Analytical Data
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Gene name
AMELY
- Application
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Species
Human
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Source
E. coli
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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
Q99218
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Expression Region
17-102aa
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Molecular Weight
17.3 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
The study of AMELY (Amelogenin Y) recombinant proteins is rooted in their pivotal role in dental enamel formation and their potential applications in biomedical and forensic sciences. Amelogenins are key extracellular matrix proteins synthesized during tooth development, primarily involved in the mineralization and structural integrity of enamel. The AMELY gene, located on the Y chromosome, encodes a variant of amelogenin that has garnered interest due to its sex-specific expression, making it a valuable tool in determining biological sex in forensic contexts. Recent advancements in recombinant DNA technology have enabled the production of AMELY proteins in controlled laboratory settings, allowing researchers to investigate their structural and functional properties. Studies have shown that these proteins can influence the crystallization of hydroxyapatite, a crucial component of enamel, thereby offering insights into enamel-related dental pathologies. Furthermore, the development of AMELY recombinant proteins has opened avenues for novel therapeutic strategies in regenerative dentistry, such as promoting enamel repair and regeneration. Overall, the research into AMELY not only enhances our understanding of dental biology but also contributes to broader applications in forensic science and tissue engineering.
