Recombinant Crimean-Congo hemorrhagic fever virus Envelopment polyprotein (GP), partial (Active)

Crimean-Congo hemorrhagic fever virus (CCHFV) Envelopment polyprotein (GP) is the major surface glycoprotein that mediates viral attachment, membrane fusion and host cell entry, serving as the primary target for vaccine development, diagnostic assay design and antiviral therapeutic research against this highly pathogenic hemorrhagic fever virus. This mammalian-expressed partial construct spanning residues 1078–1439 carries a C-terminal 10×His tag for efficient purification, with a theoretical molecular weight of 42.2 kDa. Functional ELISA validation demonstrates specific binding to an anti-GP recombinant antibody (CSB-RA810349MA1CSC) with an EC50 of 3.136–3.585 ng/mL when immobilized at 2 μg/mL, confirming that the native conformational epitopes critical for antibody recognition are preserved. The quantified binding activity supports use in antibody development and validation workflows, including epitope mapping, competitive inhibition screening, and neutralizing antibody characterization for CCHFV research and countermeasure development. With >95% purity verified by SDS-PAGE and endotoxin levels below 1.0 EU/μg as determined by the LAL method, this lyophilized active protein meets the rigorous quality thresholds required for surface plasmon resonance affinity characterization, biolayer interferometry kinetic studies, and use as a positive control in CCHFV diagnostic assays and viral entry mechanism investigations.