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Item No. 40878

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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWMiddle East respiratory syndrome coronavirus (MERS-CoV) is an enveloped positive-stranded RNA virus, a member of the Betacoronavirus genus, and a causative agent of MERS, an acute respiratory disease that often leads to pneumonia and renal failure.1,2 The MERS-CoV nucleocapsid protein is composed of an intrinsically disordered region (IDR), an N-terminal domain that binds RNA, a flexible linker containing serine and arginine phosphorylation sites, a C-terminal domain that also participates in RNA binding and is responsible for dimerization, and another IDR.3,4 Coronavirus nucleocapsid proteins, including the MERS-CoV nucleocapsid protein, package the viral genome into a ribonucleoprotein (RNP) complex.4 In addition, the MERS-CoV nucleocapsid protein interacts with the ubiquitin ligase TRIM25 and inhibits the activation of retinoic acid-inducible gene I (RIG-I) and phosphorylation of IFN regulatory factor 3 (IRF3) and NF-κB.5 It reduces IFN-β and IFN-λ1 promoter activity induced by the RIG-I caspase activation and recruitment domain (RIG-I-CARD), but not MDA5-CARD, and reduces Sendai virus-induced increases in IFN-β and IFN-λ1 mRNA levels. Cayman's MERS-CoV Nucleocapsid Protein (recombinant) consists of 424 amino acids and has a calculated molecular weight of 46.51 kDa.
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1. MERS-
2. SARS-
3. Structural characterization of the N-
4. Comparing the nucleocapsid proteins of human coronaviruses: Structure, immunoregulation, vaccine, and targeted drug. Front. Mol. Biosci. 9, 761173 (2022).
5. Middle East respiratory syndrome coronavirus nucleocapsid protein suppresses type I and type III interferon induction by targeting RIG-