Analytical Data
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Gene name
QPCTL
- Application
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Alternative Names
Golgi-resident glutaminyl-peptide cyclotransferaseisoQC ;gQC
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NXS2
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Expression Region
212-382aa
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Molecular Weight
35.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
QPCTL (Qualitative Peptide C-Terminal Lipeptide) is an essential enzyme involved in post-translational modifications within cellular systems. It plays a critical role in the maturation of various peptides, impacting their biological functions and interactions. Extensive research on QPCTL has revealed its significance in processes such as protein degradation, signaling pathways, and cellular metabolism. The enzyme catalyzes the removal of C-terminal residues from peptide substrates, thereby influencing protein activity and stability. Understanding the molecular structure and functional mechanisms of QPCTL can provide insights into its potential implications in diseases like cancer, neurodegeneration, and metabolic disorders. Studies have shown that dysregulation of QPCTL activity is linked to various pathological conditions, making it a viable target for therapeutic interventions. Given its vital role in protein dynamics, there is a growing interest in the recombinant expression and purification of QPCTL for further characterization and potential drug development. Advancements in recombinant protein technology facilitate the production of high-quality QPCTL, enabling researchers to explore its enzymatic properties, substrate specificity, and potential as a biomarker for disease states. As the field evolves, investigations into QPCTL's interactions with other cellular components will enhance our understanding of its regulatory role and pave the way for novel therapeutic strategies exploiting its unique attributes.
