TPST1 Protein (His tag)
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- Target See all TPST1 Proteins
- TPST1 (Tyrosylprotein Sulfotransferase 1 (TPST1))
- Protein Type
- Recombinant
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This TPST1 protein is labelled with His tag.
- Purpose
- Recombinant Human TPST1 Protein (His Tag)
- Sequence
- Gln 26-Glu 370
- Characteristics
- A DNA sequence encoding the human TPST1 (NP_003587.1) extracellular domain (Gln 26-Glu 370) was expressed, with a polyhistidine tag at the N-terminus.
- Purity
- > 80 % as determined by reducing SDS-PAGE.
- Endotoxin Level
- < 1.0 EU per μg as determined by the LAL method.
- Top Product
- Discover our top product TPST1 Protein
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from sterile PBS, pH 7.4
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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- Target
- TPST1 (Tyrosylprotein Sulfotransferase 1 (TPST1))
- Alternative Name
- TPST1 (TPST1 Products)
- Synonyms
- MGC82552 Protein, MGC97723 Protein, R75054 Protein, Tango13a Protein, TANGO13A Protein, fj54g11 Protein, wu:fj54g11 Protein, tyrosylprotein sulfotransferase 1 Protein, tyrosylprotein sulfotransferase 1 L homeolog Protein, protein-tyrosine sulfotransferase 1 Protein, TPST1 Protein, tpst1.L Protein, tpst1 Protein, Tpst1 Protein
- Background
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Background: Protein-tyrosine sulfotransferase 1, also known as Tyrosylprotein sulfotransferase 1 and TPST1, is a single-pass type I I membrane protein which belongs to the protein sulfotransferase family. Tyrosine O-sulfation is a common posttranslational modification of proteins in all multicellular organisms. This reaction is mediated by a Golgi enzyme activity called tyrosylprotein sulfotransferase (TPST) that catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to tyrosine residues within acidic motifs of polypeptides. Tyrosine O-sulfation has been shown to be important in protein-protein interactions in several systems. Tyrosine sulfation is mediated by one of two Golgi isoenzymes, called tyrosylprotein sulfotransferases (TPST-1 and TPST-2). A relatively small number of proteins are known to undergo tyrosine sulfation, including certain adhesion molecules, G-protein-coupled receptors, coagulation factors, serpins, extracellular matrix proteins, and hormones. TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion. TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262. TPST1 and TPST2 have distinct biological roles that may reflect differences in their macromolecular substrate specificity.
Synonym: TANGO13A
- Molecular Weight
- 41.7 kDa
- NCBI Accession
- NP_003587
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