Pre-formed fibrils are an invaluable preclinical model for exploring pathogenesis of neurological diseases through aggregation of misfolded proteins. Explore our pre-seeded PFFs to use in your research.
Neural factors are a class of protein molecules with neurotrophic activity that can promote the survival and regeneration of nerve cells. Explore our series of recombinant neural factors to support the culture and differentiation of nerve cells.
Partnering with Diagnostic Biochips, we now provide solutions for in vivo electrophysiology recordings, including high-quality multi-channel electrodes and other products to facilitate high-quality, efficient analysis of neural circuit structure and function.
Protein markers are an essential component in biological research and drug development. Whether it is for protein electrophoresis or western blot, our pre-stained protein markers help you quickly determine the molecular weight of the target protein or evaluate the transfer efficiency.
Streptavidin is a tetrameric protein providing 4 high-affinity biotin binding sites. We offer a wide array of products pre-conjugated with streptavidin to support your research as well as biotinylated proteins.
Setting the corresponding isotype control antibody to detect non-specific binding can reduce the generation of false positive results and evaluate the possible influencing factors accurately in the drug development process. Explore our isotype controls for your research.
The efficacy of a therapeutic antibody depends on the Fab fragment and its binding activity to the target antigen, but also depends on the Fc fragment and its interaction with key Fc receptors.Therefore, candidates must be tested against a panel of receptors during antibody engineering. Explore our comprehensive collection of recombinant Fc receptor proteins!
Pseudoviruses are virus particles that have altered nucleic acid sequences within their genome to ensure they are replication-deficient and non-pathogenic. Explore our catalog of pseudoviruses & services!
Anti-Nipah/Hendra Glycoprotein G Antibody, Human IgG1 captured on Protein A Chip can bind Nipah virus Glycoprotein G, His Tag (Cat. No. GLN-N52H3) with an affinity constant of 0.188 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).
Anti-Nipah/Hendra Glycoprotein G Antibody, Human IgG1 captured on Protein A Chip can bind Hendra virus Glycoprotein, His Tag (Cat. No. GLN-H52H3) with an affinity constant of 12.3 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).
Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. G is a type II homotetrameric transmembrane protein responsible for binding to ephrinB2 or ephrinB3 (ephrinB2/B3) receptors. F is a homotrimeric type I transmembrane protein that is synthesized as a premature F0 precursor and cleaved by cathepsin L during endocytic recycling to yield the mature, disulfide-linked, F1 and F2 subunits. Upon binding to ephrinB2/B3, NiV G undergoes conformational changes leading to F triggering and insertion of the F hydrophobic fusion peptide into the target membrane. Subsequent refolding into the more stable post-fusion F conformation drives merger of the viral and host membranes to form a pore for genome delivery to the cell cytoplasm.
Clinical and Translational Updates
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