Analytical Data
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Gene name
DAG1
- Application
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Alternative Names
Dystrophin-associated glycoprotein 1
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Species
Rabbit
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q28685
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Expression Region
30-653aa
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Molecular Weight
73.5 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
DAG1, also known as dystroglycan, is a crucial component of the dystrophin-glycoprotein complex, which plays a significant role in maintaining muscle integrity and function. Mutations or dysfunctions in DAG1 have been implicated in a variety of muscular dystrophies, particularly those affecting skeletal and cardiac muscle. Research into DAG1 recombinant proteins has gained momentum as scientists seek to understand the biochemical pathways associated with muscular diseases and explore potential therapeutic avenues. These recombinant proteins serve as valuable tools for elucidating DAG1’s structure-function relationships, examining its interactions with other cellular components, and studying its regulation in muscle tissues. Moreover, engineering DAG1 variants could facilitate the development of targeted treatments for diseases linked to dystroglycanopathies, aiming to restore its function or compensate for its loss. The ongoing investigations into DAG1 also aim to leverage advanced biotechnological approaches, such as gene therapy and protein replacement strategies, to ameliorate conditions caused by DAG1 deficiency. Overall, the study of DAG1 recombinant proteins not only enhances our understanding of muscular pathologies but also paves the way for innovative therapeutic interventions that could improve the quality of life for patients suffering from related disorders.
