Analytical Data
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Gene name
SGCb
- Application
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Alternative Names
A3b; LGMD2E; SGC; 43DAG; 43kDa Dystrophin-Associated Glycoprotein
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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 90% as determined by SDS-PAGE.
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Uniprot
Q16585
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Expression Region
Trp87~His318
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Molecular Weight
30kDa
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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
SGCb, or Shiga toxin-producing Escherichia coli (STEC) GcnB-like protein, has garnered significant research interest due to its role in the pathogenicity of STEC, a major cause of foodborne illnesses worldwide, leading to severe gastroenteritis and complications such as hemolytic uremic syndrome. This protein is involved in the bacterium's stress response and virulence regulation, impacting its ability to thrive in hostile environments and evade the host immune system. Studies have indicated that SGCb can modulate the expression of various virulence factors, affecting the bacterium’s adherence to host tissues and its capacity to cause disease. Understanding the structure and function of SGCb is crucial for developing therapeutic strategies and preventive measures against STEC infections. Recent advances in molecular biology and structural analysis techniques have enabled researchers to investigate the intricate mechanisms of SGCb, paving the way for potential vaccine development and targeted antimicrobial therapies. By elucidating the role of SGCb in the life cycle of STEC, scientists aim to provide insights that could lead to reduced incidence of STEC-related diseases and improved public health outcomes. The ongoing research in this area highlights the importance of SGCb not only as a significant factor in bacterial pathogenesis but also as a potential target for innovative interventions against one of the leading causes of food safety concerns globally.
