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HRSV Pre-Fusion glycoprotein F0 (site V) Specific ELISA Kit

For research use only.

组分(Materials Provided)

IDComponentsSize
RAS202-C01Pre-coated Anti-RSV-Pre-Fusion glycoprotein F0 (site V) Antibody Microplate1 plate
RAS202-C02Pre-Fusion glycoprotein F0 (RSV) Standard15 μg
RAS202-C03HRP-Anti-Pre-Fusion glycoprotein F0 (RSV) Antibody20 μg
RAS202-C0410×Washing Buffer 50 mL
RAS202-C052×Dilution Buffer50 mL
RAS202-C06Substrate Solution12 mL
RAS202-C07Stop Solution7 mL

产品概述(Product Overview)

Respiratory syncytial virus (RSV) is a highly contagious virus causing severe infection in infants and the elderly. Various approaches are being used to develop an effective RSV vaccine. The RSV fusion (F) subunit, particularly the cleaved trimeric pre-fusion F, is one of the most promising vaccine candidates under development.

A rapid and effective assay kit detecting the levels of HRSV Pre-Fusion glycoprotein F0 is urgently needed to accelerate the development of RSV vaccines.

应用说明(Application)

The kit has been tested to specifically identify HRSV (A) and HRSV (B) Pre-Fusion glycoprotein. It was developed for the specific quantitative detection of HRSV Pre-Fusion glycoprotein F0 (site V) in samples.

It is for research use only.

重构方法(Reconstitution)

Please see Certificate of Analysis for details of reconstitution instruction and specific concentration.

存储(Storage)

2-8℃

 

典型数据-Typical Data Please refer to DS document for the assay protocol.

Pre-Fusion glycoprotein F0 TYPICAL DATA

For each experiment, a standard curve needs to be set for each micro-plate, and the specific OD value may vary depending on different laboratories, testers, or equipments. The following example data is for reference only.

 
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前沿进展

Crystallization and preliminary X-ray diffraction analysis of post-fusion six-helix bundle core structure from Newcastle disease virus F protein
Li, Zhu, Wu et al
Acta Crystallogr D Biol Crystallogr (2003) 59 (Pt 7), 1296-8
Abstract: Fusion of virus members from the Paramyxoviridae family involves two glycoproteins. They are termed attachment glycoprotein (HN, H or G) and fusion protein (F). The F protein contains two highly conserved heptad-repeat (HR) regions, HR1 and HR2. Through conformational changes in the F protein, HR1 and HR2 are believed to form a stable six-helix coiled-coil bundle during the membrane-fusion process. However, no crystal structure has yet been documented for this state in the Newcastle disease virus (NDV, a member of the Paramyxoviridae family) F protein, despite the recent success on its F(0) crystal structure (Chen et al., 2001), which was thought to represent the pre-fusion conformation of F glycoprotein. In this study, a single-chain polypeptide constructed by linking two truncated HR regions of the NDV F protein has been expressed, purified and crystallized by means of the hanging- or sitting-drop vapour-diffusion method. Crystals in hexagonal and trapezoid forms with a resolution limit of 2.6 A were obtained. These crystals belonged to space group C2, with unit-cell parameters a = 66.4, b = 38.2, c = 102.0 A, beta = 100.2 degrees. Crystals in the rhombic form with a resolution limit of 2.5 A were also obtained. These crystals belonged to space group P2(1), with unit-cell parameters a = 59.0, b = 31.9, c = 62.3 A, beta = 117.0 degrees. This will add to the repertoire of viral fusion protein post-fusion state structures and help further the understanding of the molecular mechanism of enveloped virus fusion.
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