Analytical Data
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Gene name
DMP-1
- Application
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Alternative Names
/
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Species
Dog
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
F1PHT7
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Expression Region
1-435aa
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Molecular Weight
63.5 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
DMP-1, or dentin matrix protein 1, is a critical non-collagenous protein predominantly expressed in the dental matrix and plays a significant role in tooth development and mineralization. It is part of the acidic phosphoprotein family, which is essential for regulating enamel and dentin formation. Research into DMP-1 has gained momentum due to its involvement in various physiological and pathological processes, including its influence on the differentiation of odontoblasts and its potential role in dental diseases such as caries and pulpitis. Additionally, DMP-1 is implicated in the regulation of mineralization not only in teeth but also in bone tissue, making it a target for studies related to osteogenesis and bone disorders. Recent advancements in recombinant protein technology have enabled the production of DMP-1 in a laboratory setting, facilitating in-depth studies of its structure-function relationship, signaling pathways, and potential therapeutic applications. Understanding the mechanisms by which DMP-1 operates could provide insights into strategies for regenerative dentistry and the treatment of calciotropic disorders. This rising interest highlights the need for comprehensive characterization of DMP-1’s properties and its applications in regenerative medicine and tissue engineering.
