Cancer Diagnostics Solutions
Desmin is a type of intermediate filament found near the Z line in sarcomeres. Both vimentin and desmin are characteristics of mesenchymal cells.
Desmin antibody detects a protein that is expressed by cells of normal smooth, skeletal and cardiac muscles. Light microscopy studies of desmin suggest that it is primarily located at or near the periphery of Z lines in striated muscle fibrils. In smooth muscle, Desmin interconnects cytoplasmic dense bodies with membranebound dense plaques. Desmin antibody react with Leiomyomas, Rhabdomyomas, and Perivascular cells of Glomus Tumors of the skin (if they are of myogenic nature). This antibody is used to demonstrate the myogenic components/derivation of tumors.
DOG1, or Discovered on GIST-1, is an antibody widely utilized in immunohistochemistry (IHC) for the identification of gastrointestinal stromal tumors (GISTs). GISTs are mesenchymal tumors originating primarily in the stomach and small intestine, and the DOG1 antibody serves as a crucial diagnostic marker for these tumors. DOG1 is a protein encoded by the ANO1 gene, also known as TMEM16A, which functions as a calcium-activated chloride channel. The DOG1 antibody is specifically designed to target the DOG1 protein, exhibiting high sensitivity and specificity for GISTs. Its expression is observed in a vast majority of GISTs, including those that do not express KIT or CD34, other common markers for these tumors.
DOG1, "discovered on GIST 1" encodes for a protein of unknown function that is highly sensitive and specific for gastrointestinal stromal tumors (GIST). GISTs occur in bowel walls and are proposed to originate from the interstitial cells of Cajal. The majority of GISTs harbor activating mutations in KIT but approximately 5-15% of GIST are negative for c-Kit by immunohistochemistry, mainly associated with mutations in the PDGFRA gene.
Dystrophin is an essential cytoskeletal protein that anchors the actin cytoskeleton to the extracellular matrix through the dystrophin-glycoprotein complex (DGC), ensuring sarcolemmal stability and preserving muscle fiber integrity. Mutations or deletions in the dystrophin gene result in Duchenne and Becker muscular dystrophies. The dystrophin gene spans 2.4 Mb, contains over 80 exons, and produces a 14 kb mRNA regulated by multiple tissue-specific promoters and polyadenylation sites. Alternative splicing generates various isoforms with distinct tissue distributions. Although comprising only ~0.002% of total striated muscle protein, dystrophin is enriched at triadic junctions, contributing to calcium homeostasis and mechanical force transmission during muscle contraction.
Dystrophin, the protein encoded by the Duchene and Becker muscular dystrophy (DMD/BMD) gene, exhibits a relative molecular mass of approximately 400 kDa. Immunohistochemical analysis using anti-dystrophin antibodies reveals that individuals affected by DMD exhibit a complete absence or markedly reduced levels of dystrophin in muscle fibers. In contrast, BMD patients express dystrophin of diminished quantity and/or aberrant molecular size. The monoclonal antibody utilized in this analysis specifically targets an epitope located within the central rod domain of dystrophin, encompassing amino acid residues 1181 to 1388. Immunodetection of dystrophin is a valuable diagnostic tool for differentiating DMD and BMD from other neuromuscular disorders