Overview
- Peptide (C)KYGLHVNPAYEDR, corresponding to amino acid residues 84 - 96 of mouse Nectin-4 (Accession Q8R007).
Extracellular, N-terminus.
Human – 11 out of 13 amino acid residues identical.
- Western blot analysis of mouse brain membranes (lanes 1 and 3) and rat lung lysate (lanes 2 and 4):1-2. Anti-Nectin-4 (extracellular) Antibody (#ANR-054), (1:200).
3-4. Anti-Nectin-4 (extracellular) Antibody, preincubated with Nectin-4 (extracellular) Blocking Peptide (BLP-NR054). - Western blot analysis of human THP-1 monocytic leukemia cell line lysate (lanes 1 and 3) and human MCF-7 breast adenocarcinoma cell line lysate (lanes 2 and 4):1-2. Anti-Nectin-4 (extracellular) Antibody (#ANR-054), (1:200).
3-4. Anti-Nectin-4 (extracellular) Antibody, preincubated with Nectin-4 (extracellular) Blocking Peptide (BLP-NR054).
Nectin Cell Adhesion Molecule 4 (nectin-4), also known as Poliovirus Receptor-Related Protein 4 (PVRL4), is a Ca2 + -independent type 1 transmembrane protein that is a member of the immunoglobulin-like adhesion molecules protein family 1.
All nectins (Nectin-1, Nectin-2, Nectin-3, and Nectin-4) share common structure features: an extracellular region of three Ig-like domains, a transmembrane region, and a cytoplasmic tail region 2.
Nectin-4 interacts with afadin, a protein that has a role in cell-cell adhesion, and with nectin-1, but not with nectin-2 or 3 3.
Nectin-4 was found to be overexpressed in several human cancers, including lung, ovarian, pancreatic, and breast cancer. It was also demonstrated that a soluble form of Nectin-4 is a potential diagnostic marker for several cancers and that knockdown of Nectin-4 inhibits tumor growth and reduces cell-cell contact in certain cancer types 4.
Recently, an antibody-drug conjugate designed for the treatment of cancer expressing Nectin-4 was approved for use in bladder cancer patients.