Analytical Data
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Gene name
MIA
- Application
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Alternative Names
MIA;Melanoma-derived growth regulatory 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
Q16674
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Expression Region
25-131aa
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AA Sequence
GPMPKLADRK LCADQECSHP ISMAVALQDY MAPDCRFLTI HRGQVVYVFS KLKGRGRLFW GGSVQGDYYG DLAARLGYFP SSIVREDQTL KPGKVDVKTD KWDFYCQ
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Molecular Weight
12.1 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
Related Products
Protein Description
MIA (Melanoma Inhibitory Activity) is a protein originally identified in the context of melanoma, a type of skin cancer, known for its role in tumor progression and metastasis. Research into MIA has revealed its potential significance not only as a biomarker for melanoma diagnosis but also as a therapeutic target due to its involvement in cell survival and proliferation pathways. MIA protein is secreted by melanoma cells, and its elevated levels in the serum of patients have been correlated with poor prognosis and advanced disease stages. Moreover, MIA has been shown to interact with various cellular processes, including the regulation of extracellular matrix components and immune evasion mechanisms. As a result, the study of MIA recombinant proteins has gained momentum in recent years, aiming to elucidate its structural and functional properties, as well as its potential applications in diagnostics and targeted therapies. Researchers are exploring the use of recombinant MIA in developing novel therapeutic strategies, including antibody-based approaches and targeted delivery systems, to improve treatment outcomes for melanoma patients. This growing interest underscores the importance of understanding MIA at a molecular level to harness its diagnostic and therapeutic potential effectively.
