Name :
Recombinant Human Nectin-2 Protein (ECD, hFc & AVI Tag), Biotinylated, HPLC-verified
Biological Activity :
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.
Biological Activity :
Measured by its binding ability in a functional ELISA. Immobilized Human PVRIG hFc(Cat:28312-H02H2) at 2 μg/mL (100 μL/well) can bind Human Nectin-2 (ECD, hFc & AVI Tag), Biotinylated(Cat:10005-H41H-B), the EC50 of Human Nectin-2 (ECD, hFc & AVI Tag), Biotinylated(Cat:10005-H41H-B) is 10-60 ng/mL.
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
NP_002847.1
NCBI Gene ID :
Synonyms :
Synonyms :
poliovirus receptor-related 2 (herpesvirus entry mediator B)
Amino Acid Sequence :
Molecular Weight :
The recombinant human NECTIN2 consists of 582 amino acids and predicts a molecular mass of 64.08 kDa. It migrates as an approximately 75.99 kDa band in SDS-PAGE under reducing conditions.
Purity :
≥ 95 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.
Protein Construction :
A DNA sequence encoding the human NECTIN2 (NP_002847.1)(Met1-Leu360) was expressed with a c-terminal AVI tagged Fc region of human IgG1 at the C-terminus (Fc-AVI). The expressed protein was biotinylated in vivo by the Biotin-Protein ligase (BirA enzyme) which is co-expressed.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
CD112 Protein, Human; HVEB Protein, Human; Nectin-2 Protein, Human; PRR2 Protein, Human; PVRR2 Protein, Human Nectin-2 背景信息 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.
References & Citations :
Bachelet I, et al. (2006) Mast cell costimulation by CD226/CD112 (DNAM-1/Nectin-2): a novel interface in the allergic process. J Biol Chem. 281(37): 27190-6.Wang L, et al. (2009) Molecular cloning, characterization and three-dimensional modeling of porcine nectin-2/CD112. Vet Immunol Immunopathol. 132(2-4): 257-63.
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