Recombinant Human CD112/Nectin-2 Protein (Active) | PKSH031939

Recombinant Human CD112/Nectin-2 Protein (Active) | PKSH031939 | Gentaur US, UK & Europe Disrtribition

Synonyms: Poliovirus Receptor-Related Protein 2; Herpes Virus Entry Mediator B; Herpesvirus Entry Mediator B; HveB; Nectin-2; CD112; PVRL2; HVEB; PRR2

Active Protein: Active protein

Activity: The mature form of recombinant human CD112 (NP_002847.1) extracellular domain (Met 1-Leu 360) with quinary-aa peptide (DDDDK) at the C-terminus was expressed and purified.

Protein Construction: The mature form of recombinant human CD112 (NP_002847.1) extracellular domain (Met 1-Leu 360) with quinary-aa peptide (DDDDK) at the C-terminus was expressed and purified.

Fusion Tag:

Species: Human

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 36.2 kDa

Formulation: Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5

Reconstitution: Please refer to the printed manual for detailed information.

Background: Cluster of Differentiation 112 (CD112), also known as poliovirus receptor related protein 2 (PVRL2 or PRR2), is a single-pass type I transmembrane glycoprotein belonging to the Immunoglobulin superfamily. CD112 protein also serves as an entry for certain mutant strains of herpes simplex virus and pseudorabies virus, and thus is involved in cell to cell spreading of these viruses. CD112 protein has been identified as the ligand for DNAM-1 (CD226), and the interaction of CD226/CD112 protein can induce NK cell- and CD8+ T cell-mediated cytotoxicity and cytokine secretion. CD112 has been regarded as a critical component in allergic reactions, and accordingly may function as a novel target for anti-allergic therapy.

Research Area: Microbiology, immunology