Analytical Data
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Gene name
LNPEP
- Application
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Alternative Names
CAP; PLAP; OTASE; IRAP; Oxytocinase; Insulin-regulated membrane aminopeptidase; Insulin-responsive aminopeptidase; Placental leucine aminopeptidase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UIQ6
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Expression Region
Leu782~Leu1025
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Molecular Weight
28kDa
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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
LNPEP, or leucine aminopeptidase, is an essential enzyme involved in the regulation of various physiological processes, including protein metabolism and immune responses. Its role in processing peptides by removing N-terminal leucine residues makes it vital for the maturation of bioactive peptides and hormones. Research into LNPEP has gained momentum due to its implications in various diseases, particularly those related to metabolic and neurodegenerative disorders. Studies have demonstrated that dysregulation of LNPEP activity can lead to abnormal peptide accumulation and contribute to pathological conditions such as Alzheimer's disease and hypertension. As a result, the development and characterization of recombinant LNPEP are essential for understanding its biological functions and therapeutic potential. Through recombinant DNA technology, researchers can produce large quantities of LNPEP, enabling detailed biochemical studies and high-throughput screening for potential inhibitors or modulators. This work not only aids in elucidating the enzyme's mechanisms but also identifies LNPEP as a potential biomarker and therapeutic target. Given the enzyme's significance in maintaining cellular homeostasis and its involvement in disease mechanisms, continued exploration into recombinant LNPEP may yield valuable insights into novel treatment strategies and therapeutic applications.
