Analytical Data
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Gene name
Aminopeptidase A
- Application
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Alternative Names
CD249; GluAP; gp160; ATA; EAP; AP-A; Aminopeptidase A; Glutamyl Aminopeptidase
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 97% as determined by reducing SDS-PAGE.
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Uniprot
P50123
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Expression Region
Gly409~Ala624
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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
Aminopeptidase A (APA) is an important enzyme involved in the metabolism of neuropeptides and angiotensin, playing a crucial role in blood pressure regulation and neuronal signaling. Its primary function is to catalyze the cleavage of N-terminal amino acids from peptides, thus modulating bioactive peptide levels in various physiological processes. Research into recombinant APA has gained momentum due to its potential therapeutic implications, particularly in the context of hypertension and neurodegenerative diseases. The production of recombinant APA allows for a more detailed study of its enzymatic mechanisms, substrate specificity, and regulatory pathways. Additionally, achieving high yields of functional protein is essential for structural and functional analyses, facilitating insights into its catalytic activity and interactions with inhibitors. The development of robust expression systems has enabled scientists to produce APA in sufficient quantities for extensive characterizations, paving the way for the design of targeted inhibitors that could serve as novel therapeutic agents. Furthermore, understanding the molecular structure and dynamics of recombinant APA can provide valuable information for drug discovery efforts aimed at treating conditions associated with dysregulated peptide metabolism. Overall, the study of recombinant aminopeptidase A holds significant promise for advancing our understanding of its biological functions and potential applications in medicine.
