Recombinant Human Protein-Tyrosine Sulfotransferase 2 (TPST2) Protein (His-SUMO)

Name: Recombinant Human Protein-Tyrosine Sulfotransferase 2 (TPST2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09975P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Human Protein-Tyrosine Sulfotransferase 2 (TPST2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O60704
Target Symbol	TPST2
Synonyms	EC 2.8.2.20; Protein tyrosine sulfotransferase 2; Protein-tyrosine sulfotransferase 2; TANGO13B; TPST-2; Tpst2; TPST2_HUMAN; Transport and golgi organization 13 homolog B; Tyrosylprotein phosphotransferase 2; Tyrosylprotein sulfotransferase 2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	QQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLKGYFQVNQNSTSSHLGSS
Expression Range	26-377aa
Protein Length	Full Length of Mature Protein
Mol. Weight	55.3kDa
Research Area	Cardiovascular
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	Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
Subcellular Location	Golgi apparatus membrane; Single-pass type II membrane protein.
Protein Families	Protein sulfotransferase family
Database References	HGNC: 12021 OMIM: 603126 KEGG: hsa:8459 STRING: 9606.ENSP00000339813 UniGene: Hs.632768
Tissue Specificity	Widely expressed.

Gene Functions References

Using a quantum mechanics protocol of alanine scanning, the study identified unequivocally the role of the amino acids involved in the TPST-2 catalytic mechanism. PMID: 26108987
the first crystal structure of the human tyrosylprotein sulfotransferase isoform 2 complexed with a substrate peptide (C4P5Y3) derived from complement C4 and 3'-phosphoadenosine-5'-phosphate at 1.9 A resolution, is reported. PMID: 23481380
The p.R153H variant was found in a family with hereditary pancreatitis; however, it did not segregate with the disease. PMID: 20460947
Shear stress-dependent upregulation of TPST2 in human endothelium is mediated by a tyrosine kinase-dependent pathway PMID: 12056800
Tyrosine sulfation of CCR5 N-terminal peptide follows a discrete pattern and temporal sequence PMID: 12169668
The kinetic parameters of tyrosylprotein sulfotransferase-1 and -2, catalyzing tyrosine sulfation of CCR8 peptides, were determined using liquid chromatography electrospray ionisation mass spectrometry. PMID: 18672380

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.