Analytical Data
-
Gene name
MIA
- Application
-
Alternative Names
MIA；Melanoma-derived growth regulatory Protein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q16674
-
Expression Region
25-131aa
-
AA Sequence
GPMPKLADRK LCADQECSHP ISMAVALQDY MAPDCRFLTI HRGQVVYVFS KLKGRGRLFW GGSVQGDYYG DLAARLGYFP SSIVREDQTL KPGKVDVKTD KWDFYCQ
-
Molecular Weight
12.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 pivotal protein initially identified for its role in melanoma cell biology. Its expression has been linked to tumor progression and metastasis, making it a subject of intense study in cancer research. MIA is known to influence cell adhesion, migration, and interaction with the extracellular matrix, contributing to the aggressive nature of melanoma. Beyond melanoma, its expression has been observed in various other malignancies, suggesting a broader role in oncogenic processes. The reconstitution of MIA in research settings enables the exploration of its structural and functional characteristics, revealing insights into its mechanisms of action. This includes its potential as a biomarker for diagnosis and prognosis in cancer patients. Additionally, recombinant MIA proteins can be utilized in therapeutic contexts, where they may assist in the development of targeted treatments. The ongoing investigation of MIA not only enhances our understanding of melanoma biology but also underscores the importance of protein interactions in cancer progression and metastasis.
