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pMD18-T Simple Vector is a high-efficiency TA cloning vector constructed from pUC18, of which the initial multiple cloning sites (MCS) were destroyed. Thus the cDNA should be amplified by PCR with primers containing a restriction site for subclone. Competent cells appropriate for pUC18 are also appropriated for the Vector, e.g. JM109, DH5α, TOP10. The pMD18-T Simple Vector is 2.6kb in size. Selection of the plasmid in E. coli is conferred by the ampicillin resistance gene. The coding sequence was inserted by TA cloning at site 425.
The coding sequence can be amplified by PCR with M13-47 and RV-M primers.
|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 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|
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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.