Analytical Data
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Gene name
MOBP
- Application
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Alternative Names
Myelin-associated oligodendrocyte basic protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13875
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Expression Region
1-81 aa
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AA Sequence
MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRLKRKIRPTPKKK
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Molecular Weight
34.65 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
MOBP (Myelin Oligodendrocyte Basic Protein) is a key component in the myelin sheath of the central nervous system, playing a critical role in the structure and function of oligodendrocytes. Research into MOBP has gained momentum due to its implications in neurodegenerative diseases such as multiple sclerosis, where myelin degeneration leads to impaired neuronal communication and ultimately, neurological dysfunction. Understanding the structure and function of MOBP at the molecular level is vital for the development of potential therapeutic interventions. Furthermore, the recombinant production of MOBP allows researchers to study its properties in detail, enabling the investigation of its interactions with other proteins and its role in myelination. Advances in protein engineering techniques have facilitated the generation of various isoforms of MOBP, providing insights into how different forms may influence oligodendrocyte function and myelin stability. Additionally, by exploring the post-translational modifications of MOBP, researchers are uncovering the regulatory mechanisms that govern its expression and function during both normal development and pathological conditions. This knowledge is invaluable for designing targeted therapies aimed at restoring myelin integrity and enhancing remyelination processes in demyelinating diseases. Overall, the study of recombinant MOBP not only enhances our understanding of myelin biology but also opens new avenues for clinical applications in neuroprotection and regeneration.
