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Name :
Human MOG/BTN6/BTNL11 Protein, ECD (Extracellular Domain), Fc-fusion, Biotinylated, Recombinant

Description :
MOG (myelin oligodendrocyte glycoprotein) is a two-pass type I transmembrane protein belonging to the BTN/MOG family of the immunoglobulin (Ig) superfamily. MOG contains an Ig-like V-type domain in the first extracelluar region followed by two transmembrane regions and a small second extracellular tail. MOG is found exclusively in the CNS, where it is localized on the surface of myelin and oligodendrogliocyte membranes. The MOG genes are highly conserved in mammals, suggesting an important biological role for this protein. While the primary molecular function of MOG is not yet known, its likely role with the myelin sheath is either in sheath completion and/or maintenance. MOG may mediate homophilic cell-cell adhesion. MOG is considered as an autoantigen capable to produce a demyelinating multiple sclerosis (MS)-like disease in experimental animals. Several studies have shown a role for antibodies against MOG in the pathogenesis of MS. The mutation in the MOG gene is associated with Narcolepsy 7 (NRCLP7), a neurological disabling sleep disorder, characterized by excessive daytime sleepiness, sleep fragmentation, symptoms of abnormal rapid-eye-movement sleep, cataplexy, hypnagogic hallucinations, and sleep paralysis.

Gene Symbol :

NCBI Gene ID :
4340

Uniprot Entry :
Q16653

Construct Details :
The recombinant human MOG-Fc fusion is expressed as a 354 amino acid protein consisting of Gly30 – Glu145 region of MOG (Uniprot Accession #Q16653) and a C-terminal Fc from human IgG1, which exists as a dimer under non-reducing conditions.

Source :
Human cells stably expressing MOG-Fc growing in chemical-defined media with no animal components or antibiotics

Amino Acid Sequence: :
10 20 30 40 50 60 GQFRVIGPRH PIRALVGDEV ELPCRISPGK NATGMEVGWY RPPFSRVVHL YRNGKDQDGD 70 80 90 100 110 120 QAPEYRGRTE LLKDAIGEGK VTLRIRNVRF SDEGGFTCFF RDHSYQEEAA MELKVESTTE 130 140 150 160 170 180 NLYFQGSTGT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV 190 200 210 220 230 240 KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE 250 260 270 280 290 300 KTISKAKGQP REPQVYTLPP SREEMTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT 310 320 330 340 350 TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK M.W.: Calculated molecular mass (kDa): 39.9; Estimated by SDS-PAGE under reducing condition (kDa): 45-50 Calculated PI: 6.87 Calculated Extinction Coefficient (M-1 cm-1, at 280nm): 48860 Purity: >95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as DTT “+”) Formulation: Supplied at 0.5 mg/ml in sterile PBS pH7.4 (carrier and preservative free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule) using the standard procedure. Endotoxin Level: Biological Activity: Not available FOR RESEARCH USE ONLY. NOT FOR DIAGNOSTIC OR THERAPEUTIC USE IN HUMAN. Restriction: This product is not transferable or re-sellable. Customer obtain no right to transfer, assign, or sublicense its use rights, or to transfer, resell, package, or otherwise distribute the product, or to use the product for the benefit of any third party or for any commercial purpose. Customer may only use the product in compliance with applicable local, state and federal laws, regulations and rules. Customer may not directly or indirectly use the product or allow the transfer, transmission, export or re-export of all or any part of the product in violation of any export control law or regulation of the united states or any other relevant jurisdiction. Your use of this product constitutes acceptance of the terms of this limited use agreement. Please refer to our “terms & conditions” for details. If you are not willing to accept the limitation of this agreement, G&P Biosciences will accept return of the product for a full/partial refund. Storage The product is shipped at 4°C for immediate use. Upon receipt, centrifuge the product briefly before opening the vial. It is recommended to store small aliquots at the temperature below –20°C for long-term storage and the product is stable for 3 months. The undiluted protein can be stored at 4°C for no more than 2 weeks. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. FOR RESEARCH USE ONLY. NOT FOR DIAGNOSTIC OR THERAPEUTIC USE IN HUMAN. References 1. J. Neurochem. 63:2353 (1993) 2. J. Neurochem. 65:309 (1994) 3. J. Neurochem. 72: 1 (1999) 4. N. Engl. J. Med. 349: 139 (2003) 5. Am. J. Hum. Genet. 89:474 (2010) Documentation Product datasheet (pdf) can be downloaded here: FCL2128B-PDS.pdf Additional supporting documents, including COA and MSDS are available upon request.

M.W. :
: 6.87

Calculated PI :

Calculated Extinction Coefficients :

Endotoxin Level :
>95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as DTT “+”)

Formulation :
Supplied at 0.5 mg/ml in sterile PBS pH7.4 (carrier and preservative free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule) using the standard procedure.

Endotoxin Level :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method

Biological Activity :
Not available

Molecule Class :
2-Pass Type I Transmembrane

Gene Synonym :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method

Gene Family :
MOG; BTN6; BTNL11; MOGIG2; NRCLP7

Research Area :
Neuroscience

Pathway/Disease :
Cell Adhesion

Species :
Human

CD Antigen :

References :

MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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