Cat: IPD-X37523

Recombinant Human SULT1A2 Protein,His

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Analytical Data

  • Gene name

    SULT1A2

  • 简介

    Sulfotransferase 1A2 (SULT1A2) is a phenol sulfotransferase with thermostable enzyme activity. SULT1A2 utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. SULT1A2 is also responsible for the sulfonation and activation of minoxidil. SULT1A2 induces the mutagenicity and carcinogenicity of certain substrates by influencing DNA adduct formation. SULT1A2 Protein, Human (His) is the recombinant human-derived SULT1A2 protein, expressed by E. coli , with N-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Sulfotransferase 1A2; ST1A2; Aryl Sulfotransferase 2; Phenol Sulfotransferase 2; Phenol-Sulfating Phenol Sulfotransferase 2; P-PST 2; SULT1A2; STP2

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    AAI13728.1

  • Expression Region

    M1-L295

  • AA Sequence

    MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL

  • Protein Length

    Full Length

  • Molecular Weight

    33 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

SULT1A2, or Sulfotransferase 1A2, is an important enzyme that catalyzes the sulfonation of various endogenous and exogenous compounds, playing a critical role in drug metabolism and detoxification processes. This enzyme is part of the sulfotransferase family, which is involved in the phase II metabolic reactions that modify small molecules, including hormones, neurotransmitters, and drugs, to enhance their solubility and excretion. Recent studies have highlighted the individual variability in SULT1A2 activity due to genetic polymorphisms, leading to differences in drug responses and susceptibility to toxins. Furthermore, SULT1A2 has been implicated in the metabolism of environmental contaminants and pharmaceuticals, making it a significant focus of pharmacogenomics and toxicology research. Understanding the structure and function of SULT1A2 through the study of its recombinant protein is essential for elucidating its role in biotransformation pathways and its potential implications in personalized medicine. Advances in recombinant DNA technology have enabled the production of SULT1A2 protein in vitro, allowing researchers to investigate its enzymatic properties, substrate specificity, and interaction with various inhibitors. These insights not only contribute to a fundamental understanding of the enzyme's biochemistry but also hold promise for developing therapeutic strategies and improving drug safety profiles in clinical settings.

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