Analytical Data
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Gene name
XPNPEP3
- Application
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Alternative Names
XPNPEP3；Xaa-Pro aminopeptidase 3
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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
Q9NQH7
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Expression Region
1-507aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMPWLLSAPKLVPAVANVRGLSGCMLCSQRR YSLQPVPERRIPNRYLGQPSPFTHPHLLRPGEVTPGLSQVEYALRRHKLM SLIQKEAQGQSGTDQTVVVLSNPTYYMSNDIPYTFHQDNNFLYLCGFQEP DSILVLQSLPGKQLPSHKAILFVPRRDPSRELWDGPRSGTDGAIALTGVD EAYTLEEFQHLLPKMKAETNMVWYDWMRPSHAQLHSDYMQPLTEAKAKSK NKVRGVQQLIQRLRLIKSPAEIERMQIAGKLTSQAFIETMFTSKAPVEEA FLYAKFEFECRARGADILAYPPVVAGGNRSNTLHYVKNNQLIKDGEMVLL DGGCESSCYVSDITRTWPVNGRFTAPQAELYEAVLEIQRDCLALCFPGTS LENIYSMMLTLIGQKLKDLGIMKNIKENNAFKAARKYCPHHVGHYLGMDV HDTPDMPRSLPLQPGMVITIEPGIYIPEDDKDAPEKFRGLGVRIEDDVVV TQDSPFILSADCPKEMNDIEQICSQASLEHHHHHH
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Molecular Weight
60 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
XPNPEP3, or X-Prolyl Aminopeptidase 3, is an essential enzyme that plays a crucial role in protein metabolism and regulation, particularly in the hydrolysis of N-terminal proline-containing peptides. Its importance has been increasingly recognized in various biological processes, including cell signaling, metabolic regulation, and immune response. Recent studies have linked XPNPEP3 to several physiological and pathological conditions, such as cancer, cardiovascular diseases, and neurodegenerative disorders. This has spurred interest in understanding its structure, function, and potential as a therapeutic target. Researchers aim to produce recombinant XPNPEP3 to elucidate its enzymatic mechanisms, explore its interactions with other biomolecules, and investigate its role in disease development. By generating recombinant protein through expression systems, scientists can obtain large quantities of XPNPEP3 for biochemical assays and structural studies. This research could pave the way for novel treatments targeting XPNPEP3-related pathways and contribute to the broader understanding of proline metabolism in human health and disease. The exploration of XPNPEP3 not only enhances our comprehension of enzyme function in cellular environments but also holds promise for biomedical applications, making it a significant focus in current biomedical research.
