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Oligodendrocytic myelin paranodal and inner loop protein (OPALIN) is a glial transmembrane protein encoded by the OPALIN gene, localizing to paranodal and inner loop segments of mature myelin sheaths produced by oligodendrocytes. Consistent with its type-I membrane topology, OPALIN contains an extracellular N-terminal region, a single transmembrane segment, and a short cytoplasmic C-terminal region. It is primarily used as an oligodendrocyte- and myelin-associated membrane marker, while its precise molecular functions remain under investigation. OPALIN expression is associated with oligodendrocyte maturation and myelin formation. Emerging studies also describe interaction with LGI1 and a possible role in oligodendrocyte differentiation, but direct lipid-binding or membrane-crosslinking activity has not been established.
Variants of the OPALIN gene may alter membrane localization or partner interactions in oligodendrocyte models. OPALIN's type-I membrane localization places it in mature oligodendrocytes and myelin, including paranodal and inner-loop regions, rather than in soluble cytoplasmic pools. Variations in OPALIN expression have been linked to oligodendrocyte maturation, and emerging studies describe LGI1-OPALIN interaction. These observations make OPALIN a useful research target for myelin biology, oligodendrocyte differentiation, and membrane-protein interaction studies, while its precise molecular mechanism remains under investigation.
Fig. 1 Multiple‑species sequence alignment highlights the predicted transmembrane segment of human OPALIN; differential antibody staining under non‑permeabilized and permeabilized conditions supports its type‑I transmembrane orientation.1
The biological functions of transmembrane OPALIN glial protein are focused on myelin-associated localization and membrane-protein interactions, with additional functions still under investigation:
Creative Biolabs offers purified OPALIN membrane samples produced under unified preparation workflows, including full-length OPALIN constructs and isolated extracellular domain variants. Full-length and domain constructs can support studies of OPALIN topology, localization, and partner interactions. All batches receive uniform quality screening. Functional assessments may only be performed on full-length protein under simulated membrane microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis between experimental groups. Full-length OPALIN samples maintain native membrane-associated topology after standardized preparation, supporting comparative analysis of OPALIN localization and protein-partner interactions.
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Creative Biolabs provides cell research models with adjustable OPALIN expression levels, suitable for structural observation of glial transmembrane proteins and research into myelin-associated membrane localization and partner interactions. Sample assessment covers sustained target expression detection and preliminary partner-interaction analysis, enabling side-by-side comparison of membrane localization and interaction behavior under varying expression abundances. These cell models can be paired with diverse laboratory analysis schemes to track shifts in partner-interaction profiles alongside changing target protein levels.
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Anti-OPALIN recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for glial membrane localization mapping and identification of OPALIN-associated protein complexes. The antibody series works with common laboratory detection reagents to support multi-dimensional observation of target distribution within neural tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for OPALIN research:
OPALIN is a type-I glial transmembrane protein enriched in mature oligodendrocyte myelin, including paranodal and inner-loop regions; its precise function remains under investigation.
OPALIN expression is associated with oligodendrocyte maturation and myelin biology, and emerging LGI1 interaction data make it relevant to studies of glial differentiation and membrane-protein interactions.
No, all OPALIN related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material design and functional screening are optimized exclusively for basic laboratory research, without meeting clinical application criteria.
Offerings include full-length OPALIN membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on myelin biology and oligodendrocyte differentiation.
Laboratory analysis schemes may include localization and protein-binding assays to assess OPALIN membrane distribution and interaction behavior in defined cell systems.