Analytical Data
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Gene name
fpaP
- Application
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Alternative Names
Prolyl aminopeptidase (PAP)
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Species
Elizabethkingia meningoseptica
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O05420
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Expression Region
1-298aa
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Molecular Weight
41.6 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
The research on FpaP recombinant protein has garnered significant interest due to its potential applications in biotechnology and medicine. FpaP, a member of the family of preproteins, is known for its role in the protein translocation across membranes in various prokaryotic systems. Understanding its structure and function can shed light on the mechanisms of protein secretion, which is crucial for both basic biological research and industrial applications. Recent studies have indicated that FpaP may serve as a target for the development of novel antimicrobial agents, given its unique features in bacterial survival and pathogenicity. Furthermore, recombinant expression of FpaP in heterologous systems allows for detailed investigations into its biochemical properties, facilitating the exploration of its interactions with other proteins and its role in the development of bacterial biofilms. As antibiotic resistance continues to be a major global health challenge, FpaP presents an attractive candidate for research aimed at overcoming these issues, highlighting the importance of recombinant protein studies in developing new therapeutic strategies. Overall, the exploration of FpaP and its recombinant forms promises to expand our understanding of microbial physiology and pave the way for innovative solutions in fighting infectious diseases.
