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CUSABIO used viral structural constituents in the form of recombinant proteins produced in mammalian cells to generate the recombinant human C5AR1 virus-like particle (VLP). The recombinant human C5AR1 VLP contains a C-terminal 10xHis-tag. Its expression region codes for the full-length human C5AR1 protein. It contains endotoxin less than 1.0 EU/ug determined by the LAL method. It has been confirmed to be an active protein through a functional ELISA. This recombinant C5AR1 protein can bind to the recombinant antibody against C5AR1, with the EC50 of 1.239-3.760 ng/mL.
C5AR1 is widely expressed in various cell types, with the highest expression level in neutrophils. C5AR1/C5a interaction mediates a variety of biological effects, such as stimulating myeloid-derived cells such as neutrophils and monocyte-macrophages to release histamine and lysosomal enzymes, inducing smooth muscle contraction, enhancing vascular permeability, recruiting inflammatory cells such as neutrophils and monocytes to the inflammatory sites, promoting endothelial cells to express adhesion molecules, as well as playing an immunoregulatory role by inducing or inhibiting the release of cytokines from monocytes. Considering the key roles in innate immunity, targeting the C5AR1/C5a signaling pathway can treat a variety of related diseases, including chronic kidney disease, cardiovascular disease, neurological disease, and cancer.
Applications : Binding assay/Protein-protein interaction
Review: I used the CSB-MP003996HU protein for an ELISA experiment, and the EC50 was measured to be 0.8830-2.771 ng/ml, indicating good protein activity. In the subsequent antibody screening, we employed flow cytometric analysis to determine whether this protein can bind to molecules expressed on the cell surface. The results showed that some antibodies were able to bind to this protein. The protein quality is quite good.