呼吸道合胞病毒编码的多种蛋白质，包括融合蛋白和附着蛋白，负责病毒入侵宿主细胞及诱导免疫反应。
| 产品号 | 产品名称 | 蛋白编码 | 图片 |
|---|---|---|---|
| ALP6267 | P11209(Phe22-Thr529) |
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| The fusion glycoprotein F0/F protein is cleaved to generate mature F1 and F2 fusion glycoproteins.It functions as a viral fusion protein, promoting the fusion of virus and cell membranes through different state transitions. | |||
| ALP6245 | P03420.1(Gln26-Thr529) |
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| Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. The G protein mediates attachment of the virus to cell surface receptors, while the F protein promotes fusion of the viral and cellular membranes, allowing entry of the virus ribonucleoprotein into the cell cytoplasm. The fusion (F) protein of RSV is synthesized as a nonfusogenic precursor protein (F), which during its migration to the cell surface is activated by cleavage into the disulfide-linked F1 and F2 subunits. This fusion is pH independent and occurs directly at the outer cell membrane, and the F2 subunit was identifed as the major determinant of RSV host cell specificity. The trimer of F1-F2 interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and induces the fusion between host cell and virion membranes. Notably, RSV fusion protein is unique in that it is able to interact directly with heparan sulfate and therefore is sufficient for virus infection. Furthermore, the fusion protein is also able to trigger p53-dependent apoptosis. | |||
| ALP6310 | P27022-1(Asn66-Arg297) |
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| Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. HRSV G protein is a type II glycoprotein of 289-299 amino acids (depending on the virus strain) with a signal/anchor hydrophobic domain and is extensively modified by the addition of both N-and O-linked oligosaccharides to achieve the mature form of 8-9 kDa. The C-terminal ectodomain of the G protein has a central region and four cysteines which are conserved in all HRSV isolates and have been proposed as the putative receptor binding site. The G protein mediates attachment of the virus to the host cell membrane by interacting with heparan sulfate, initiating the infection. As similar to mucins in amino acid compositions, the RSV G protein can interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, and thus modulates the immune response and facilitate infection. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. Unlike the other paramyxovirus attachment proteins, HRSV-G lacks both neuraminidase and hemagglutinating activities. | |||
| ALP6333 |
Recombinant Human RSV (B1) glycoprotein G / RSV-G Protein (C-His Tag) 重组蛋白Human RSV (B1) glycoprotein G / RSV-G Protein (C-His Tag) |
O36633-1(His67-Ala299) |
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| Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. HRSV G protein is a type II glycoprotein of 289-299 amino acids (depending on the virus strain) with a signal/anchor hydrophobic domain and is extensively modified by the addition of both N-and O-linked oligosaccharides to achieve the mature form of 8-9 kDa. The C-terminal ectodomain of the G protein has a central region and four cysteines which are conserved in all HRSV isolates and have been proposed as the putative receptor binding site. The G protein mediates attachment of the virus to the host cell membrane by interacting with heparan sulfate, initiating the infection. As similar to mucins in amino acid compositions, the RSV G protein can interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, and thus modulates the immune response and facilitate infection. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. Unlike the other paramyxovirus attachment proteins, HRSV-G lacks both neuraminidase and hemagglutinating activities. | |||
| ALP23092 | AII22117(S64-K321) |
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| RSV G protein is a type II, highly glycosylated membrane protein with a full length of 292-319 amino acids (AA), an intracellular cytoplasmic tail (AA 1-37), and a transmembrane domain (AA 38 -66) and the extracellular domain ending in its carboxyl terminus.The RSV G protein has broad effects on the biology of RSV infection as well as host immune responses and infection-associated diseases. | |||
| ALP23130 |
Recombinant Fusion glycoprotein F0/F Protein,HRSV,E. coli,His,N-B2M |
P03420(N27-T529) |
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| The fusion glycoprotein F0/F protein is initially an inactive precursor that is cleaved by furin-like proteases to produce the mature F1 and F2 fusion glycoproteins. As a class I viral fusion protein, it undergoes prefusion, prehairpin, and postfusion states. | |||
