|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Human TPST1 ORF mammalian expression plasmid, C-GFPSpark tag||HG11258-ACG|
|Human TPST1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG11258-ACR|
|Human TPST1 ORF mammalian expression plasmid, C-Flag tag||HG11258-CF|
|Human TPST1 ORF mammalian expression plasmid, C-His tag||HG11258-CH|
|Human TPST1 ORF mammalian expression plasmid, C-Myc tag||HG11258-CM|
|Human TPST1 ORF mammalian expression plasmid, C-HA tag||HG11258-CY|
|Human TPST1 Gene cDNA clone plasmid||HG11258-M|
|Human TPST1 ORF mammalian expression plasmid, N-Flag tag||HG11258-NF|
|Human TPST1 ORF mammalian expression plasmid, N-His tag||HG11258-NH|
|Human TPST1 ORF mammalian expression plasmid, N-Myc tag||HG11258-NM|
|Human TPST1 ORF mammalian expression plasmid, N-HA tag||HG11258-NY|
|Human TPST1 natural ORF mammalian expression plasmid||HG11258-UT|
|Learn more about expression Vectors|
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.