Analytical Data
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Gene name
MAG
- Application
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Alternative Names
MAG；GMA；Myelin-associated glycoProtein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20916
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Expression Region
20-516aa
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AA Sequence
GHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSNVSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQASFPNTTLQFEGYASMDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGTVLREAVAESLLLELEEVTPAEDGVYACLAENAYGQDNRTVGLSVMYAPWKPTVNGTMVAVEGETVSILCSTQSNPDPILTIFKEKQILSTVIYESELQLELPAVSPEDDGEYWCVAENQYGQRATAFNLSVEFAPVLLLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNESEREFVYSERSGLVLTSILTLRGQAQAPPRVICTARNLYGAKSLELPFQGAHRLMWAKIGP
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Molecular Weight
58.8 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
MAG (Myelin Associated Glycoprotein) is a critical myelin component in the peripheral and central nervous systems, playing a significant role in myelin stability and axonal integrity. Research on MAG has gained momentum due to its implications in various neurodegenerative diseases, including multiple sclerosis and peripheral neuropathy, where demyelination leads to severe neurological deficits. MAG functions primarily through its interactions with axonal surface proteins, promoting myelin-axon adhesion and modulating nerve repair processes. Additionally, it is involved in signaling pathways that influence neuronal growth and survival. Given the rising incidence of demyelinating diseases and the limited effectiveness of existing therapies, understanding the mechanisms of MAG and its potential for therapeutic targeting is crucial. Recent studies have explored recombinant MAG proteins as potential biological agents to promote remyelination and axonal protection in experimental models. These investigations aim to clarify the multifaceted roles of MAG, enhance our understanding of myelin biology, and inform the development of innovative treatments for myelin-related disorders. As research progresses, MAG continues to be a focal point in neurobiology, presenting therapeutic opportunities that could transform the management of demyelinating diseases.
