{"product_id":"recombinant-st-louis-encephalitis-virus-genome-polyprotein-partial-bhp10509964","title":"Recombinant St. louis encephalitis virus Genome polyprotein, partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003eRecombinant St. louis encephalitis virus Genome polyprotein, partial is a recombinant protein reagent derived from St.louis encephalitis virus (strain MS1-7) and produced in E.coli. It is commonly used to support Others 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 1500-2117aa. 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 E.coli. 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 N-terminal 10xHis-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 74.6 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\u003eSLEV-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 St.louis encephalitis virus (strain MS1-7) 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 C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.; [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer.; [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.; [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.; [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.; [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.; [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).; [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha\/beta interferon antiviral response.; [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins.; [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.; [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.; [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.; [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha\/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.; [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha\/beta (IFN-alpha\/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.\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 \u003cli\u003eE. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProtKB entry for P09732 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/P09732\/entry - PubMed search (SLEV-PP-P) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=SLEV-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":53065305686381,"sku":"CSB-EP357746SKT-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53065463562605,"sku":"CSB-EP357746SKT-100UG","price":729.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53065463595373,"sku":"CSB-EP357746SKT-20UG","price":388.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP357746SKT-SDS.jpg?v=1772476523","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-st-louis-encephalitis-virus-genome-polyprotein-partial-bhp10509964","provider":"BioHippo","version":"1.0","type":"link"}