MERS Spike protein trimer (R748A, R751A, V1060P, L1061P), His Tag (MALS verified)

The MERS or Middle East Respiratory Syndrome Coronavirus, is a member of the coronavirus family and is known to cause severe respiratory illness in humans. The MERS protein is a type I transmembrane protein that plays a vital role in the virus's ability to infect host cells. It is composed of three main domains: the extracellular domain, the transmembrane domain, and the cytoplasmic domain. The extracellular domain, further divided into S1 and S2 subunits, is responsible for receptor recognition and binding. The S1 subunit contains the Receptor Binding Domain (RBD), which is crucial for the virus's attachment to and entry into host cells. The RBD specifically interacts with the host cell receptor, facilitating the initial step of infection. The S2 subunit, on the other hand, is responsible for membrane fusion. It contains a fusion peptide that inserts into the host cell membrane, initiating the fusion process. This fusion allows the virus's genetic material to be released into the host cell, initiating the infection process.

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 145.9 kDa. The protein migrates as 150 kDa and 175-200 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

-20°C to -70°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Immobilized Human DPPIV, Fc Tag (Cat. No. DP4-H5266) at 5 μg/mL (100 μL/well) can bind MERS Spike protein trimer, His Tag (Cat. No. SPN-M52H5) with a linear range of 0.1-3 ng/mL (QC tested).