Analytical Data
-
Gene name
CPQ
- Application
-
Alternative Names
CPQ；LCH1；PGCP；Carboxypeptidase Q
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y646
-
Expression Region
1-472aa
-
AA Sequence
MKFLIFAFFGGVHLLSLCSGKAICKNGISKRTFEEIKEEIASCGDVAKAIINLAVYGKAQNRSYERLALLVDTVGPRLSGSKNLEKAIQIMYQNLQQDGLEKVHLEPVRIPHWERGEESAVMLEPRIHKIAILGLGSSIGTPPEGITAEVLVVTSFDELQRRASEARGKIVVYNQPYINYSRTVQYRTQGAVEAAKVGALASLIRSVASFSIYSPHTGIQEYQDGVPKIPTACITVEDAEMMSRMASHGIKIVIQLKMGAKTYPDTDSFNTVAEITGSKYPEQVVLVSGHLDSWDVGQGAMDDGGGAFISWEALSLIKDLGLRPKRTLRLVLWTAEEQGGVGAFQYYQLHKVNISNYSLVMESDAGTFLPTGLQFTGSEKARAIMEEVMSLLQPLNITQVLSHGEGTDINFWIQAGVPGASLLDDLYKYFFFHHSHGDTMTVMDPKQMNVAAAVWAVVSYVVADMEEMLPRS
-
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
Cystic Fibrosis (CF) is a genetic disorder caused by mutations in the CFTR gene, leading to dysfunctional chloride channels and resulting in thick mucus accumulation in organs, particularly the lungs and pancreas. One promising therapeutic approach is the use of CPQ (Cystic Fibrosis Protein Quality) recombinant proteins to correct the misfolding and trafficking of the CFTR protein. Research has focused on understanding the structure and function of these proteins, which can potentially restore the normal activity of CFTR at the cellular level. Various strategies, including the development of small molecules and biologics, have been explored to enhance the stability and folding of the misfolded CFTR protein, thereby improving chloride ion transport and alleviating the symptoms of CF. Recent advancements in protein engineering and biotechnology have opened new avenues for the production of CPQ recombinant proteins with enhanced efficacy and reduced side effects. Ongoing studies aim to optimize these proteins for better delivery mechanisms and augmented therapeutic outcomes in CF patients, fostering hope for more effective treatments that address the root cause of the disease rather than just its symptoms. The integration of multidisciplinary approaches, including molecular biology, biochemistry, and pharmacology, remains crucial in the quest to develop novel interventions for CF, with CPQ recombinant proteins representing a significant focus of current research efforts.
