Recombinant Mouse Cadherin-4/R-Cadherin Protein, CF

Cadherin‑4, also known as R‑Cadherin, is a 120‑140 kDa type I transmembrane protein belonging to the Cadherin superfamily of calcium‑dependent adhesion molecules. Cadherins are involved in multiple processes including embryonic development, cell migration, and maintenance of epithelial integrity (1, 2). Mouse Cadherin‑4 is synthesized with a 20 amino acid (aa) signal peptide and a 146 aa N‑terminal propeptide. The mature cell surface‑expressed protein consists of a 565 amino acid (aa) extracellular domain (ECD) that contains five Cadherin repeats, a 22 aa transmembrane segment, and a 160 aa cytoplasmic domain (3, 4). Within the propeptide and ECD, mouse Cadherin‑4 shares 92% and 98% aa sequence identity with human and rat Cadherin‑4, respectively. Cadherin‑4 is expressed in epithelial cells, vascular smooth muscle cells, glial and neuronal cells, pancreatic beta ‑cells, thyroid follicular cells, and bone marrow Lin^‑ hematopoietic stem cells (4 ‑ 10). It interacts in cis to form homodimers as well as heterodimers with N‑Cadherin which function as adhesion multimers in trans-configuration (3, 11, 12). It is down‑regulated in invasive breast cancer but up‑regulated in rhabdomyosarcoma and has been shown to exert both positive and negative effects on cell migration and tumor cell invasiveness (5, 13, 14). Cadherin‑4 is involved in a variety of homing processes including guidance of the optic nerve and pioneer axons in early brain development, branching and guidance of the retinal vasculature, and targeting of hematopoietic stem cells to sites of ischemia (7, 10, 15, 16). Cadherin‑4 additionally binds to KLRG1, an inhibitory receptor expressed on NK cells (17).