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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.

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Key facts

Purity

>95% SDS-PAGE

Endotoxin level

= 1 EU/µg

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, HPLC

Biologically active

No

Amino acid sequence

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

Reactivity data

Application

SDS-PAGE

Reactivity

Reacts

Dilution info

-

Notes

-

Application

HPLC

Reactivity

Reacts

Dilution info

-

Notes

-

Associated Products

Select an associated product type

3 products for Alternative Product

Target data

Function

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).

Alternative names

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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.

Alternative names

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

= 1 EU/µg

Expression system

Escherichia coli

Applications

SDS-PAGE, HPLC

Accession
P50225-1
Animal free

No

Species

Human

Concentration
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Storage buffer

pH: 8
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride

Sequence info

Amino acid sequence

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

Accession

P50225

Protein length

Full Length

Predicted molecular weight

35.6 kDa

Amino acids

1 to 295

Nature

Recombinant

Tags

His tag N-Terminus

Specifications

Form

Liquid

Additional notes

Purity greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. ab172852 is 0.2 µM filtered.

General info

Function

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).

Sequence similarities

Belongs to the sulfotransferase 1 family.

Storage

Shipped at conditions

Dry Ice

Appropriate long-term storage conditions

-20°C

Storage information

Avoid freeze / thaw cycle

Notes

This product was previously labelled as SULT1A1

Supplementary info

Activity summary

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.

Biological function summary

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.

Pathways

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.

Associated diseases and disorders

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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