Anti-DYKDDDDK affinity agarose is made by covalent coupling of high-quality DYKDDDDK mouse monoclonal antibody and agarose gel. It has the characteristics of high binding capacity of protein, high specificity, stability and repeatability. It can be used for affinity purification and immuno (co) precipitation of DYKDDDDK tagged fusion proteins.
Anti-DYKDDDDK immunomagnetic beads is made by covalently coupling high-quality DYKDDDDK mouse monoclonal antibody and magnetic beads, It has characteristics of high binding capacity of protein, high specificity, fast and convenient operation, stability and repeatability. It can be used for affinity purification and immuno (co) precipitation of DKKDDDDK tagged fusion proteins.
Anti-DYKDDDDK-tag fast IP kit is composed of Anti-DYKDDDDK affinity gel, Mouse IgG affinity gel, DYKDDDDK-Tag Rabbit pAb and Goat Anti-Rabbit IgG(peroxidase/HRP conjugated), which is used for fast, efficient and specific (Co)IP of DYKDDDDK tag fusion protein.Anti-DYKDDDDK affinity gel is made by covalent coupling of high-quality DYKDDDDK-Tag Mouse mAb and Sepharose 4B agarose granules. It has the characteristics of high binding capacity of protein, high specificity and stability. Mouse IgG affinity gel is used as the control for CoIP experiment, and its properties are stable. The DYKDDDDK-Tag Rabbit pAb antibody has the advantages of high specificity, high affinity and high valence; Goat Anti-Rabbit IgG (peroxidase/HRP conjugated) is purified by cross-adsorption and only DYKDDDDK-Tag Rabbit pAb is identified, and there is no cross-reaction with the heavy-chain and light-chain of the mouse monoclonal antibody. The four components are strictly inspected and can be used independently; the combination of four sets has the advantages of fast, convenience and no interference band.
The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and a 11 kDa secreted glycoprotein (sGP). Both GP and sGP have an identical 295-residue N-terminus, however, they have different C-terminal sequences. Recently, great attention has been paid to GP for vaccines design and entry inhibitors isolation. GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . The GP1 subunit contains a mucin domain and a receptor-binding domain (RBD); the GP2 subunit has a fusion peptide, a helical heptad-repeat (HR) region, a transmembrane (TM) domain, and a 4-residue cytoplasmic tail. The RBD of GP1 mediates the interaction of EBOV with cellular receptor (e.g. DC-SIGN/LSIGN, TIM-1, hMGL, NPC1, β-integrins, folate receptor-α, and Tyro3 family receptors), of which TIM1 and NPC1 are essential for EBOV entry; the mucin domain having N- and O-linked glycans enhances the viral attachment to cellular hMGL, and participates in shielding key neutralization epitopes, which helps the virus evades immune elimination. There are large conformation changes of GP2 during membrane fusion, which enhance the insertion of fusion loop into cellular membrane and facilitate the release of viral nucleocapsid core to cytoplasm.
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