Analytical Data
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Gene name
mnp2c
- Application
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Alternative Names
/
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Species
Lentinula edodes
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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
B5U994
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Expression Region
21-377aa
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Molecular Weight
42.6 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
MNP2C, a specific recombinant protein, has garnered significant attention in the research community due to its potential applications in various fields, including biotechnology and medicine. Initially, studies focusing on the MNP2C protein were motivated by its structural similarities to other integral membrane proteins that play crucial roles in cellular signaling and transport mechanisms. Researchers recognized that understanding the biophysical properties and functional characteristics of MNP2C could provide insights into its role in cellular processes and its interactions with other biomolecules. Moreover, the recombinant expression of MNP2C in various host systems has enabled the generation of sufficient quantities of this protein, facilitating detailed biochemical analyses and functional assays. Such investigations have highlighted MNP2C's potential in therapeutic applications, including drug delivery systems and the development of novel biomaterials. Additionally, the exploration of MNP2C's role in disease mechanisms has opened new avenues for research, particularly in understanding cellular responses to stress and signaling pathways involved in cancer and other disorders. As a result, MNP2C has emerged as a pivotal subject in studies aimed at elucidating complex biological systems, with promising prospects for innovation in health and disease management.
