Recombinant Rat Sulfotransferase 1A1 (SULT1A1) Protein (His-SUMO&Myc)

Name: Recombinant Rat Sulfotransferase 1A1 (SULT1A1) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-02890P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Rattus norvegicus (Rat) Sult1a1.

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Product Overview

Description	Recombinant Rat Sulfotransferase 1A1 (SULT1A1) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P17988
Target Symbol	SULT1A1
Synonyms	Sult1a1; St1a1; Sulfotransferase 1A1; ST1A1; EC 2.8.2.1; Aryl sulfotransferase; Aryl sulfotransferase IV; ASTIV; Minoxidil sulfotransferase; Mx-ST; PST-1; Phenol sulfotransferase; Sulfokinase; Tyrosine-ester sulfotransferase
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	MEFSRPPLVHVKGIPLIKYFAETIGPLQNFTAWPDDLLISTYPKSGTTWMSEILDMIYQGGKLEKCGRAPIYARVPFLEFKCPGVPSGLETLEETPAPRLLKTHLPLSLLPQSLLDQKVKVIYIARNAKDVVVSYYNFYNMAKLHPDPGTWDSFLENFMDGEVSYGSWYQHVKEWWELRHTHPVLYLFYEDIKENPKREIKKILEFLGRSLPEETVDSIVHHTSFKKMKENCMTNYTTIPTEIMDHNVSPFMRKGTTGDWKNTFTVAQNERFDAHYAKTMTDCDFKFRCEL
Expression Range	1-291aa
Protein Length	Full Length
Mol. Weight	53.9kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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 roles 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	KEGG: rno:83783 STRING: 10116.ENSRNOP00000026186 UniGene: Rn.1507
Tissue Specificity	Liver, kidney, heart and colon.

Gene Functions References

SULT1A1 is responsible for bioactivation of food genotoxicants 5-hydroxymethylfurfural and furfuryl alcohol. PMID: 25370010
Higher SULT1A1 levels were observed in rats as well as in humans exposed to high altitude, when compared to sea-level controls PMID: 26022216
Results suggest that the physiological functions of SULT1A1 in different brain regions can be affected by methamphetamine. PMID: 23026138
Data suggest that Sult1a1 and Sult2a1 can be induced in small intestinal mucosa by dietary factors (here, by various levels of caffeine); induction is gender specific and organ specific. Consumption of caffeine may enhance xenobiotic detoxification. PMID: 21721019
mechanistic studies on enzyme activity of purified recombinant Sult1a1 and Sult1a1 in viable liver slices after treatment with the same oxidants [1,1'-azobis(N,N-dimethylformamide); tert-butylhydroperoxide] and the same substrate (7-hydroxycoumarin) PMID: 22041107
Stp1 is important for appropriate regulation of Stk1 function, hemolysin activity, autolysis, and GBS virulence PMID: 22081606
there is a possible Cys modification mechanism for stress regulation of SULT1A1 PMID: 15351727

FAQs

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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.