Analytical Data
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Gene name
CPN2
- Application
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Alternative Names
CPN2；ACBP；Carboxypeptidase N subunit 2
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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
P22792
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Expression Region
22-545aa
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AA Sequence
CPMGCDCFVQEVFCSDEELATVPLDIPPYTKNIIFVETSFTTLETRAFGSNPNLTKVVFLNTQLCQFRPDAFGGLPRLEDLEVTGSSFLNLSTNIFSNLTSLGKLTLNFNMLEALPEGLFQHLAALESLHLQGNQLQALPRRLFQPLTHLKTLNLAQNLLAQLPEELFHPLTSLQTLKLSNNALSGLPQGVFGKLGSLQELFLDSNNISELPPQVFSQLFCLERLWLQRNAITHLPLSIFASLGNLTFLSLQWNMLRVLPAGLFAHTPCLVGLSLTHNQLETVAEGTFAHLSNLRSLMLSYNAITHLPAGIFRDLEELVKLYLGSNNLTALHPALFQNLSKLELLSLSKNQLTTLPEGIFDTNYNLFNLALHGNPWQCDCHLAYLFNWLQQYTDRLLNIQTYCAGPAYLKGQVVPALNEKQLVCPVTRDHLGFQVTWPDESKAGGSWDLAVQERAARSQCTYSNPEGTVVLACDQAQCRWLNVQLSPQQGSLGLQYNASQEWDLRSSCGSLRLTVSIEARAAGP
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Molecular Weight
59.2 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
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Protein Description
CPN2, also known as cytosolic peptidase N2, is a key enzyme involved in the processing of intracellular peptides, playing a crucial role in various physiological and pathological processes, including immune response and protein degradation. Its function is vital for maintaining cellular homeostasis and regulating the levels of bioactive peptides that can influence cell signaling pathways. Recent studies have highlighted the potential of CPN2 as a therapeutic target for various diseases, including cancer and neurodegenerative disorders, where peptide misfolding or aberrant peptide levels contribute to disease progression. The recombinant expression of CPN2 has garnered significant interest, enabling researchers to produce large quantities of the protein for in-depth functional analysis, structural studies, and the development of inhibitors or modulators. This research not only enhances the understanding of CPN2's biological role but also paves the way for innovative therapeutic strategies targeting peptide-mediated pathways. As an evolving field, investigations into CPN2's structure-function relationships and its interactions with substrates and other molecular partners remain critical for unlocking its full potential in medicine and biotechnology.
