{"product_id":"recombinant-human-myelin-oligodendrocyte-glycoprotein-mog-fluorescent-vlps-bhp10512854","title":"Recombinant Human Myelin-oligodendrocyte glycoprotein (MOG), Fluorescent-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eMOG\u003c\/strong\u003e from Homo sapiens (Human). In the supplied product notes, the target is described as \u003cem\u003eMediates homophilic cell-cell adhesion.\u003c\/em\u003e; the narrative below provides general biological context to help interpret experiments (research use only).\u003c\/p\u003e\n\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eTarget and identity:\u003c\/strong\u003e MOG. When working across orthologs or family members, confirm naming\/synonyms and sequence-level relatedness to reduce ambiguity in downstream interpretation.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 30-247aa. For many transmembrane proteins, recombinant constructs may focus on soluble domains or extracellular\/luminal segments; the chosen region can shape which binding sites, motifs, or interaction surfaces are represented.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Mammalian cell. Expression host can influence folding efficiency and post-translational modifications (for example, disulfide bonding and glycosylation), which can matter for ligand-binding or antibody-recognition studies.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFormat and quality attributes:\u003c\/strong\u003e form: Lyophilized powder; purity: The purity information is not available for VLPs proteins.; molecular weight: 55.9 kDa. Use these attributes to anticipate detectability in assays and to plan appropriate controls and normalization strategies.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eRecombinant proteins derived from membrane-associated targets are often studied as isolated domains to improve solubility and enable biophysical or immunochemical readouts. Mammalian expression can better recapitulate many native post-translational features, which is helpful when the experimental question is sensitive to conformation, glycosylation, or complex assembly.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eMOG is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Viral membrane proteins and envelope glycoproteins are widely studied for their roles in entry, fusion, assembly, and immune recognition; recombinant domains are often used to probe receptor binding or antigenic surfaces in a controlled format.\u003c\/p\u003e\n\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eStructure-enabled questions: cryo-EM, computational modeling, and integrative structural biology are increasingly used to connect domain-level constructs to full-length membrane protein architecture and interaction interfaces.\u003c\/li\u003e\n  \u003cli\u003eAntigen design and immune mapping: recombinant envelope and surface proteins are frequently used for epitope mapping, neutralization-focused antigen design, and comparative studies across strains or variants.\u003c\/li\u003e\n  \u003cli\u003eHost–pathogen interfaces: receptor engagement, fusion machinery, and assembly pathways remain active areas, often combining biochemical binding assays with cell-based validation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2\u003eCommon research applications\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eBinding and interaction studies: use recombinant domains to evaluate whether a ligand, antibody, or receptor interaction is compatible with the expressed region and expected post-translational context.\u003c\/li\u003e\n  \u003cli\u003eReference material for comparative measurements: when used as a calibrator, consider matrix effects and ensure the construct region matches the epitope or binding site being measured.\u003c\/li\u003e\n  \u003cli\u003eStructural and biophysical characterization: soluble domains can support stability screening, complex formation, and hypothesis generation about the full-length membrane protein.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003eWhen interpreting signal changes, distinguish between abundance effects (expression level), accessibility effects (conformation or compartment), and chemistry effects (post-translational modifications). For membrane-associated targets, trafficking and proteolytic processing can create multiple detectable species that differ from predicted mass.\u003c\/p\u003e\n\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\n\u003cul\u003e\n  \u003cli\u003eIsoforms and truncations: alternative splicing or proteolytic processing can shift which domains are present in the native sample relative to the recombinant region.\u003c\/li\u003e\n  \u003cli\u003ePost-translational modifications: glycosylation, disulfide bonding, lipidation, and phosphorylation can alter apparent size and binding; expression-system differences may change these features.\u003c\/li\u003e\n  \u003cli\u003eMembrane environment: many binding sites and conformations are stabilized by lipids or neighboring subunits; isolated domains may not fully recapitulate full-length behavior.\u003c\/li\u003e\n  \u003cli\u003eControl concepts: include negative controls matched for tags or host background where relevant, and consider orthogonal evidence (e.g., genetic perturbation rationale such as knockout\/knockdown) to support specificity claims.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c!-- Sources (internal):\n- UniProtKB search: MOG — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=MOG\n- NCBI Gene search: MOG — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=MOG\n- Ensembl search: MOG — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=MOG\n- AlphaFold DB search: MOG — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/MOG\n- RCSB PDB search: MOG — RCSB PDB — https:\/\/www.rcsb.org\/search?query=MOG\n- PubMed search: MOG transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=MOG+transmembrane\n- Review search: membrane protein structural biology (cryo-EM) — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+cryo-EM+review\n- Review search: membrane protein trafficking \u0026 quality control — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=membrane+protein+trafficking+review\n--\u003e","brand":"CUSABIO TECHONOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207335633261,"sku":"CSB-MP619083HU(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320607105389,"sku":"CSB-MP619083HU(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320607138157,"sku":"CSB-MP619083HU(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-MP619083HU_A4_-WB.jpg?v=1778623157","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-myelin-oligodendrocyte-glycoprotein-mog-fluorescent-vlps-bhp10512854","provider":"BioHippo","version":"1.0","type":"link"}