Recombinant Human Glutaminyl-peptide cyclotransferase(QPCT)


In Stock
Code CSB-EP019135HU
Product Type Recombinant Protein
Size US$1726Purchase it in Cusabio online store
(only available for customers from the US)
Uniprot No. Q16769
Relevance Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP019135HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) QPCT.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP019135HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) QPCT.
Storage Buffer Tris-based buffer,50% glycerol
Alias Glutaminyl cyclase ;QC ;sQCGlutaminyl-tRNA cyclotransferaseGlutamyl cyclase ;EC
Species Homo sapiens (Human)
Purity Greater than 90% as determined by SDS-PAGE.
Sequence VSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL
Research Area Neuroscience
Source E.coli
Gene Names QPCT
Expression Region 29-361aa
Tag Info N-terminal 6xHis-SUMO-tagged
Mol. Weight 53.9kDa
Protein Description Full Length of Mature Protein
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Function Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Subcellular Location Secreted
Protein Families Glutaminyl-peptide cyclotransferase family
Database Links

HGNC: 9753

OMIM: 607065

KEGG: hsa:25797

STRING: 9606.ENSP00000344829

UniGene: Hs.79033

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