl.88, STP, SULT1A1
>95% SDS-PAGE
= 1 EU/µg
Escherichia coli
His tag N-Terminus
SDS-PAGE, HPLC
No
No
Human
pH: 8
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride
M N H K V H H H H H H M E L I Q D T S R P P L E Y V K G V P L I K Y F A E A L G P L Q S F Q A R P D D L L I S T Y P K S G T T W V S Q I L D M I Y Q G G D L E K C H R A P I F M R V P F L E F K A P G I P S G M E T L K D T P A P R L L K T H L P L A L L P Q T L L D Q K V K V V Y V A R N A K D V A V S Y Y H F Y H M A K V H P E P G T W D S F L E K F M V G E V S Y G S W Y Q H V Q E W W E L S R T H P V L Y L F Y E D M K E N P K R E I Q K I L E F V G H S L P E E T V D F V V Q H T S F K E M K K N P M T N Y T T V P Q E F M D H S I S P F M R K G M A G D W K T T F T V A Q N E R F D A D Y A E K M A G C S L S F R S E L
Full Length
35.6 kDa
1 to 295
Recombinant
His tag N-Terminus
Liquid
Purity greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. ab172852 is 0.2 µM filtered.
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (PubMed:16221673, PubMed:12471039, PubMed:22069470, PubMed:21723874, PubMed:10199779, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621).
Belongs to the sulfotransferase 1 family.
Dry Ice
-20°C
Avoid freeze / thaw cycle
This product was previously labelled as SULT1A1
SULT1A1 also known as STP is an enzyme that plays an important role in the metabolism of various hormones drugs and other xenobiotic compounds. It belongs to the sulfotransferase family responsible for catalyzing the sulfate conjugation of many endogenous and exogenous compounds. SULT1A1 has a molecular mass of approximately 34 kDa. The enzyme is highly expressed in the liver but is also found in other tissues like the intestine and lung. It facilitates the transfer of a sulfo group from the universal sulfate donor 3’-phosphoadenosine-5’-phosphosulfate (PAPS) to substrates such as phenolic compounds.
The enzyme contributes significantly to the detoxification and activation of its substrates in the body. SULT1A1 functions without being part of a larger protein complex allowing it direct interaction with its substrates. By modifying hormones such as estrogens and catecholamines it helps regulate their activity and half-life. Additionally SULT1A1 plays a role in the metabolic processing of drugs influencing their pharmacokinetics and pharmacodynamics.
SULT1A1 is a critical component of both the phenolic metabolism pathway and the metabolism of xenobiotics by cytochrome P450. These pathways involve other proteins like CYP2C9 and GSTP1 which participate in further detoxification and conjugation reactions. Within these pathways SULT1A1 contributes to the inactivation or activation of compounds altering their biological activity and facilitating their excretion from the body.
SULT1A1 has been associated with variable drug responses and certain cancers. Altered activity of this enzyme can influence clearance of drugs potentially leading to adverse drug reactions or therapeutic failure. Moreover the dysregulation of estrogen metabolism partly mediated by SULT1A1 may contribute to hormone-related cancers such as breast cancer. The enzyme's interaction with proteins like UGT1A1 within these disease contexts highlights its role in the broader framework of metabolic processes impacting health and disease outcomes.
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