Recombinant Nipah Virus G Protein
Referência DRA265-500ug
Tamanho : 500ug
Marca : Novoprotein
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Description Recombinant Nipah virus Glycoprotein G is produced by our Mammalian expression system and the target gene encoding Gln71-Thr602 is expressed with a 6His tag at N-terminus.
Accession Q9IH62
Known As Glycoprotein G; G
Mol Mass 60.1 kDa
APMol Mass 65-85 kDa, reducing conditions
Formulation Description Supplied as a 0.2 μm filtered solution of PBS, pH7.4.
Purity-SDS-PAGE 
Greater than 95% as determined by reducing SDS-PAGE. (QC verified) Bioactivity-ELISA 
Immobilized Recombinant Nipah Virus G Protein(DRA265) at 2μg/ml (100 μl/well) can bind Recombinant Human EFNB2 (C-6His)(C465)*. *: Biotinylated by NHS-biotin prior to testing.The ED50 of Recombinant Human EFNB2 (C-6His)(C465) is 6.92ng/ml.(Regularly tested) Bioactivity-BLI 
Loaded Nipah Virus G Antibody (3G8) (DA150) on AMC Biosensor, can bind Recombinant Nipah Virus G Protein(DRA265) with an affinity constant of 10.3 pM as determined in BLI assay. (Regularly tested) Storage - Reconstituted protein solution should be stored at ≤ -20°C.
- Stable for at least 24 months when stored as instructed.
Shipping The product is shipped on dry ice pack.Upon receipt, store it immediately at the temperature listed below.
Background Nipah virus is bat-borne paramyxoviruses that are the prototypic members of the genus Henipavirus. And the virus first appeared in Malaysia and subsequent outbreaks have occurred in Bangladesh and India. Their broad species tropism and ability to cause fatal respiratory and/or neurologic disease in humans and animals make them important transboundary biological threats. The viral G glycoprotein is an effective post-exposure treatment against Hendra and Nipah virus infection. The G protein is a type II membrane glycoprotein of 602 amino acids and functions primarily as receptor-binding protein, and G glycoprotein monomer consists of a stalk and globular head. Besides its function in receptor binding, the G protein is essentially required for F-mediated fusion of lipid membranes.