CALIXAR offers a unique and patented technological platform allowing to isolate in solution – with the highest purity levels – full-length membrane proteins, while keeping their structural and functional integrity. Our approach represents the opportunity for pharmaceutical companies to start and work with high quality targets or antigens before developing antibodies, formulating vaccines and/or discovering a primary lead through Structure Based Drug Design or High Throughput Screening assays.
CALIXAR’s approach allows to preserve the original structure and function of membrane proteins (GPCRs, Ion Channels, Transporters, Receptors, Anchors and Viral Proteins) providing solutions for pharmaceutical industries, biotechnology companies and academic teams to develop conformational antibodies, formulate new vaccines, carry out Structure Based Drug Discovery and/or HTS assays. Moreover, the expertise is also specifically adapted to downstream processing (DSP) as well as upstream processing (USP – expression part).
To overcome this crucial issue, our company develops new tools and protocols for the deorphanization, identification, expression, extraction, purification, stabilization, structural functional characterization, crystallization of membrane proteins as well as detergent quantification. The starting biological material (virus, bacteria, primary cells, organs,…) can be endogenous or recombinant systems. CALIXAR uses original, innovative and customized chemistry that aims to adapt to the biochemical characteristics of the target during the solubilization/ purification/stabilization steps.
CALIXAR presentation at PEGS Summit: 08-12 April 2019
Anass JAWHARI - CSO of CALIXAR - will be giving a presentation on new exciting results obtained in collaboration with THERMOFISHER SCIENTIFIC.
13 March 2019
Novel innovative detergent family for MP extraction and stabilization
CALIXAR announces the publication of a new article in the framework of the CHEM2STAB common laboratory.
20 February 2019
CALIXAR and ASTRAZENECA to publish new insight on KCC2 architecture and function in Scientific Reports
28 November 2017