Analytical Data
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Gene name
CPB2
- Application
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Alternative Names
TAFI; CPU; PCPB; Thrombin Activatable Fibrinolysis Inhibitor; Plasma Carboxypeptidase B; Carboxypeptidase U
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96IY4
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Expression Region
Glu138~Val386
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Molecular Weight
32kDa
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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
Related Products
Protein Description
CPB2 is a serine protease produced by certain parasitic organisms, notably those within the Phylum Nematoda, which play significant roles in host-parasite interactions. The understanding of CPB2 has gained attention due to its potential impact on both the virulence of these parasites and the immune response of the host. Research indicates that CPB2 may facilitate tissue invasion and evasion of host defense mechanisms, thus contributing to the pathogenicity of parasitic infections. As such, the characterization and functional study of CPB2 recombinant proteins have become pivotal in immunological and therapeutic research. Investigating the structure and function of CPB2 can provide insights into its enzymatic activity, substrate specificity, and interaction with host molecules. Furthermore, recombinant CPB2 proteins are being explored as potential vaccine candidates or therapeutic targets, meaning that understanding their properties could aid in the development of effective strategies for controlling parasitic diseases. The study of CPB2 not only enriches the existing knowledge of parasitic biology but also holds promise for advancing medical interventions against infections that pose significant global health challenges.
