simplex

Major allergen Ani s 1 Protein, Anisakis simplex, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 26.3 kDa and the accession number is Q7Z1K3.

CD112 is a type I transmembrane glycoprotein belonging to the Immunoglobulin superfamily. It comprises one Ig-like V-type domain and two Ig-like C2-type domains in the extracellular region. The V domain is believed to mediate nectin binding to its ligands. Nectin2 is known to bind the pseudorabies virus, and herpes simplex virus2 (HSV2), involving in cell to cell spreading of these viruses. It does not bind poliovirus. As a homophilic adhesion molecule, CD112 is found concentrated in adherens junctions, and exists on neurons, endothelial cells,epithelial cells and fibroblasts. CD112 has been identified as the ligand for DNAM-1 (CD226), and the interaction of CD226 CD112 mediates cytotoxicity and cytokine secretion by T and NK cells. The costimulatory responses may be a critical component in allergic reactions and may therefore become targets for anti-allergic therapy.

Herpes simplex viruses (human herpesviruses types 1 and 2) commonly cause recurrent infection affecting the skin, mouth, lips, eyes, and genitals. Herpes simplex virus type 2 (HSV-2) infection is responsible for significant neurological morbidity, perhaps more than any other virus. Herpes simplex virus type 2–associated neurological disease may result from primary infection or reactivation of latent HSV-2. Common severe infections include encephalitis, meningitis, neonatal herpes, and, in immunocompromised patients, disseminated infection.

Herpes simplex virus type 2 (HSV-2) is the predominant cause of genital ulcer disease in human. Glycoprotein E (gE) and glycoprotein I (gI) are expressed as a heterodimer on the surface of Herpes simplex virus (HSV). Glycoprotein E binds Fc domain of immunoglobulin G (IgG) and inhibits activities mediated by the IgG Fc domain, contributing to immune evasion by HSV.