Analytical Data
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Gene name
FAM20C
- Application
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Alternative Names
Dentin matrix protein 4 (DMP-4) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK) (DMP4)
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Species
Human
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Source
HEK293
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IXL6
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Expression Region
93-584aa
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Molecular Weight
61.4 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
FAM20C, a member of the Fam20 family of proteins, has gained significant attention in recent years due to its critical role in bone mineralization and dental health. This protein is primarily known for its function as a kinase that phosphorylates several extracellular proteins, particularly in the enamel matrix of teeth. Mutations in the FAM20C gene are linked to conditions such as amelogenesis imperfecta and various skeletal dysplasias, highlighting its importance in normal physiological processes. Research on the recombinant form of FAM20C aims to elucidate its precise mechanisms of action, characterizing how it interacts with its substrates and contributes to biomineralization. Recombinant protein studies enable scientists to investigate the phosphorylation patterns and functional implications of FAM20C in various cellular contexts, thereby advancing our understanding of its role in enamel and bone formation. Additionally, insights gained from these studies could pave the way for therapeutic approaches in treating dental and skeletal disorders linked to FAM20C deficiencies. Overall, the ongoing research on FAM20C recombinant proteins provides valuable knowledge that bridges the gap between molecular biology and clinical applications in dentistry and orthopedics.
