|Datasheet||Specific References||Reviews||Related Products||Protocols|
|ORF Clone of glutaminyl-peptide cyclotransferase DNA.|
|GCT, QC, sQC, QPCT|
|Identical with the Gene Bank Ref. ID sequence.|
|Whatman FTA elute card (Cat: WB120410) contains 5-10 μg of plasmid.|
|The Whatman FTA elute card can be stored at room temperature for three months under dry condition.|
The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Human QPCT Gene cDNA Clone (full-length ORF Clone), expression ready, FLAG-tagged||HG13752-G-F|
|Human QPCT Gene cDNA Clone (full-length ORF Clone), expression ready, His-tagged||HG13752-G-H|
|Human QPCT Gene cDNA Clone (full-length ORF Clone), expression ready, Myc-tagged||HG13752-G-M|
|Human QPCT Gene cDNA Clone (full-length ORF Clone), expression ready, untagged||HG13752-G-N|
|Human QPCT Gene cDNA Clone (full-length ORF Clone), expression ready, HA-tagged||HG13752-G-Y|
|Product name||Product name|
Glutaminyl cyclase, also known as QPCT, can promote the N-terminal cyclization reaction of N-terminal pyroglutamate(pGlu). The pGlu formation from its glutaminyl precursor is required in the maturation of numerous bioactive peptides, while the aberrant formation of pGlu may be related to several pathological processes, such as osteoporosis and amyloidotic diseases. Glutaminyl cyclase's structure reveals an alpha/beta scaffold akin to that of two-zinc exopeptidases but with several insertions and deletions, particularly in the active-site region. Glutaminyl cyclase's amino acid sequence of this enzyme is 86% identical to that of bovine glutaminyl cyclase. It is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides.