Ebola virus Glycoprotein/GP Protein RBD (AHX24649, HEK293, Fc)

Ebola virus glycoproteins (GPs) play a key role in the virus entry process, with GP1 serving as the receptor-binding subunit and GP2 for membrane fusion. GP downregulates host cell surface molecules, disrupts adhesion and may lead to disruption of vascular integrity. Ebola virus Glycoprotein/GP Protein RBD (AHX24649, HEK293, Fc) is the recombinant Virus-derived Ebola virus Glycoprotein/GP protein RBD, expressed by HEK293 , with C-hFc labeled tag. The total length of Ebola virus Glycoprotein/GP Protein RBD (AHX24649, HEK293, Fc) is 308 a.a., with molecular weight of ~57.6 KDa.

The trimeric GP1,2 complexes of the Ebola virus Glycoprotein (GP) play a crucial role in viral entry processes, where GP1 serves as the receptor-binding subunit and GP2 acts as the membrane fusion subunit. During later stages of infection, GP down-regulates the expression of various host cell surface molecules, including integrins such as ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV, and ITGB1, disrupting cell adhesion and contributing to the detachment of cells, potentially leading to blood vessel integrity disruption and hemorrhages. GP also interacts with host TLR4, stimulating the differentiation and activation of monocytes, resulting in bystander death of T-lymphocytes. Additionally, GP counteracts the antiviral effect of host BST2/tetherin, cooperates with VP40 and host BST2 to activate the canonical NF-kappa-B pathway, and functions as a decoy for anti-GP1,2 antibodies, contributing to viral immune evasion. Moreover, GP interacts with and activates host macrophages and dendritic cells, inducing the up-regulation of cytokine transcription through the activation of host TLR4.

Virus

HEK293

C-hFc

AHX24649 (M1-F308)

/

Approximately 57.6 kDa.

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.