Recombinant Human Nectin-2/CD112 His-tag Avi-tag Protein, CF Summary
Accession # NP_002847.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human DNAM-1 Fc Chimera (666-DN) is immobilized at 2.00 µg/mL (100 µL/well), Biotinylated Recombinant Human Nectin-2/CD112 His-tag Avi-tag Protein (Catalog # AVI2229) binds with an ED50 of 0.600‑3.60 µg/mL.
2 μg/lane of Biotinylated Recombinant Human Nectin‑2/CD112 His-tag Avi-tag Protein (Catalog # AVI2229) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 43-55 kDa.
Nectin-2, also known as Poliovirus receptor-related 2 (PRR2), is a member of the Nectin family which are Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions (1). The Nectin family is comprised of 4 family members and 5 nectin‑like molecules and they are structurally homologous to the poliovirus receptors (2). Mature human Nectin‑2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a single transmembrane segment, and a cytoplasmic domain bind the F-actin–binding protein afadin (3). Within the ECD, human Nectin‑2 shares 72% amino acid (aa) sequence identity with mouse Nectin‑2. Alter native splicing generates an isoform with a truncated cytoplasmic tail (1). Nectin-2 localizes to adherens junctions between neurons, endothelial cells, epithelial cells, and fibroblasts (3, 4). It forms homodimers in cis, followed by dimers in trans (between cells) (4). It does not cis‑dimerize with other Nectins but forms cis‑dimers between its two splice forms. Notably, a Nectin-2 cis‑dimer on one cell can heterodimerize with a Nectin‑3 cis‑dimer on a neighboring cell (4). Nectin‑2 additionally binds to DNAM-1/CD226 on NK cells and triggers NK cell cytolytic activity (5, 6). Nectin‑2 is known to bind pseudorabies virus and herpes simplex virus-2 (HSV-2), but not HSV-1 or poliovirus (4, 7). Nectin‑2 is a component of cardiac intercalated discs and limits fibrosis and dysfunction resulting from pressure overload (8). Our Avi-tag Biotinylated Nectin‑2 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Eberle, F. et al. (1995) Gene 159:267.
- Samanta, D. and S.C. Almo (2015) Cell. Mol. Life Sci. 72:645.
- Samanta, D. et al. (2012) PNAS 109:14836.
- Struyf, F. et al. (2002) J. Virol. 76:12940.
- Bottino, C. et al. (2003) J. Exp. Med. 198:557.
- Pende, D. et al. (2005) Mol. Immunol. 42:463.
- Warner, M.S. et al. (1998) Virology 246:179.
- Satomi-Kobayashi, S. et al. (2009) Hypertension 54:825.
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