Recombinant Mouse Glutaminyl-Peptide Cyclotransferase (QPCT) Protein (His)

Name: Recombinant Mouse Glutaminyl-Peptide Cyclotransferase (QPCT) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07882P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Glutaminyl-Peptide Cyclotransferase (QPCT) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9CYK2
Target Symbol	QPCT
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AWTQEKNHHQPAHLNSSSLQQVAEGTSISEMWQNDLRPLLIERYPGSPGSYSARQHIMQRIQRLQAEWVVEVDTFLSRTPYGYRSFSNIISTLNPEAKRHLVLACHYDSKYFPRWDSRVFVGATDSAVPCAMMLELARALDKKLHSLKDVSGSKPDLSLRLIFFDGEEAFHHWSPQDSLYGSRHLAQKMASSPHPPGSRGTNQLDGMDLLVLLDLIGAANPTFPNFFPKTTRWFNRLQAIEKELYELGLLKDHSLERKYFQNFGYGNIIQDDHIPFLRKGVPVLHLIASPFPEVWHTMDDNEENLHASTIDNLNKIIQVFVLEYLHL
Expression Range	36-362aa
Protein Length	Full Length of Mature Protein
Mol. Weight	41.6 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.
Subcellular Location	Secreted.
Protein Families	Glutaminyl-peptide cyclotransferase family
Database References	KEGG: mmu:70536 STRING: 10090.ENSMUSP00000038732 UniGene: Mm.293870

Gene Functions References

Authors identified a placenta-specific imprinted gene Qpct. Results show that Qpct is widely expressed during early embryonic development and can be detected in the telencephalon, midbrain, and rhombencephalon at E9.5-E11.5. PMID: 26447138
co-regulation of the enzyme glutaminyl cyclase and its substrate TRH was reflected by a co-induction of both proteins in reactive astrocytes in proximity of Abeta deposits PMID: 25446989
This study provide a thorough comparative characterization of the glutaminyl cyclases QC and isoQC in defined brain regions of different inbred and outbred mouse strains PMID: 24886834
This study presents a first comparison of two mammalian QCs (mouse and human)containing typical, conserved post-translational modifications. PMID: 21671571
Glutaminyl cyclase in a mouse knockout model has a role in hypothyroidism but not hypogonadism PMID: 21330373
QC is crucial for modulating AbetapE3-42 levels in vivo and prove on a genetic base the concept that reduction of QC activity is a promising new therapeutic approach for AD. PMID: 21148560
Murine isoQC proteins displayed a broad substrate specificity and preference for hydrophobic substrates, similar to the related QC. PMID: 19804409
Results describe the expression of glutaminyl cyclase throughout the mouse brain during early postnatal development. PMID: 19699792
The observations of this study indicated that brain ischemia might be a pathogenic factor of alzheimer disease through increasing BACE1, cathepsin B, and glutaminyl cyclase. PMID: 19809370
QC is a zinc-dependent catalyst PMID: 16201766

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.