|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Rhesus TPST1 ORF mammalian expression plasmid, C-GFPSpark tag||CG90690-ACG|
|Rhesus TPST1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||CG90690-ACR|
|Rhesus TPST1 ORF mammalian expression plasmid, C-Flag tag||CG90690-CF|
|Rhesus TPST1 ORF mammalian expression plasmid, C-His tag||CG90690-CH|
|Rhesus TPST1 ORF mammalian expression plasmid, C-Myc tag||CG90690-CM|
|Rhesus TPST1 ORF mammalian expression plasmid, C-HA tag||CG90690-CY|
|Rhesus TPST1 Gene cDNA clone plasmid||CG90690-G|
|Rhesus TPST1 ORF mammalian expression plasmid, N-Flag tag||CG90690-NF|
|Rhesus TPST1 ORF mammalian expression plasmid, N-His tag||CG90690-NH|
|Rhesus TPST1 ORF mammalian expression plasmid, N-Myc tag||CG90690-NM|
|Rhesus TPST1 ORF mammalian expression plasmid, N-HA tag||CG90690-NY|
|Rhesus TPST1 natural ORF mammalian expression plasmid||CG90690-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.