Reagents and instruments for immunology, cell biology and molecular biology.

Yellow fever virus envelope glycoprotein E Antibody, HRP Conjugated

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Cat# bs-2041R-HRP

Size : 100ul

Brand : Bioss

bs-2041R-HRP [Conjugated Primary Antibody]

Yellow fever virus envelope glycoprotein E Antibody, HRP Conjugated

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DATASHEET

Host: Rabbit

Target Protein: Yellow fever virus envelope glycoprotein E

Immunogen Range: 601-700/3411

Clonality: Polyclonal

Isotype: IgG

Entrez Gene: 1502173

Swiss Prot: P03314

Source: KLH conjugated synthetic peptide derived from Yellow fever virus envelope glycoprotein E (IIVGRGDSRLTY)

Purification: Purified by Protein A.

Storage Buffer: Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.

Storage: Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Background:

Capsid 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.

Conjugation: HRP

Excitation/ Emission: N/A

Size: 100ul

Concentration: 1ug/ul

Applications: ELISA(1:500-1000)

Predicted Molecular Weight: 54/375

Cross Reactive Species: Virus
(Yellow fever virus)

For research use only. Not intended for diagnostic or therapeutic use.