Analytical Data
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Gene name
MOG
- Application
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Alternative Names
Myelin-Oligodendrocyte Glycoprotein; MOG
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Species
Rat
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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
Q63345
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Expression Region
Gly28~Gly152
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Molecular Weight
18kDa
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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
The study of Myelin Oligodendrocyte Glycoprotein (MOG) recombinant proteins has gained significant attention in the field of neuroimmunology, primarily due to their pivotal role in demyelinating diseases such as multiple sclerosis (MS). MOG is a crucial component of the myelin sheath formed by oligodendrocytes in the central nervous system (CNS), and it serves as a target for autoimmune responses in various demyelinating conditions. Research has focused on the structural and functional characterization of MOG, and the development of recombinant forms has provided valuable tools for both diagnostic and therapeutic applications. By generating MOG recombinant proteins, scientists can study the specific immune responses they elicit, paving the way for potential interventions that could modulate these responses. Furthermore, these proteins are instrumental in understanding the mechanisms of myelin repair and regeneration, as well as aiding in the identification of biomarkers for early disease diagnosis. Recent advancements in recombinant DNA technology have enabled the production of high-purity MOG proteins, facilitating innovative experimental designs, including in vitro assays and animal models that simulate autoimmune responses. Overall, the exploration of MOG recombinant proteins represents a promising avenue for advancing our understanding of CNS autoimmune diseases and developing targeted therapies that could mitigate the progression of demyelination and promote neurological recovery.
