Anti-Human RSV (B1) glycoprotein G / RSV-G Magnetic Beads Immunoprecipitation (IP) Kit

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Anti-RSV Glycoprotein G Magnetic Beads-IP Kit Product Components

Components Storage
Anti-RSV Glycoprotein G Magnetic Beads1,3 2-8℃ for 12 months
NP40 Cell Lysis Buffer2 -20℃ for 12 months
5×TBST(pH7.4)  
1×TBST(pH7.4)  
ddH2O  
Alkaline Elution Buffer 2-8℃ for 12 months
Acidity Elution Buffer 2-8℃ for 12 months
Neutralization Buffer 2-8℃ for 12 months

【1】The IP KIT contains anti-RSV Glycoprotein G magnetic Beads (2 mg/mL) in phosphate buffered saline (PBS, pH 7.4) with sodium azide (0.1%).

【2】Using NP-40 cell lysate buffer in the kit is required,otherwise,the magnetic beads may be precipitated.

【3】Shipping: Magnetic Beads kits are shipped at ambient temperature in which magnetic beads are provided in liquid buffer.

Anti-RSV Glycoprotein G Magnetic Beads-IP Kit Product Description

The Anti-RSV Glycoprotein G magnetic Beads, conjugated with Anti-RSV Glycoprotein G antibody, are used for immuneprecipitation (IP) of RSV Glycoprotein G proteins which expressed in vitro expression systems. For IP, the beads are added to a sample containing RSV Glycoprotein G proteins to form a bead-protein complex. The complex is removed from the solution manually using a magnetic separator. The bound RSV Glycoprotein G proteins are dissociated from the magnetic beads using an elution buffer.

Anti-RSV Glycoprotein G Magnetic Beads-IP Kit Antibody Information

Antibody
Human RSV (B1) glycoprotein G / RSV-G Antibody, Rabbit PAb, Antigen Affinity Purified(13029-T52)
Immunogen
Recombinant Human RSV (B1) glycoprotein G / RSV-G Protein (Catalog#13029-V08H)
Species Reactivity
Human RSV (B1) glycoprotein G / RSV-G
Source
Polyclonal RSV Rabbit IgG
Preparation
Produced in rabbits immunized with purified, recombinant Human RSV (B1) glycoprotein G / RSV-G ( Catalog#13029-V08H; O36633-1; His67-Ala299). Human RSV (B1) glycoprotein G / RSV-G specific IgG was purified by Human RSV (B1) glycoprotein G / RSV-G affinity chromatography.
Applications
Immunoprecipitation (IP), Minimum Protein Purification

Anti-Human RSV (B1) glycoprotein G / RSV-G Magnetic Beads Immunoprecipitation (IP) Kit: Alternative Names

Anti-GALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit

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 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.
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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