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. Ideal for investigators involved in Cell Biology, Signal Transduction and Stem Cell research.
Anti-Collagen antibodies have been used for indirect trapping ELISA for quantitation of antigen in serum using a standard curve, immunoprecipitation, immunohistochemistry, native (non-denaturing, non-dissociating) PAGE, and western blotting for highly sensitive qualitative analysis.
Type: Primary
Antigen: COL2A1
Clonality: Polyclonal
Clone:
Conjugation:
Epitope:
Host: Rabbit
Isotype:
Reactivity: