Analytical Data
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Gene name
Carboxypeptidase B2/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
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9EQV9
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Expression Region
Gly164~His417
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Molecular Weight
33kDa
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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
Carboxypeptidase B2 (CPB2) is a crucial serine protease that plays a significant role in various physiological processes, particularly in the activation of proenzymes and the regulation of blood coagulation. This enzyme, primarily found in the pancreas, is responsible for cleaving basic amino acids from the C-terminus of peptides and proteins, thereby participating in protein maturation and degradation. The heterogeneity of CPB2 isoforms and their specific functions in different tissues has garnered attention in biomedical research, particularly concerning their implications in pathological conditions such as inflammation, cancer, and cardiovascular diseases. Given its importance, the recombinant production of CPB2 has become a focal point for researchers aiming to better understand its structure-function relationships, regulatory mechanisms, and potential therapeutic targets. The availability of recombinant CPB2 enables detailed studies into its enzymatic activity, inhibition, and interactions with other proteins, facilitating the development of novel biochemical tools and therapeutic agents. Advances in recombinant DNA technology have streamlined the expression and purification of CPB2, making it easier to investigate its properties in vitro. This research not only contributes to the fundamental understanding of proteolytic enzymes but also opens avenues for the development of CPB2-based diagnostics and therapeutics, further underscoring its relevance in clinical and biotechnological applications.
