Analytical Data
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Gene name
Dermatopontin/DPT
- Application
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Alternative Names
TRAMP; Tyrosine-rich acidic matrix protein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q07507
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Expression Region
Pro26~Glu197
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Molecular Weight
21kDa
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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
Mucin-15 (MUC15) is a member of the mucin family, characterized by its high molecular weight and special glycosylation patterns that confer unique biological functions. Research into MUC15 has gained interest due to its potential roles in tumor biology, cell signaling, and immune responses. Originally identified in various epithelial tissues, MUC15 is believed to contribute to the maintenance of mucosal barriers and modulate cell adhesion processes. Its aberrant expression has been implicated in several cancers, making it a promising target for therapeutics and diagnostics. The recombinant production of MUC15 protein allows for detailed studies into its structure-function relationships and biological activities. By investigating MUC15 through recombinant techniques, researchers can better understand its role in pathological conditions, explore its function in cellular interactions, and evaluate its potential as a biomarker for cancer diagnosis and prognosis. Furthermore, studying MUC15 in a controlled environment aids in the development of targeted therapies that could enhance treatment strategies for cancer patients. Overall, the exploration of MUC15/MUC15 recombinant protein not only advances our understanding of mucin biology but also opens avenues for innovative clinical applications.
