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Human MOG Protein, His Tag (MALS verified)

Human MOG Protein, His Tag (MALS verified)

CAT#: IVD-P016

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Overview Specification
Species Human
Tag His
Expression Systems HEK293 cell
Keywords In vitro diagnostic proteins
Synonyms MOG, BTN6, BTNL11, MOGIG2, NRCLP7, Myelin oligodendrocyte glycoprotein
Background Myelin oligodendrocyte glycoprotein (MOG), is a single-pass transmembrane glycoprotein of the immunoglobulin (Ig) superfamily. MOG is a myelin protein exclusively expressed in the CNS at the outermost surface of myelin sheaths and oligodendrocyte membranes. This makes MOG a potential target of cellular and humoral immune responses in inflammatory demyelinating diseases. Due to its late postnatal developmental expression, MOG is an important marker for oligodendrocyte maturation.
Source Human MOG
SWISS Q16653-1
Theoretical Molecular Weight 16.2 kDa
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4 with trehalose as protectant.
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Molecular Characterization This protein carries a polyhistidine tag at the C-terminus. The protein migrates as 20-24 kDa when calibrated against star ribbon prestained protein marker under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin Less than 1.0 EU per μg by the LAL method.
Purity >90% as determined by SDS-PAGE.
Storage For long term storage, the product should be stored at lyophilized state at -20°C or lower. Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.
Notes This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.
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