Analytical Data
-
Gene name
QPCT
- Application
-
Alternative Names
QPCT；Glutaminyl-peptide cyclotransferase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q16769
-
Expression Region
29-361aa
-
AA Sequence
VSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL
-
Molecular Weight
41.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
QPCT (Quinone-Dependent Phenolic Compound Transporter) proteins are an emerging area of interest in molecular biology, particularly in the context of plant physiology and stress response. These proteins play a crucial role in the transport and metabolism of phenolic compounds, which are vital for plant defense mechanisms and overall resilience against biotic and abiotic stresses. The study of QPCT recombinant proteins allows researchers to elucidate the structure-function relationships and transport mechanisms of these proteins, providing insights into how they contribute to the biosynthesis of secondary metabolites that are important for plant growth and adaptation. Recent advancements in molecular cloning and protein expression techniques have facilitated the generation of purified QPCT proteins, enabling detailed biochemical characterization and functional assays. Understanding QPCT functions not only contributes to fundamental plant science but also holds potential applications in agriculture, such as improving crop resistance to diseases and enhancing the nutritional quality of plant products. As the demand for sustainable agricultural practices increases, research on QPCT may pave the way for innovative strategies to boost plant health and productivity.
