Analytical Data
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Gene name
CPN1
- Application
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Alternative Names
CPN1；S11BH；Cytochrome P450 11B1. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15169
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Expression Region
21-458aa
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AA Sequence
VTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIPQVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA
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Molecular Weight
56.2 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
CPN1, also known as carboxypeptidase N, is a crucial enzyme involved in the processing of bioactive peptides and proteins, playing a significant role in various physiological processes, including inflammation and immune response. Its importance in the pathophysiology of diseases such as cancer and cardiovascular disorders has garnered increasing attention in recent years. Research on the recombinant expression of CPN1 enables the production of this enzyme in a controlled laboratory setting, facilitating detailed studies of its biochemical properties, interactions, and regulatory mechanisms. Moreover, recombinant CPN1 can serve as a valuable tool for therapeutic applications and biomarker discovery. Advances in protein engineering techniques, such as site-directed mutagenesis and fusion protein strategies, have further enhanced the ability to modify CPN1 for improved stability and activity. This research not only expands our understanding of CPN1's role in health and disease but also holds potential for the development of novel therapeutic approaches targeting pathways involving bioactive peptides. Through these studies, scientists aim to elucidate the functional implications of CPN1 in various biological contexts, paving the way for innovative strategies in disease management and treatment.
