Analytical Data
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Gene name
pepF
- Application
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Alternative Names
pepF; MPN_197; MP634Oligoendopeptidase F homolog; EC 3.4.24.-
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Species
Mycoplasma pneumoniae
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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
P54125
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Expression Region
1-210aa
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Molecular Weight
40.6 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
Related Products
Protein Description
PepF is a recombinant protein that has garnered significant attention in the field of biotechnology and molecular biology due to its unique enzymatic properties and potential applications. Originally identified as a peptidase involved in the degradation of peptides, PepF plays a crucial role in various biological processes, including protein turnover and metabolic regulation. Its ability to cleave specific peptide bonds makes it an attractive candidate for industrial applications, such as in food processing and the development of therapeutic agents. Moreover, the study of PepF has implications for understanding disease mechanisms, particularly those related to protein misfolding and aggregation, which are implicated in various disorders like Alzheimer's disease. Researchers have focused on the structural and functional characterization of PepF to elucidate its catalytic mechanism and improve its stability and activity through protein engineering techniques. The advancement in recombinant DNA technology has facilitated the production of PepF in host organisms, enabling large-scale synthesis for research and industrial purposes. As a result, ongoing studies aim to optimize PepF's production, enhance its functional properties, and explore its potential as a biocatalyst in different applications, paving the way for innovative solutions in medicine, agriculture, and biotechnology.
