Analytical Data
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Gene name
DMT1
- Application
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Alternative Names
DMT1；DMT1；Doublesex- and mab-3-related transcription factor 1
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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
Q9UQN3
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Expression Region
2-213aa
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AA Sequence
ASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
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Molecular Weight
50.8kDa
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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
DMT1, or Divalent Metal Transporter 1, is a vital protein that facilitates the uptake of divalent metal ions, including iron, manganese, and cobalt, across cellular membranes. Its role is particularly crucial in maintaining metal homeostasis and preventing deficiencies or toxicities in cells. Dysregulation of DMT1 is associated with various pathological conditions, including anemia, neurodegenerative diseases, and iron overload disorders like hemochromatosis. Research on recombinant DMT1 has gained momentum as scientists aim to elucidate its structure-function relationships, regulatory mechanisms, and interactions with other cellular proteins. The recombinant expression of DMT1 in heterologous systems allows for detailed biochemical characterization and functional studies. By producing purified DMT1, researchers can investigate its transport kinetics, substrate specificity, and the effects of mutations linked to human diseases. Furthermore, understanding the molecular mechanisms governing DMT1 activity could pave the way for therapeutic strategies targeting metal ion dysregulation in diseases. Advancements in techniques such as X-ray crystallography and cryo-electron microscopy are expected to provide insights into the 3D structure of DMT1, enhancing our comprehension of how this transporter operates at the molecular level. Overall, the study of recombinant DMT1 is not only essential for basic biological understanding but also holds potential clinical implications for developing interventions in metal-related disorders.
