Human respiratory syncytial virus (RSV) Glycoprotein G / RSV-G Antibody, Rabbit Pab

Cat: 11070-RP01
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Human respiratory syncytial virus (RSV) Glycoprotein G / RSV-G Antibody, Rabbit Pab (Rabbit Polyclonal antibody) General Information
Product name
Human respiratory syncytial virus (RSV) Glycoprotein G / RSV-G Antibody, Rabbit Pab
Validated applications
WB,ELISA (Antibody's applications have not been validated with corresponding viruses. Optimal concentrations/dilutions should be determined by the end user.)
Application notes
(Antibody's applications have not been validated with corresponding viruses. Optimal concentrations/dilutions should be determined by the end user.)
Specificity
RSV RSV Glycoprotein G
Immunogen
Recombinant Human RSV Glycoprotein G / RSV-G (Catalog#11070-V08H)
Preparation
Produced in rabbits immunized with purified, recombinant Human respiratory syncytial virus glycoprotein G (HRSV-G; Catalog#11070-V08H; His 67-Arg 297; AAB59857.1). Total IgG was purified by Protein A affinity chromatography.
Source
Polyclonal Rabbit IgG
Purification
Protein A
Formulation
0.2 μm filtered solution in PBS
Conjugate
Unconjugated
Form
Liquid
Shipping
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Storage
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Human respiratory syncytial virus (RSV) Glycoprotein G / RSV-G Antibody, Rabbit Pab (Rabbit Polyclonal antibody) Validated Applications
Application Dilution Notes
WB his antibody can be used at 1:500-1:1000 with the appropriate secondary reagents to detect HRSV glycoprotein G in WB.  
ELISA 1:1000-1:2000  

**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********

Human respiratory syncytial virus (RSV) Glycoprotein G / RSV-G Antibody, Rabbit Pab Alternative Names
Anti-G Antibody
RSV Glycoprotein G Background Information

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 80-90 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.

References
  • Martin-Gallardo A. et al., 1993, J Gen Virol. 74 : 453-8.
  • Jose AM. et al.,1997, J Gen Virol. 78: 2411-8.
  • Feldman SA. et al., 1999, J Virol. 73: 6610-7.
  • García-Beato R. et al., 2000, J Gen Virol. 81: 919-27.
  • Zlateva KT. et al., 2004, J Virol. 78: 4675-83.
  • Trento A. et al., 2006, J Virol. 80: 975-84.
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