Product Name	Anti-Yellow fever virus envelope glycoprotein E/HRP
Chinese Name	辣根过氧化物酶标记的黄热病毒包膜glycoprotein抗体
Alias	Envelope protein E; Genome polyprotein; polyprotein [Yellow fever virus]; polyprotein YFV; POLG_YEFV1; YFVgp1; YFVgp1 polyprotein precursor [ Yellow fever virus ].
Research Area	immunology  Bacteria and viruses
Immunogen Species	Rabbit
Clonality	Polyclonal
React Species
Applications	WB=1:500-2000 ELISA=1:100-1000 IHC-P=1:50-200 IHC-F=1:50-200  not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user.
Molecular weight	54/375kDa
Form	Lyophilized or Liquid
Concentration	1mg/ml
immunogen	KLH conjugated synthetic peptide derived from Yellow fever virus envelope glycoprotein E (IIVGRGDSRLTY)
Lsotype	IgG
Purification	affinity purified by Protein A
Storage Buffer	0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Storage	Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Product Detail	background: 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. Function: Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA. 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. 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. 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 (Potential). 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. NS4A might also regulate the ATPase activity of the NS3 helicase (By similarity). Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. Non-structural protein 4B 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 (By similarity). RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) 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 genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway Subunit: Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. Subcellular Location: Capsid protein C: Virion (Potential). Peptide pr: Secreted. Small envelope protein M: Virion membrane; Multi-pass membrane protein (Potential). Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Envelope protein E: Virion membrane; Multi-pass membrane protein (Potential). Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=Remains non-covalently associated to NS3 protease. Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Located in RE-associated vesicles hosting the replication complex. Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein. RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Host nucleus. Note=Located in RE-associated vesicles hosting the replication complex. Post-translational modifications: Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site (By similarity). RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. Envelope protein E and non-structural protein 1 are N-glycosylated. Similarity: In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 mRNA cap 0-1 NS5-type MT domain. Contains 1 peptidase S7 domain. Contains 1 RdRp catalytic domain. Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

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