mCherry, a red fluorescent protein derived from sea anemone (Discosoma sp.), is composed of 266 amino acids. Because of its color and light stability of monomer molecules, it performs better than other fluorescent protein tags. mCherry is often used as eukaryotic protein recombinant expression marker.Anti-mCherry nanobody affinity gel is made by covalently coupling high-quality mCherry nanobody with agarose gel. As the nanobody only contains the variable region of antibody molecules, there will be no signal interference from the heavy and light chains of the antibody during immuno (co) precipitation. It has the characteristics of high binding capacity of protein, high specificity and stability, and can be used for immuno (co) precipitation of mCherry tagged fusion protein.
mCherry, a red fluorescent protein derived from sea anemone (Discosoma sp.), is composed of 266 amino acids. Because of its color and light stability of monomer molecules, it performs better than other fluorescent protein tags. mCherry is often used as eukaryotic protein recombinant expression marker.Anti-mCherry nanobody immunomagnetic beads are made by covalently coupling high-quality mCherry nanobody with magnetic beads. It has the characteristics of high binding capacity of protein, high specificity and stability, fast and convenient operation, repeatability and can be used for immuno (co) precipitation of mCherry tagged fusion proteins.
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
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