Analytical Data
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Gene name
MMP20
- Application
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Alternative Names
MMP20;Matrix metalloProteinase-20
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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
O60882
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Expression Region
108-483aa
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AA Sequence
YRLFPGEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSF VRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDN AEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFH LPKDDVKGIQALYGPRKVFLGKPTLPHAPHHKPSIPDLCDSSSSFDAVTM LGKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMSNVDAAYEVAERG TAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRHVQQIDAAVYLREPQKTL FFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVELNGYIYFFS GPKTYKYDTEKEDVVSVVKSSSWIGC
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Molecular Weight
54 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
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Protein Description
MMP20, or Matrix Metalloproteinase 20, is an enzyme that plays a critical role in the remodeling of extracellular matrix components, particularly in the context of dental and bone development. Its expression is primarily observed in various tissues, including the developing teeth, where it contributes to enamel formation and mineralization processes. Abnormal regulation or deficiency of MMP20 has been associated with several dental anomalies, such as amelogenesis imperfecta, which affects enamel thickness and quality. Given its significant biological functions, MMP20 has garnered interest in both basic and applied research, particularly in regenerative medicine and dentistry. Recombinant MMP20 protein studies aim to elucidate its structure-function relationships, biochemical properties, and regulatory mechanisms, offering insights into its potential therapeutic applications. By producing MMP20 in recombinant systems, researchers can investigate its role in enamel matrix degradation, cellular signaling pathways, and interactions with other matrix components, paving the way for innovations in dental treatments and biomaterials for tooth regeneration. Understanding MMP20's mechanistic pathways could also lead to novel strategies in preventing and treating dental diseases, thereby improving oral health outcomes.











