{"product_id":"recombinant-rubella-virus-structural-polyprotein-partial-bhp10510780","title":"Recombinant Rubella virus Structural polyprotein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eRecombinant Rubella virus Structural polyprotein, partial is a recombinant protein reagent derived from Rubella virus (strain RA27\/3 vaccine) (RUBV) and produced in Baculovirus. It is commonly used to support Microbiology research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eExpressed region:\u003c\/strong\u003e 583-1028aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e Baculovirus. Expression host can influence folding and the presence\/absence of post-translational modifications.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eTag \/ fusion:\u003c\/strong\u003e C-terminal 6xHis-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.\u003c\/li\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular weight (reported):\u003c\/strong\u003e 53.4 kDa. Apparent size may vary with tags, processing, and gel conditions.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eWhen comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.\u003c\/p\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eRV-PP-P refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Rubella virus (strain RA27\/3 vaccine) (RUBV) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt\/NCBI) and the recent literature for the specific organism and isoform.\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eUsing recombinant proteins to enable quantitative binding measurements and reagent benchmarking.\u003c\/li\u003e \u003cli\u003eStudying domain- and isoform-specific effects in pathway models and interaction networks.\u003c\/li\u003e \u003cli\u003eDeveloping robust, reproducible assays that connect molecular readouts to cellular phenotypes.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003e\u003cstrong\u003eRelevance:\u003c\/strong\u003e [Capsid protein]: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP\/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. [Spike glycoprotein E2]: Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement. [Spike glycoprotein E1]: Class II viral fusion protein . Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1\/E2 heterodimer and concomitant trimerization of the E1 subunits . This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement .\u003c\/p\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eAssay and standard development for immunoassays or binding-based detection methods.\u003c\/li\u003e \u003cli\u003eProtein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.\u003c\/li\u003e \u003cli\u003eStructure–function analysis, including domain mapping or evaluation of sequence variants.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eIn quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative\/positive controls and, where possible, orthogonal assay formats that support the same conclusion.\u003c\/p\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e \u003cli\u003eRecombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.\u003c\/li\u003e \u003cli\u003eTag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.\u003c\/li\u003e \u003cli\u003eSpecies and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProtKB entry for P19725 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P19725\/entry - PubMed search (RV-PP-P) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=RV-PP-P - Reactome Pathway Browser — Reactome — https:\/\/reactome.org\/ - Ensembl genome browser — Ensembl — https:\/\/www.ensembl.org\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53065330458989,"sku":"CSB-BP324845ROR1-1MG","price":3278.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53065512681837,"sku":"CSB-BP324845ROR1-100UG","price":1478.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53065512714605,"sku":"CSB-BP324845ROR1-20UG","price":528.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-BP324845ROR1-SDS.jpg?v=1772476640","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-rubella-virus-structural-polyprotein-partial-bhp10510780","provider":"BioHippo","version":"1.0","type":"link"}