Analytical Data
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Gene name
GM2A
- Application
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Alternative Names
SAP-3; Cerebroside Sulfate Activator Protein; Sphingolipid Activator Protein 3
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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
P17900
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Expression Region
His24~Ile193
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Molecular Weight
24kDa
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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
GM2A, or GM2 activating protein, plays a crucial role in the metabolism of GM2 gangliosides, which are glycosphingolipids found in the nervous system. The study of GM2A is particularly important due to its association with GM2 ganglioside accumulation in lysosomal storage disorders, such as GM2 gangliosidoses, which include Tay-Sachs disease and Sandhoff disease. These conditions are characterized by the deficiency of specific hexosaminidase enzymes, leading to harmful levels of GM2 in the body, particularly affecting neuronal function and resulting in severe neurological symptoms. Understanding the structure and function of GM2A can provide insights into the molecular mechanisms underlying these disorders, potentially facilitating the development of therapeutic strategies. Researchers have focused on GM2A's role as a cofactor in the enzymatic degradation of GM2 gangliosides, enhancing the activity of hexosaminidase enzymes. Furthermore, GM2A's interactions with other cellular components and lipid membranes are of significant interest, as they may influence the lysosomal pathway and ganglioside metabolism. Advances in recombinant protein technology have enabled the production of GM2A for in vitro studies, allowing for detailed investigations of its biochemical properties, stability, and functionality. Such research is vital for elucidating the pathophysiology of GM2-related diseases and may ultimately lead to innovative treatment methods, including enzyme replacement therapies or gene therapies aimed at restoring normal metabolic function in affected individuals. As our understanding of GM2A and its mechanisms improves, it holds promise for addressing the challenges posed by GM2 gangliosidoses and enhancing patient outcomes.
