Analytical Data
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Gene name
MT1F
- Application
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Alternative Names
Metallothionein-IF ;MT-IF
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04733
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Expression Region
1-59aa
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Molecular Weight
7.9 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
The MT1F recombinant protein has garnered significant attention in the field of molecular biology and biotechnology due to its potential applications in cancer research and therapy. MT1F, a member of the metallothionein (MT) family, is characterized by its high cysteine content, which allows it to bind metal ions and play a crucial role in metal ion homeostasis, detoxification, and oxidative stress response. Its expression has been linked to various physiological processes and pathologies, notably in cancer, where altered levels may influence tumor development and progression. Researchers are particularly interested in the functional characterization of MT1F to elucidate its specific roles in cellular mechanisms and its potential as a biomarker for cancer diagnostics or as a therapeutic target. The recombinant production of MT1F facilitates detailed biochemical studies, enabling the examination of its structure-function relationship and interactions with other cellular components. Furthermore, understanding the regulation of MT1F expression could provide insights into novel therapeutic strategies aimed at modulating its activity to combat cancer effectively. Overall, the exploration of MT1F recombinant protein presents an exciting opportunity to advance our understanding of metallothioneins and their implications in health and disease.











