Analytical Data
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Gene name
SGCa
- Application
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Alternative Names
SGC-A; A2; 50-DAG; ADL; DAG2; DMDA2; LGMD2D; SCARMD1; Adhalin; Dystroglycan-2; 50kDa Dystrophin-Associated Glycoprotein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16586
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Expression Region
Gln24~His387
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Molecular Weight
70kDa
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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
SGCa (Sarcoglycan alpha) is a crucial component of the muscle membrane dystrophin-glycoprotein complex, playing a significant role in stabilizing muscle fibers and facilitating communication between the cytoskeleton and the extracellular matrix. Mutations or deficiencies in SGCa are implicated in various forms of muscular dystrophy, particularly limb-girdle muscular dystrophy (LGMD), leading to progressive muscle weakness and degeneration. The study of SGCa recombinant protein is essential for understanding its structural and functional properties, as well as its interactions within the dystrophin-glycoprotein complex. By exploring the biochemical characteristics of SGCa, researchers aim to elucidate the molecular mechanisms underlying muscle maintenance and pathogenesis in muscular dystrophies. Moreover, this research can pave the way for potential therapeutic strategies, including gene therapy and protein replacement approaches, targeting the restoration of SGCa function in affected muscle tissues. Investigating the folding, stability, and interactions of SGCa at a molecular level provides valuable insights into its role in muscle health and disease, and could lead to advancements in treatment options for patients suffering from SGCa-related myopathies. As such, the recombinant expression and characterization of SGCa are critical for both basic research and the development of novel therapeutic interventions.
