{"product_id":"recombinant-epstein-barr-virus-latent-membrane-protein-2-lmp2-vlps-bhp10515228","title":"Recombinant Epstein-Barr virus Latent membrane protein 2 (LMP2)-VLPs","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eLMP2\u003c\/strong\u003e (also reported as Terminal protein) from Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4). In the supplied product notes, the target is described as \u003cem\u003eIsoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking.\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 LMP2 (also reported as Terminal protein). 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 1-497aa. 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: 54.4 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\u003eLMP2 is a transmembrane or membrane-associated protein that can participate in signaling, transport, adhesion, or host–pathogen interactions depending on the biological system. Alternative naming conventions are common for membrane protein families; mapping synonyms to sequence identifiers (for example via UniProt\/NCBI\/Ensembl) can help avoid reagent mismatches.\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\u003eContext dependence: current work often emphasizes how lipid composition, membrane microdomains, and trafficking pathways modulate receptor\/transport behavior and shape downstream signaling outputs.\u003c\/li\u003e\n  \u003cli\u003eConformation and state-selective reagents: many studies focus on ligands, antibodies, or binders that preferentially recognize specific conformational states, supporting mechanistic hypotheses beyond simple abundance measurements.\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: LMP2 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=LMP2\n- NCBI Gene search: LMP2 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=LMP2\n- Ensembl search: LMP2 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=LMP2\n- AlphaFold DB search: LMP2 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/LMP2\n- RCSB PDB search: LMP2 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=LMP2\n- PubMed search: LMP2 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=LMP2+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 TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53207341597037,"sku":"CSB-MP321086EFA(A4)-1MG","price":6546.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53320615231853,"sku":"CSB-MP321086EFA(A4)-100UG","price":1235.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320615264621,"sku":"CSB-MP321086EFA(A4)-20UG","price":620.0,"currency_code":"USD","in_stock":true}],"url":"https:\/\/www.ebiohippo.com\/products\/recombinant-epstein-barr-virus-latent-membrane-protein-2-lmp2-vlps-bhp10515228","provider":"BioHippo","version":"1.0","type":"link"}