Analytical Data
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Gene name
mipA
- Application
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Alternative Names
mipA；yeaF；MltA-interacting Protein
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Species
Human
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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
P0A908
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Expression Region
23-248aa
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AA Sequence
EGKFSLGAGVGVVEHPYKDYDTDVYPVPVINYEGDNFWFRGLGGGYYLWNDATDKLSITAYWSPLYFKAKDSGDHQMRHLDDRKSTMMAGLSYAHFTQYGYLRTTLAGDTLDNSNGIVWDMAWLYRYTNGGLTVTPGIGVQWNSENQNEYYYGVSRKESARSGLRGYNPNDSWSPYLELSASYNFLGDWSVYGTARYTRLSDEVTDSPMVDKSWTGLISTGITYKF
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Molecular Weight
33.1 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
MipA, a member of the Mip protein family, is a highly conserved protein that plays a crucial role in the cellular processes of various organisms, including bacteria, plants, and humans. Initially identified in the context of bacterial stress responses, MipA has garnered attention for its involvement in maintaining cellular integrity under adverse conditions, such as nutrient deprivation and environmental stress. Research indicates that MipA possesses unique structural and functional properties that allow it to interact with other proteins and cellular components, facilitating the regulation of important pathways such as cell signaling and metabolism. Advances in recombinant protein technology have made it feasible to produce MipA in significant quantities, providing researchers with the tools necessary to explore its functional mechanisms in detail. This has opened new avenues for investigating MipA's potential applications in biotechnology and medicine, including the development of novel therapeutic strategies and molecular tools. As our understanding of MipA enhances, further studies may illuminate its potential roles in pathogenesis, immunity, and cellular development, positioning MipA as a promising target for future research endeavors and innovative applications.
