Recombinant Human SULT1A1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4371

Recombinant Human SULT1A1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4371
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His
Host Species Human
Accession P50225
Background Sulfate conjugation catalyzed by cytosolic sulfotransferase (SULT) enzymes. The SULTs are Phase II drug-metabolizing enzymes that catalyze the addition of a sulfuryl moiety to both endogenous compounds, including steroids and neurotransmitters, and certain xenobiotics, including N-hydroxy-2-acetylaminoflourine and phenolic compounds, like alpha-naphthol. SULTs may be involved in the individual genetic disposition, species differences, and organotropisms for toxicological effects of chemicals. Particularly SULT1A1 (Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1), a member of the sulfotransferase 1 subfamily, which is a major pathway for drug metabolism in humans. Humans have at least 1 functional SULT genes. There has been an explosion in information on sulfotransferase polymorphisms and their functional consequences. An Arg213His polymorphism in SULT1A1 has a strong influence on the level of enzyme protein and activity in platelets, which have been widely used for phenotyping. Statistically significant associations were observed between the SULT1A1 genotype (Arg213His) and age, obesity and certain neoplasias (mammary, pulmonary, esophageal and urothelial cancer). Furthermore, the polymorphism of the SULT1A1 may be closely associated with breast cancer.
Description A DNA sequence encoding the human SULT1A1 (P50225-1) (Glu 2-Leu 295) was fused with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Glu 2-Leu 295
Molecular Weight The recombinant human SULT1A1 consisting of 301 a.a. and has a calculated molecular mass of 35 kDa. It migrates as an approximately 32 kDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 50mM Tris, 150mM NaCl, 10% glycerol, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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. Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil. Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis.
Subcellular Location Cytoplasm.
Protein Families Sulfotransferase 1 family
Database References
Tissue Specificity Liver, lung, adrenal, brain, platelets and skin.

Gene Functions References

  1. SULT1A1 Arg213His (rs9282861) polymorphism might be associated with breast cancer risk, especially among Asian population. PMID: 29233949
  2. No significant difference was observed in the RNA levels of CYP1A1 and SULT1A1 between the two groups. The frequency of expression of the CYP17 T/C variant tended to be higher and the A allele of COMT polymorphism together with down-regulation of its mRNA expression may be more frequent in Chinese women with idiopathic POI PMID: 28887105
  3. The importance of SULT1A1 genotype for hepatic methyleugenol DNA adducts in humans, and a strong impact of SULT1A1 copy number variations on SULT1A1 hepatic phenotype. PMID: 28326452
  4. SULT1A1 role in the metabolic detoxification of heterocyclic aromatic amines PMID: 28160022
  5. Silencing the SULT1A1 gene led to changes in resveratrol metabolism, with higher intracellular accumulation of the nonmetabolized resveratrol. PMID: 28523759
  6. the NQO1 Pro187Ser or SULT1A1 Arg213His polymorphism combination with smoking significantly confer susceptibility to BC. [META-ANALYSIS] PMID: 28589969
  7. SULT1A1 gene copy number affected the minor allele frequency for each single nucleotide polymorphisms tested. Before administration of exogenous hormones, increasing number of G alleles at rs9282861 was associated with earlier age at menopause, lower frequency of night sweats, and less severe insomnia. Variability in onset of menopause and symptoms before initiation of hormone therapy is partly due to SULT1A1 variation. PMID: 27300114
  8. SULT1A1 copy number variation was negatively correlated with estrone-sulfate to estrone ratio predominantly in males (E1S/E1; p=0.03, r=-0.21) and may be associated with increased risk for common allergies. PMID: 28867356
  9. This study demonstrates that the presence of His allele and Gln allele in case of SULT1A1 rs9282861 and XRCC1 rs25487, respectively, involve in lung cancer prognosis in Bangladeshi population. PMID: 29110586
  10. We conclude from these studies that SULT1A1 is involved in the bioactivation of AA-I through the sulfonation of AL-I-NOH, contributing significantly to the toxicities of AA observed in vivo. PMID: 27207664
  11. Epigallocatechin gallate (EGCG) displays high affinity and specificity for SULT1A1. The allosteric network is shown to involve 14 distinct complexes. ECGG binds both the allosteric site and, relatively weakly, the active site of SULT1A1. PMID: 27356022
  12. The polymorphism of SULT1A1*2 is not associated with esophageal squamous cell carcinoma risk. PMID: 26455829
  13. SULT1A1 high Copy Number Variation on high Estrogen Concentration and Tamoxifen-Associated Adverse Drug Reactions in Premenopausal Thai Breast Cancer. PMID: 27221864
  14. SULT1A1 is responsible for bioactivation of food genotoxicants 5-hydroxymethylfurfural and furfuryl alcohol. PMID: 25370010
  15. Cytosolic sulfotransferase 1A1 regulates HIV-1 minus-strand DNA elongation in primary human monocyte-derived macrophages. PMID: 26906565
  16. A systematic analysis showed that three of the twelve human SULTs, SULT1A1, SULT1A3 and SULT1C4, displayed the strongest sulphating activity towards acetaminophen. PMID: 26067475
  17. Higher SULT1A1 levels were observed in rats as well as in humans exposed to high altitude, when compared to sea-level controls PMID: 26022216
  18. The present study provided epidemiological evidence for a significantly increased risk of UCB in ever smokers with the Ala/Ala genotype of the GSTO1 gene and the Arg/Arg genotype of the SULT1A1 gene. PMID: 25103078
  19. Sulfotransferase 1A1 Substrate Selectivity: A Molecular Clamp Mechanism. PMID: 26340710
  20. The aim of the study was to assess whether selected single nucleotide polymorphisms of CYP1A1 and 2E1, GSTM1, GSTT1, and SULT1A1 influence susceptibility towards hepatocellular carcinoma. PMID: 25654087
  21. Results indicate that SULT1A1 Arg(213)His may act as a low-penetrance risk allele for developing MBC and could be associated with a specific tumor subtype associated with HER2 overexpression. PMID: 25385181
  22. Sulfo-conjugation of the multi-hydroxylated metabolites of benzene by human SULT1A1 may represent an important detoxifying pathway. PMID: 25771868
  23. the SULT1A1 Arg213His polymorphism may contribute UADT cancer risk, but didn't show any association with breast cancer. PMID: 25225888
  24. that SULT1A1 Arg213His polymorphism is associated with bladder cancer risk. PMID: 25194687
  25. 3'-Phosphoadenosine 5'-phosphosulfate binds antisynergistically to the subunits of the SULT1A1 dimer. PMID: 25314023
  26. The results of this meta-analysis indicate that the SULT1A1 Arg213His polymorphism is associated with the risk bladder cancer under a recessive model. PMID: 24763827
  27. The SNP rs9282861 with GG genotype of SULT1A1 was associated with an elevated risk of total neural tube defects. PMID: 24307569
  28. The SULT1A1 genetic variability is associated with cancer risk and response to therapy (review). PMID: 24010997
  29. Association between BRCA2 mutation and SULT1A1 gene deletion in male breast cancer emerged. PMID: 23711090
  30. SULT1A1 variant allele increases breast cancer risk among subjects who were exposed to high smoked meat intake. PMID: 23157889
  31. The functional significance of the single nucleotide polymorphisms/haplotypes located upstream of the SULT1A1 start codon. PMID: 23080433
  32. discussion of possible association between lower-activity of SULT1A1 with sudden cardiac death (both holiday sudden cardiac death in older adults and sudden infant death syndrome) [REVIEW] PMID: 22678655
  33. We observed a previously unreported association between the SULT1A1 rs9282861 genotype and overall survival of breast cancer patients treated with adjuvant chemotherapy or tamoxifen. PMID: 22708928
  34. Arg213His polymorphism is not associated with lung cancer. PMID: 22524828
  35. SULT1A1 Arg213His polymorphism is associated with breast cancer. PMID: 22011087
  36. Women in Siberia with SNPS in CYP1A1 gene, in CYP1A2 gene,and in the SULT1A1 gene have an increased risk of development of breast cancer . PMID: 21977969
  37. SULT1A1 Arg213His polymorphism, ethnicity, and smoking may modulate environment-related cancer risk. PMID: 21670965
  38. Stp1 is important for appropriate regulation of Stk1 function, hemolysin activity, autolysis, and GBS virulence PMID: 22081606
  39. This meta-analysis demonstrates that there is no association between the SULT1A1 R213H polymorphism and colorectal cancer. PMID: 21695180
  40. SULT1A1 1/2 does not contribute to the variation in SULT1A1 enzymatic activity when the 3'-UTR SNPs are included in the statistical model PMID: 20881232
  41. mechanism of SULT1A1-catalyzed sulfation of adenosine 3',5'-diphosphate by para-nitrophenyl sulfate PMID: 21111704
  42. Only NAT1 showed a significant lower DNA methylation rate in the control group than in the tamoxifen-resistant breast cancer group, and no significant difference in methylation was found in COMT, CYP1A1, CYP2D6, and SULT1A1 genes. PMID: 20628863
  43. Polymorphism of SULT1A1 Arg213His is associated with breast cancer. PMID: 20663177
  44. Meta-analysis did not find a significant general relationship between SULT1A1 R213H polymorphism & the risk of breast cancer, but ethnic population analysis revealed a significantly increased breast cancer risk for HH allele carriers among Asians. PMID: 19949855
  45. The interaction between SULT1A1 and CYP1A2 can play an important role in hepatocarcinogenesis in the Chinese population. PMID: 19906068
  46. study demonstrates that the loss of SULT1A1 appears to be a characteristic molecular signature of hepatocellular carcinoma. PMID: 19904771
  47. human CYP2E1 and SULT1A1 activate an endogenous cellular molecule or a medium component to become mutagenic PMID: 19484729
  48. The high activity SULT1A1*1 allozyme protects against dietary and/or environmental chemicals involved in the pathogenesis of colorectal cancer. PMID: 11692076
  49. genetic polymorphism in SULT1A1 gene may be associated with increased lung cancer risk PMID: 11804685
  50. 7-OH-flavone sulfotransferase followed Michaelis-Menten kinetics PMID: 12162852


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed