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 viruss 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 viruss 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 viruss genetic material to be released into the host cell, initiating the infection process. - Proteine/Peptide
Immobilized Human DPPIV, Fc Tag (Cat. No. DP4-H5266) at 5 µg/mL (100 µL/well) can bind MERS S protein RBD, His Tag (Cat. No. SPD-M52H6) with a linear range of 0.6-5 ng/mL (QC tested).
Immobilized MERS S protein RBD, His Tag (Cat. No. SPD-M52H6) at 5 µg/mL (100 µL/well) can bind Monoclonal Anti-SARS-CoV-S protein RBD Antibody, Human IgG1 with a linear range of 0.313-2.5 µg/mL (Routinely tested).
MERS S protein RBD, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
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