Analytical Data
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Gene name
pepA
- Application
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Alternative Names
pepA；Pepsin A-5
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Species
E.coli
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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
P68768
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Expression Region
1-503aa
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AA Sequence
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG QGSQNESLMS VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG ATGRPVALLA QFLLNRAGFN GEE
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Molecular Weight
54.8 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
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Protein Description
PepA, or aminopeptidase A, is an enzyme that plays a critical role in various physiological processes, including protein turnover and regulation of peptide hormones. Found in both prokaryotic and eukaryotic organisms, PepA is involved in cleaving amino acids from the N-terminus of peptides, thus contributing to protein digestion and maturation of bioactive peptides. The study of recombinant PepA has gained significant attention due to its potential applications in biotechnology and medicine. Understanding the structure, function, and regulation of this enzyme can provide insights into metabolic pathways and aid in the development of pharmaceuticals targeting metabolic disorders or cancer. Furthermore, recombinant PepA can be utilized in industrial applications for peptide synthesis, protein purifications, and as a tool for studying peptide interactions. By overexpressing and purifying PepA in model organisms or cell systems, researchers can investigate its enzymatic properties, substrate specificity, and inhibition profiles. This knowledge not only enhances our understanding of peptide metabolism but also opens avenues for engineering PepA variants with improved properties for specific applications. Overall, the study of recombinant PepA serves as a cornerstone for advancing our comprehension of proteolytic enzymes and their broader implications in health and disease.
