Collagen Type I Antibody

Rockland produces highly active antibodies and conjugates to collagens. Collagens are highly conserved throughout evolution and are characterized by an uninterrupted ''Glycine-X-Y'' triplet repeat that is a necessary part of the triple helical structure. For these reasons, it is often extremely difficult to generate antibodies with specificities to collagens. The development of ‘type’ specific antibodies is dependent on NON-DENATURED three-dimensional epitopes. Rockland extensively purifies collagens for immunization from human and bovine placenta and cartilage by limited pepsin digestion and selective salt precipitation. This preparation results in a native conformation of the protein. Antibodies are isolated from rabbit antiserum and are extensively cross-adsorbed by immunoaffinity purification to produce 'type' specific antibodies. Greatly diminished reactivity and selectivity of these antibodies will result if denaturing and reducing conditions are used for SDS-PAGE and immunoblotting. Collagen Type I is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white part of the eye (sclera) . Collagen Type I triple helix comprises of two alpha1 chains and one alpha2 chain. COL1A1/A2 could be useful for detecting melanoma, lung, liver, glioma, skin, stomach, and other cancers. Mutations in the gene may be related to caffey disease, osteogenesis, and ehlers-danlos syndrome. Anti-Collagen Type I Antibody is ideal for investigators involved in extracellular matrix protein, osteoporosis research, Cell Biology, Signal Transduction, and Stem Cell research. Anti-Collagen Type I has been tested by dot blot and IHC and are useful for indirect trapping ELISA for quantitation of antigen in serum using a standard curve, immunoprecipitation, native (non-denaturing, non-dissociating) PAGE, immunohistochemistry, Immunofluorescence, FLOW, and western blotting for highly sensitive qualitative analysis.