Recombinant Mouse MOG Protein (aa30-149, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3401

Recombinant Mouse MOG Protein (aa30-149, His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3401
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Product Overview

Tag His
Host Species Mouse
Accession Q61885
Synonym B230317G11Rik
Background Myelin oligodendrocyte glycoprotein (MOG) is a transmembrane protein belonging to immunoglobulin superfamily, and contains an Ig-like domain followed by two potential membrane-spanning regions. MOG is expressed only in the CNS with very low content (approximately .1% total proteins) in oligodendrogliocyte membrane. Three possible functions for MOG were suggested: (a) a cellular adhesive molecule, (b) a regulator of oligodendrocyte microtubule stability, and (c) a mediator of interactions between myelin and the immune system, in particular, the complement cascade. A direct interaction might exist between the membrane-associated regions of MOG and the myelin-specific glycolipid galactocerebroside (Gal-C), and such an interaction may have important consequences regarding the membrane topology and function of both molecules. It is considered that MOG is an autoantigen capable to produce a demyelinating multiple sclerosis-like disease in experimental animals.
Description A DNA sequence encoding the mouse MOG (Q61885) extracellular domain (Gly 29-Thr 156) was expressed, with a C-terminal His tag.
Source E.coli
Predicted N Terminal Met
AA Sequence Gly 29-Thr 156
Molecular Weight The recombinant mouse MOG comprises 138 a.a. and migrates as an approximately 16 kDa band as predicted in SDS-PAGE under reducing conditions.
Purity >97% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 5.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication. Mediates homophilic cell-cell adhesion.
Subcellular Location Membrane; Multi-pass membrane protein.
Protein Families Immunoglobulin superfamily, BTN/MOG family
Database References
Tissue Specificity Found exclusively in the CNS, where it is localized on the surface of myelin and oligodendrocyte cytoplasmic membranes. Reduced expression levels are observed in jimpy and quacking dysmyelinating mutant mice.

Gene Functions References

  1. The aim of this work was to explore the conformational characteristics of rat/mouse MOG35-55 immunodominant epitope. The results are discussed in terms of rational design of altered peptide ligands or non-peptide mimetics based on rat MOG35-55 that could be served as potential inhibitors of experimental autoimmune encephalomyelitis PMID: 27483998
  2. Identify nerve growth factor as a binding partner for MOG and demonstrate that this interaction is capable of sequestering NGF from TrkA-expressing neurons to modulate axon growth and survival. PMID: 26347141
  3. the absence of N-glycan did not interfere with MOG's subcellular localization and it did not result in activation of endoplasmic reticulum stress. PMID: 25541284
  4. Data indicate that in mixed chimeras with bone marrow-encoding myelin oligodendrocyte glycoprotein (MOG), the development of MOG-specific B cells was abrogated, resulting in a lack of MOG-specific B cells in all B cell compartments examined. PMID: 24532581
  5. Different forms of evolution of optic neuritis are observed in this animal model suggest that variations of biosynthetic MOG35-55 peptide concentration are capable of inducing different profiles of optic neuritis. PMID: 24083391
  6. Identify immunogenic/encephalitogenic T-cell epitopes within MOG capable of inducing experimental autoimmune encephalomyelitis in C57BL/6 mice. PMID: 23876060
  7. PLP significantly suppresses both models of experimental autoimmune encephalitis (EAE)even when there is some evidence of epitope spreading in the myelin oligodendrocyte (MOG)38-50-induced EAE model. PMID: 23911075
  8. CNTF may play a role in the process of remyelination by inducing the MOG expression. PMID: 23443463
  9. MOG-specific CD4-positive T cells accumulate within the chemokine-expressing draining lymph nodes, rather than within the brain or spinal cord during induction of autoimmune encephalomyelitis. PMID: 22287719
  10. This study provides valuable information about requirements of anti-myelin oligodendrocyte glycoprotein reactivity for being regarded as a prognostic biomarker in a subtype of MS. PMID: 22093619
  11. Mice immunized with encephalitogenic myelin oligodendrocyte glycoprotein MOG(35-55) peptide develop significant serum levels of anti-MOG antibodies in parallel with disease progression. PMID: 21993076
  12. B cell-deficient mice exhibit reduced medullary thymic epithelial cell numbers and reduced MOG mRNA expression. PMID: 21550671
  13. Cell surface targeting of MOG is not disrupted in the absence of the endoplasmic reticulum chaperones. PMID: 21172390
  14. MOG self-tolerance modulates the encephalitogenic potential of autoreactive MOG T cells in the periphery. PMID: 14624757
  15. The core epitope of immunodominant 35-55 peptide (pMOG) fragment has the potential to be citrullinated at two T cell receptor contact residues 41-Arg and 46-Arg, allowing an expanded repertoire of T cells to contribute to encephalomyelitis etiopathology. PMID: 20164413
  16. lack of systemic complement at the time of induction of EAE delays the onset and attenuates the course of the disease most probably via diminishing the response of MOG-specific T cells and production of autoantibodies PMID: 19201476
  17. The encephalitogenic peptide of intact MOG protein (resides 35-55) must be processed and presented via a functioning class II-restricted antigen processing pathway in the central nervous system in order to initiate autoimmune demyelinating disease. PMID: 11937578
  18. role in development of spontaneous autoimmune optic neuritis PMID: 12732654
  19. MOG has a role in immune tolerance and in experimental autoimmune encephalomyelitis PMID: 12925695
  20. Treatment of oligodendrocytes with anti-MOG leads to an increase in calcium influx and activation of the MAPK/Akt pathways. PMID: 15634682
  21. Opticospinal encephalomyelitis mice B cells bind high dilutions of recombinant MOG, but not MOG peptide, and process and present it to autologous T cells. PMID: 16955140
  22. Ig heavy chainMOG mice spontaneously develop a severe form of experimental autoimmune encephalomyelitis. PMID: 16955141
  23. prevention of experimental autoimmune encephalomyelitis by treatment with embryonic stem cell-derived dendritic cells(ES-DC)-TRAIL/MOG is mediated by MOG-reactive CD4(+)CD25(+) Treg propagated by ES-DC-TRAIL/MOG PMID: 17202353
  24. Results describe T cell receptor (TCR) transgenic mice (relapsing-remitting [RR] mice) carrying a TCR specific for myelin oligodendrocyte glycoprotein (MOG) peptide 92-106. PMID: 19487416
  25. CD8+ T cells reactive to MOG37-46 are pro-inflammatory and traffic to the CNS; however, the presence of CD4+ T cells elicits more severe disease and sustained inflammation of the CNS. PMID: 19540601
  26. the ligation of CEACAM1 negatively regulates the severity of experimental autoimmune encephalomyelitis by reducing MOG(35-55)-specific induction of both interferon-gamma and interleukin-17 via invariant natural killer T cell-dependent mechanisms PMID: 19700760
  27. protein localization signal PMID: 11389181


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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