Anti-Respiratory Syncytial Virus Fusion (F) Glycoprotein antibody [RSV5A6],Abcam,AB94968

What is this antibody validated in? Anti-Respiratory Syncytial Virus Fusion (F) Glycoprotein antibody [RSV5A6] (ab94968) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Immunohistochemistry (IHC-P), Immunohistochemistry (IHC-Fr), Immunocytochemistry/immunofluorescence (ICC/IF), ELISA in Respiratory syncytial virus samples. What is the molecular weight of Respiratory Syncytial Virus Fusion (F) Glycoprotein? Anti-Respiratory Syncytial Virus Fusion (F) Glycoprotein [RSV5A6] (ab94968) specifically detects a band for Respiratory Syncytial Virus Fusion (F) Glycoprotein (UniProt: P03420) at a molecular weight of 63kDa.

Host

Mouse

Reactivity

Respiratory syncytial virus

Application

ELISA, IHC-Fr, WB, ICC/IF, IHC-P

Platform ID

BAB330563076

Abcam

Headquarters

Discovery Drive Cambridge Biomedical Campus Cambridge CB2 0AX UK

Contact

Tel: +44 (0)1223 696000
Fax: +44 (0)1223 215 215

Product Specifications
Scientific Background

Specifications

NameAnti-Respiratory Syncytial Virus Fusion (F) Glycoprotein antibody [RSV5A6]
Cat. No.AB94968
HostMouse
IsotypeIgG2a
ReactivityRespiratory syncytial virus
ApplicationELISA, IHC-Fr, WB, ICC/IF, IHC-P
ClonalityMonoclonal
Clone NumberRSV5A6
Concentration1 mg/mL Batch dependent concentration
ImmunogenCell preparation containing F protein. The exact immunogen used to generate this antibody is proprietary information.
PurityAffinity purification Protein A
Appearance/FormLiquid
ShippingBlue Ice
FormulationPreservative: 0.02% Sodium azide Constituents: 99.98% PBS
Storage-20°C
Regulatory StatusResearch Use Only

Scientific Background

Target data Fusion glycoprotein F0. Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.. Fusion glycoprotein F1. Class I viral fusion protein (PubMed : 23618766). Under the current model, the protein has at least 3 conformational states : pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state (PubMed : 23618766). During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain (PubMed : 19966279, PubMed : 23618766). The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm (PubMed : 23593008, PubMed : 23618766). This fusion is pH independent and occurs at the plasma or endosomal membrane (Probable). The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed : 10864656). F protein is involved in the entry into the host cell through the interaction with host IGF1R (PubMed : 32494007). This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1 (PubMed : 21841784, PubMed : 32494007). Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (PubMed : 10438814). F protein may trigger p53-dependent apoptosis (PubMed : 18216092).. Fusion glycoprotein F2. Major determinant of the species specificity of RSV infection (PubMed : 12663767). The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed : 10864656). F protein is involved in the entry into the host cell through the interaction with host IGF1R (PubMed : 32494007). This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1 (PubMed : 32494007). Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (PubMed : 10438814). F protein seems to trigger p53-dependent apoptosis (PubMed : 18216092). See full target information F

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