Analytical Data
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Gene name
Aminopeptidase P1
- Application
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Alternative Names
Aminoacylproline aminopeptidaseCytosolic aminopeptidase PSoluble aminopeptidase P ;sAmpX-Pro aminopeptidase 1X-prolyl aminopeptidase 1, soluble
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NQW7
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Expression Region
2-623aa
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Molecular Weight
85.8 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
Aminopeptidase P1 (AP-P1) is a pivotal enzyme involved in the metabolism of biologically active peptides, particularly in the hydrolysis of N-terminal amino acids. The enzyme plays an essential role in various physiological processes, including blood pressure regulation and neurotransmitter activity, by modulating peptide levels in the body. Dysregulation of aminopeptidase P has been implicated in several pathological conditions, including hypertension and neurodegenerative diseases. Recent advancements in genetic engineering and recombinant protein technology have enabled the production of AP-P1 in heterologous systems, providing insights into its structure-function relationships and catalytic mechanisms. The recombinant version of this protein has been instrumental in studying its kinetic properties, substrate specificity, and potential as a therapeutic target. Understanding the molecular dynamics of AP-P1 may pave the way for the design of specific inhibitors or modulators that could have significant implications for treating diseases associated with peptide metabolism. Furthermore, the characterization of recombinant AP-P1 can contribute to developing diagnostic tools for monitoring related health conditions. This research holds the promise for not only elucidating the biological roles of AP-P1 but also enhancing our capability to manipulate it for therapeutic benefits.
