{"product_id":"recombinant-human-herpesvirus-6b-u24-protein-u24-bhp10509232","title":"Recombinant Human herpesvirus 6B U24 protein (U24)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\n\u003cp\u003eThis recombinant protein is designed to support research on \u003cstrong\u003eU24\u003c\/strong\u003e (also reported as U24 protein) from Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic virus). In the supplied product notes, the target is described as \u003cem\u003eDown-regulates the TCR\/CD3E complex and the transferrin receptor TFRC in host T-cells by blocking them from recycling back to the cell surface.\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 U24 (also reported as U24 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 1-88aa. 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 in vitro E.coli expression system. 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: Liquid or Lyophilized powder; purity: Greater than 85% as determined by SDS-PAGE.; molecular weight: 16.2 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.\u003c\/p\u003e\n\u003ch2\u003eBiological background\u003c\/h2\u003e\n\u003cp\u003eU24 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. 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: U24 — UniProt — https:\/\/www.uniprot.org\/uniprotkb?query=U24\n- NCBI Gene search: U24 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=U24\n- Ensembl search: U24 — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=U24\n- AlphaFold DB search: U24 — EMBL-EBI — https:\/\/alphafold.ebi.ac.uk\/search\/text\/U24\n- RCSB PDB search: U24 — RCSB PDB — https:\/\/www.rcsb.org\/search?query=U24\n- PubMed search: U24 transmembrane — NLM \/ PubMed — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=U24+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":"100 ug","offer_id":53207327474029,"sku":"CSB-CF865554HKA-100UG","price":2781.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53320595898733,"sku":"CSB-CF865554HKA-20UG","price":1668.6,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-CF865554HKA-SDS.jpg?v=1778623132","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-herpesvirus-6b-u24-protein-u24-bhp10509232","provider":"BioHippo","version":"1.0","type":"link"}