{"product_id":"abcam-ab20944","title":"Abcam, ab20944, HRP Anti-Rubella Virions antibody","description":"\u003cp\u003eSize: 500µL\u003cbr\u003e\nGoat Polyclonal Rubella Virions antibody - conjugated to HRP. Suitable for ICC and reacts with Rubella virus samples. Cited in 1 publication.\u003cbr\u003e\nKey facts\u003cbr\u003e\nHost species:Goat,\u003cbr\u003e\nClonality:Polyclonal,\u003cbr\u003e\nIsotype:IgG,\u003cbr\u003e\nConjugation:HRP,\u003cbr\u003e\nCarrier free:No,\u003cbr\u003e\nReacts with:Rubella virus,\u003cbr\u003e\nApplications:ICCSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,\u003cbr\u003e\nSpecificity:Purified virions. Negative against Vero cells by indirect immunofluorescence.\u003c\/p\u003e\n\n\u003cp\u003eProduct details:\u003cbr\u003e\nCovalently coupled to a highly purified preparation of Horseradish Peroxidase (RZ\u0026gt;3). Care is taken to ensure adequate conjugation while preserving maximum enzyme activity. Free enzyme is removed. Estimated molar HRP:IgG substitution is 2-3. Use of sodium azide as a preservative will substantially inhibit the enzyme activity of horseradish peroxidase.\u003c\/p\u003e\n\n\u003cp\u003eProperties and Storage Information:\u003cbr\u003e\nForm-Liquid, Purification technique-Affinity purification Protein G, Storage buffer-Preservative: 0.002% Thimerosal (merthiolate)Constituents: PBS, 1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C\u003c\/p\u003e\n\n\u003cp\u003eSupplementary Information:\u003cbr\u003e\nThis supplementary information is collated from multiple sources and compiled automatically.\u003cbr\u003e\nRubella virions also known as rubella virus particles are spherical and enveloped entities with an average diameter of 50-70 nm. These virions are composed mainly of three structural proteins: the capsid protein and the envelope glycoproteins E1 and E2. Within the host cell rubella virions replicate in the cytoplasm of infected epithelial cells. Their envelope derives from the host cell membrane highlighting their interaction with the infected host during budding.\u003cbr\u003e\nBiological function summary\u003cbr\u003e\nRubella virions serve as the infectious agents responsible for the transmission of rubella which is a contagious disease characterized by rash and fever. As individual units rubella virions do not form part of a complex with other viruses but require assembly via interactions among the capsid protein and envelope glycoproteins. The virion structure plays a central role in facilitating host cell receptor binding and membrane fusion which allows the virus to deliver its RNA genome into host cells for replication.\u003cbr\u003e\nPathways\u003cbr\u003e\nViral entry and replication mechanisms drive the activities of rubella virions. The virions exploit the endocytic pathway to enter host cells a process that is important for initiating infection. During replication non-structural proteins facilitate the synthesis of viral components. Important proteins in these processes include the E1 glycoprotein which is involved in receptor interaction and membrane fusion an integral part of the virion's infection cycle.\u003cbr\u003e\nRubella virions are primarily linked to rubella infection also known as German measles and congenital rubella syndrome. This viral infection triggers an immune response in the host involving cytokines and antibodies notably the anti-rubella antibody which helps clear the virus. Congenital rubella syndrome occurs when maternal infection during pregnancy results in significant developmental anomalies in the fetus. This association highlights the importance of monitoring and vaccination efforts to prevent these serious conditions.\u003c\/p\u003e","brand":"Abcam","offers":[{"title":"Default Title","offer_id":46860514787497,"sku":"ab20944","price":0.99,"currency_code":"USD","in_stock":true}],"url":"https:\/\/iright.com\/ar\/products\/abcam-ab20944","provider":"Iright","version":"1.0","type":"link"}