Analytical Data
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Gene name
DAG
- Application
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Alternative Names
DAG；Dystroglycan 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
Q14118
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Expression Region
30-312aa
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AA Sequence
MKHHHHHHASHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPD GTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEG LPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRT ASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSE VELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQN SVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRR
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Molecular Weight
32 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
DAG (Diacylglycerol) biosynthetic pathways are crucial for various cellular processes, including signaling, membrane dynamics, and energy storage. Researchers focus on DAG because it serves as a key lipid mediator in numerous physiological and pathological processes, influencing cell growth, differentiation, and apoptosis. The manipulation of DAG levels and the understanding of its interactions with different proteins and lipids are essential for elucidating its role in diseases, including cancer, cardiovascular disorders, and metabolic syndromes. The study of DAG-reconstituted proteins, particularly through techniques like protein engineering and synthetic biology, allows scientists to probe the functional mechanisms of these proteins and their contributions to cellular signaling pathways. Moreover, DAG-reconstituted proteins serve as valuable tools in drug discovery and therapeutic development, enabling the identification of novel compounds that target DAG-related pathways. As such, ongoing research in this area aims to provide deeper insights into DAG's dynamic role in cellular functions and its potential implications for human health.
