Yellow fever virus envelope glycoprotein E Antibody
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Catalog numberbs-2041R
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Price:
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Size0.1ml
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Long nameYellow fever virus envelope glycoprotein E Antibody
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Also known asYellow fever virus envelope glycoprotein E Antibody
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CategoryPrimary Antibodies
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ConjugationUnconjugated
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Target AntigenYellow fever virus envelope glycoprotein E
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SpecificityThis is a highly specific antibody against Yellow fever virus envelope glycoprotein E.
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Modification sNone
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Modification site sUnmodified antibody
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ClonalityPolyclonal antibody
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Clone numberPolyclonal antibody
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Concentration1ug per 1ul
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Immunogen range650-700/3411
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Subcellular locationExtracellular
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SourceKLH conjugated synthetic peptide derived from Yellow fever virus envelope glycoprotein E (IIVGRGDSRLTY)
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Gene ID number1502173
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Swiss ProtP03314
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Tested ApplicationsIHC-P, IF(IHC-P)
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Recommended dilutionsIHC-P(1:100-500), IF(IHC-P)(1:50-200)
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Cross reactivityVirus
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Cross reactive species detailsYellow fever virus
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Background of the target antigenCapsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3. 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 (By similarity). Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex.
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Purification methodThis antibody was purified via Protein A.
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Storage conditionsKeep the antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Store at -20°C for up to 1 year.
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Synonym namesGenome polyprotein
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PropertiesIf you buy Antibodies supplied by Bioss Primary Unconjugated Antibodies they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.
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French translationanticorps
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Gene target
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Short nameAnti-Yellow fever virus envelope glycoprotein E
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TechniqueAntibody, antibodies against human proteins, antibodies for
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HostRabbit (Oryctolagus cuniculus)
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IsotypeImmunoglobulin G (IgG)
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Labelyellow
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SpeciesVirus, Viruses
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Alternative nameYellow fever virus envelope glycoprotein E Antibody
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Alternative techniqueantibodies
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Virusfever
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MeSH Data
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Name
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ConceptScope note: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
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Tree numbers
- E05.196.401.143
- E05.301.300.096
- E05.478.566.320.200
- E05.601.262
- E05.601.470.320.200
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Qualifiersethics, trends, veterinary, history, classification, economics, instrumentation, methods, standards, statistics & numerical data