Analytical Data
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Gene name
mep
- Application
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Alternative Names
(AfuMep)(Allergen Asp f 5)(Elastinolytic metalloproteinase mep)(Fungalysin mep)(allergen Asp f 5.0101)
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Species
Neosartorya fumigata
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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
P46075
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Expression Region
246-634aa
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Molecular Weight
49.6 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
MEP (methylerythritol phosphate) pathway proteins are critical elements in the biosynthesis of isoprenoids, a diverse group of compounds that play vital roles in various biological processes, including cell membrane integrity, hormone production, and photosynthesis. Unlike the mevalonate pathway, the MEP pathway is found in many bacteria, algae, and plastids of higher plants, making it an attractive target for research in drug development and metabolic engineering. Understanding the structure and function of MEP pathway proteins, such as DXP synthase and MEP synthase, is essential for elucidating the pathway's biochemical mechanisms. Furthermore, studies have shown that certain MEP pathway products have potential therapeutic applications, including antimicrobial agents and antimalarials derived from natural products. As the demand for sustainable and efficient biosynthesis of bioactive compounds increases, the exploration of MEP pathway proteins can pave the way for novel biotechnological applications and innovative drug discovery. Overall, the MEP pathway represents a crucial area of research with significant implications for both fundamental biology and applied sciences in the context of health and agriculture.
