Human Cadherin‑11 Antibody

The cadherin superfamily comprises a large number of membrane glycoproteins with one or more cadherin repeats, which are involved in Ca²⁺ dependent cell-cell adhesion. The family can be subdivided into several major subgroups, including the type I and type II classical cadherins, desmosomal cadherins, protocadherins, seven transmembrane (Flamingo) cadherins, FAT-family cadherins, T-cadherin and other unclassified cadherins (1). Cadherin-11, also known as OB-cadherin, is a type II classical cadherin. Classical cadherins are type I transmembrane proteins with an N-terminal extracellular domain containing five tandem cadherin repeats and a C-terminal cytoplasmic domain with a characteristic sequence for binding to catenins. Type I cadherins (E-, N-, P-, R-, M-, and EP-cadherin) differ from type II cadherins (cadherin-5 to -12, -18 to -20 and -22) by the presence of the HAV tripeptide motif in the most N-terminal cadherin repeat (2). Classic cadherins mediate cell-cell adhesion preferentially via homotypic interactions and form adherens juctions that have beta -catenin and p120 (ctn) at the cytoplasmic side of the junction (3, 4). Homotypic cadherin interactions also transduce outside-in and inside-out cell signals. Cadherin signaling induces various cellular processes including cell motility, actin cytoskeleton reorganization, proliferation, and differentiation (3, 4). Cadherin-11 is expressed in a variety or normal tissues of mesodermal origin including areas of the kidney and brain, in normal osteoblasts, and in tumors of the stomach, kidney, colon, breast, and bone (osteosarcoma) (5, 6). It is also differentially expressed in the embryonic brain and may be important in regulating neural development. Human Cadherin-11 exhibits a unique mRNA splice site allowing for two forms of the protein to be expressed, a full-length 796 amino acid (aa) protein and a COOH terminus-truncated variant of 693 aa. The truncated variant has a unique cytoplasmic region due to a frameshift event (3). The full-length human and mouse Cadherin-11 share 97% homology at the aa sequence level.