Recombinant Human Glutaminyl-Peptide Cyclotransferase (QPCT) Protein (His&Myc)

Name: Recombinant Human Glutaminyl-Peptide Cyclotransferase (QPCT) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06723P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Glutaminyl-Peptide Cyclotransferase (QPCT) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q16769
Target Symbol	QPCT
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	VSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL
Expression Range	29-361aa
Protein Length	Full Length of Mature Protein
Mol. Weight	41.8 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target 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 References	HGNC: 9753 OMIM: 607065 KEGG: hsa:25797 STRING: 9606.ENSP00000344829 UniGene: PMID: 28587659 these findings demonstrate a significant association between common single nucleotide polymorphism within QPCT gene and schizophrenia risk in a Han Chinese population. PMID: 26572640 the genetic risk of QPCT gene for schizophrenia also exists in the Han Chinese population. PMID: 26492838 observations provide evidence for an involvement of QC in Alzheimer's disease pathogenesis and cognitive decline by QC-catalyzed pGlu-Abeta formation PMID: 24164736 this study demonistrated that QPCT mRNAand protein from mononuclear cells correlated with theseverity of dementia. PMID: 23207485 Upregulation of QPCT expression is associated with thyroid carcinomas. PMID: 23183267 This study presents a first comparison of two mammalian QCs (human and mouse) containing typical, conserved post-translational modifications. PMID: 21671571 The resilts of this studt provided histopathological evidence for QC being a prerequisite for pE-Abeta pathology in vivo and further underline the therapeutic potential of QC inhibition in Alzheimer Disease. PMID: 21301857 Upon binding to PBD150, a large loop movement in gQC allows the inhibitor to be tightly held in its active site primarily by hydrophobic interactions. PMID: 21288892 This study demonstrated that glutaminyl cyclase expression and pE-Abeta formation in subcortical brain regions( Edinger-Westphal nucleus, locus coeruleus and nucleus basalis Meynert) affected in Alzheimer's disease. PMID: 20383514 Human isoQC proteins displayed a broad substrate specificity and preference for hydrophobic substrates, similar to the related QC. PMID: 19804409 Functional expression of human glutaminyl cyclase in Pichia pastoris reveals the presence of a disulfide bond with an important role in the stabilization of active protein structure. PMID: 12196024 human glutaminyl cyclase is a metal-dependent transferase PMID: 14522962 Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively PMID: 14680951 Genetic variations in QPCT are important factors affecting the bone mineral density of adult women that contribute to susceptibility for osteoporosis. PMID: 15231017 structure of human QC in free form and bound to a substrate and three imidazole-derived inhibitors PMID: 16135565 Our results suggest that QPCT may be the QTL gene at chromosome 2p for spine BMD variation in the Chinese population PMID: 17687619 combined steady-state enzyme kinetic and X-ray structural analyses of 11 single-mutation human QCs to investigate the roles of the H-bond network in catalysis PMID: 18072935 The computations outline the important role of Trp329 in helping the substrate binding process and stabilizing the cyclization transition state. PMID: 18470930 Golgi apparatus retention implies a "housekeeping" protein maturation machinery conducting glycosylation and pyroglutamyl formation. For these isoenzymes, apparently similar strategies evolved to retain the proteins in the Golgi complex. PMID: 18486145

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.