Detection of CDO in C2C12 Mouse Cell Line by Flow Cytometry.|
C2C12 mouse myoblast cell line was stained with Sheep Anti-Human CDO Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4384, filled histogram) or control antibody (Catalog # 5‑001‑A, open histogram), followed by NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # NL010).
|CDO in C2C12 Mouse Cell Line. CDO was detected in immersion fixed C2C12 mouse myoblast cell line using Sheep Anti-Human CDO Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4384) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). Specific staining was localized to cell membranes. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
CDO (CAM-related/down‑regulated by oncogenes, also CDON; pronounced “kid-oh”) is a 190 kDa member of the Immunoglubulin (Ig) superfamily, Ig/Fibronectin (FN) type III repeat family of cell surface proteins (1). Human CDO is a type I transmembrane (TM) glycoprotein. It is synthesized as a 1287 amino acid (aa) precursor that contains a 25 aa signal sequence, a 938 aa extracellular domain (ECD), a 21 aa TM segment and a 303 aa cytoplasmic region (1, 2). The ECD contains five C2‑type Ig-like domains, followed by three FN type III repeats. The first FN repeat (aa 577‑673) is known to bind numerous cadherins, while the third (or juxtramembrane) FN type III repeat (aa 826‑923) binds SHH (3, 4). The intracellular region is believed to signal through various bHLH transcription factors (2). One alternate splice form is reported that shows a deletion of aa 1212‑1234 in the cytoplasmic tail. The ECD of human CDO is 85% aa identical to mouse CDO ECD. CDO is found on muscle precursor and neural progenitor cells of the embryo (5, 6). It likely promotes muscle differentiation, and contributes to axon guidance and neuronal patterning (2, 7, 8, 9). These effects may be mediated through two different receptor complexes. On muscle precursors, CDO apparently acts as both a coordinating and signaling subunit. Here, it integrates N- and M-cadherin, neogenin, netrin-3 and BOC into a cis-oriented receptor complex (2). While this complex has no identified ligand, intercellular cadherin interactions or netrin, may be enough to trigger CDO/cadherin/neogenin signaling. On axons, CDO may participate in a poorly‑defined receptor complex minimally composed of CDO, BOC and Gas1 that binds SHH, and interacts with PTCH1 (7, 8, 10).
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