Recombinant Human Nectin-4 Fc Chimera Protein, CF

Recombinant Human Nectin-4 Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

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.

Background: Nectin-4

Nectin-4 (gene name PVRL4, poliovirus receptor-like 4) is a 66 kDa type I transmembrane glycoprotein belonging to the Nectin family of Ig superfamily proteins (1). The Latin word necto means “to connect”, indicating the role of nectins in Ca2+‑independent cell-cell adhesion (2). Nectin-4 forms homodimers in cis, followed by interactions in trans with Nectin-1 or -4 (1-3). Human Nectin-4 mRNA is normally expressed in the placenta, especially in endothelial cells, while in the mouse it is found in the embryo, lung, testis and brain (1, 4, 5). Human Nectin-4 cDNA encodes 510 amino acids (aa), including a 31 aa signal sequence, a 318 aa extracellular domain (ECD), a 21 aa transmembrane segment (TM), and a 140 aa cytoplasmic region. Nectin ECDs contain three Ig-like domains: an N‑terminal V-type that mediates ligand binding, and two C2-type (1, 3). One Nectin‑4 isoform lacks aa 412-436 in the cytoplasmic domain (1). In many human ductal breast or non-small cell lung carcinomas, Nectin‑4 is upregulated and a soluble 43 kDa form is found in the plasma (4-6). This form is generated from the membrane protein via the action of TACE/ADAM-17 (6). The extracellular domain of human Nectin-4 shares 91%, 92%, 93%, 91% and 90% amino acid sequence homology with the corresponding regions of mouse, rat, canine, porcine and bovine Nectin-4, respectively. In forming adherens junctions, trans interactions of Nectin-4 initiate cell-cell interactions and recruit intracellular cadherins through afadin and other junctional proteins (1, 2). These interactions organize the actin cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections (2, 7). In humans, mutation of Nectin-4 has been correlated with ectodermal dysplasia-syndactyly syndrome, indicating a role for Nectin-4 in human development (7).

Related Research Areas

• Cell to Cell Adhesion Disassembly During EMT
• Epithelial Cell Markers and Intracellular Molecules
• Epithelial Cell Polarity
• Infectious Diseases
• Nectin and Nectin-like Binding Receptors and Ligands
• Nectins
• Search Immune Checkpoint Targets
• Surface Ectodermal Cells