Analytical Data
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Gene name
carboxypeptidase
- Application
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Alternative Names
Allergen: Api m 9
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Species
Honeybee
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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
C9WMM5
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Expression Region
19-467aa
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Molecular Weight
67.6 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
Related Products
Protein Description
Carboxypeptidase is a key enzyme that catalyzes the hydrolysis of peptide bonds in proteins, playing a crucial role in protein digestion and processing. It is part of the metallocarboxypeptidase family, which is involved in various physiological processes, including inflammation and neural signaling. The recombinant expression of carboxypeptidase proteins has gained significant attention in biochemistry and molecular biology due to their potential applications in therapeutic and industrial contexts. Recombinant technology allows for the production of these enzymes in a controlled manner, often through the use of bacterial or eukaryotic expression systems. This approach enables researchers to produce enzymes with desired characteristics, such as improved stability or activity, facilitating the study of their biochemical properties and functions. Moreover, understanding the structure-function relationship of carboxypeptidases through recombinant forms can inform drug design and the development of biocatalysts for various industrial processes. Overall, the exploration of recombinant carboxypeptidase not only enhances our comprehension of enzymatic mechanisms but also holds promise for advancing medical and biotechnological innovations.
