Analytical Data
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Gene name
DMP1
- Application
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Alternative Names
DMP1；Dentin matrix acidic phosphoProtein 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
Q13316
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Expression Region
17-513aa
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AA Sequence
LPVTRYQNNESEDSEEWKGHLAQAPTPPLESSESSEGSKVSSEEQANEDPSDSTQSEEGLGSDDHQYIYRLAGGFSRSTGKGGDDKDDDEDDSGDDTFGDDDSGPGPKDRQEGGNSRLGSDEDSDDTIQASEESAPQGQDSAQDTTSESRELDNEDRVDSKPEGGDSTQESESEEHWVGGGSDGESSHGDGSELDDEGMQSDDPESIRSERGNSRMNSAGMKSKESGENSEQANTQDSGGSQLLEHPSRKIFRKSRISEEDDRSELDDNNTMEEVKSDSTENSNSRDTGLSQPRRDSKGDSQEDSKENLSQEESQNVDGPSSESSQEANLSSQENSSESQEEVVSESRGDNPDPTTSYVEDQEDSDSSEEDSSHTLSHSKSESREEQADSESSESLNFSEESPESPEDENSSSQEGLQSHSSSAESQSEESHSEEDDSDSQDSSRSKEDSNSTESKSSSEEDGQLKNIEIESRKLTVDAYHNKPIGDQDDNDCQDGY
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Molecular Weight
56.0 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
Dentin matrix protein 1 (DMP1) is a crucial non-collagenous protein primarily involved in the mineralization of bone and dentin, making it significant for dental and orthopedic health. Research into DMP1 has garnered attention due to its role in biomineralization processes and the anomalies associated with its dysfunction, such as in disorders like dentinogenesis imperfecta and osteomalacia. Understanding the structure and function of DMP1 is essential for potential therapeutic applications in regenerative medicine and tissue engineering, as it influences the formation and repair of mineralized tissues. The recombinant expression of DMP1 has provided insights into its biochemical properties and interactive dynamics with other matrix proteins and cells. Recent studies have focused on producing recombinant DMP1 proteins to analyze their effects on osteoblast and odontoblast activity, as well as evaluating their potential to facilitate mineralization and enhance scaffold effectiveness within tissue engineering frameworks. This line of research aims to decode the underlying molecular mechanisms of DMP1 in dental and bone health and to harness its therapeutic potential, paving the way for innovative approaches in treating related conditions. The advancements in recombinant protein technology thus hold promise for improved diagnostics and therapeutics in dental and orthopedic practices, highlighting DMP1's significance in clinical applications.
