Analytical Data
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Gene name
Carboxypeptidase E/CPE
- Application
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Alternative Names
rHuCarboxypeptidase E, His; Carboxypeptidase H; Enkephalin convertase; Prohormone-processing carboxypeptidase
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16870
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Expression Region
R42-S453
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AA Sequence
RLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKTYWEDNKNSLISYLEQIHRGVKGFVRDLQGNPIANATISVEGIDHDVTSAKDGDYWRLLIPGNYKLTASAPGYLAITKKVAVPYSPAAGVDFELESFSHHHHHH
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Protein Length
Partial
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Molecular Weight
57.0 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
Carboxypeptidase E (CPE) is a critical enzyme involved in the processing and secretion of peptide hormones and neuropeptides, playing a significant role in various physiological processes, including metabolism and neurodevelopment. CPE is localized primarily in neuroendocrine tissues and is responsible for the enzymatic removal of C-terminal basic residues from pro-peptides, thus activating biologically relevant peptides. Research into recombinant CPE has been driven by its potential implications in therapeutic applications and the understanding of neuroendocrine disorders. The expression and purification of recombinant CPE provide invaluable insights into its structure-function relationships and enzymatic mechanisms. Moreover, studying recombinant CPE can aid in exploring its role in diseases such as obesity and diabetes, where peptide hormone regulation is critical. The development of recombinant proteins has also facilitated the generation of specific inhibitors, opening avenues for drug development. Overall, the study of CPE not only enhances our comprehension of endocrine function and regulation but also paves the way for novel therapeutic strategies targeting a variety of metabolic and neuroendocrine conditions.
