This antibody was included in a study aiming to characterize and validate commercially available antibodies raised against myocilin. Epitope mapping was conducted using recombinant myocilin subdomains cloned and expressed in E. coli. As positive control was used endogenously expressed full-length human myocilin secreted by trabecular meshwork (TM) cells.
We evaluated four antibodies (Ab41552, MABN866, MAB3446, sc-137233) in the applications Western blotting (denaturing conditions) and ELISA (native protein).
Our data show that sc-137233 recognizes the OLF domain (aa 244-504) of myocilin. The antibody works very well for WB, and detects both the E. coli expressed OLF as well as the full-length human myocilin.
The epitope was confirmed by ELISA.
For further information see Patterson-Orazem et al., 2018 “Epitope mapping of commercial antibodies that detect myocilin” (www.ncbi.nlm.nih.gov/pubmed/29752947)
On September 4, 2018 Athéna C. Patterson-Orazem, Georgia Institute of Technology wrote:
This antibody was included in a study aiming to characterize and validate commercially available antibodies raised against myocilin. Epitope mapping was conducted using recombinant myocilin subdomains cloned and expressed in E. coli. As positive control was used endogenously expressed full-length human myocilin secreted by trabecular meshwork (TM) cells.
We evaluated four antibodies (Ab41552, MABN866, MAB3446, sc-137233) in the applications Western blotting (denaturing conditions) and ELISA (native protein).
Our data show that sc-137233 recognizes the OLF domain (aa 244-504) of myocilin. The antibody works very well for WB, and detects both the E. coli expressed OLF as well as the full-length human myocilin.
The epitope was confirmed by ELISA.
For further information see Patterson-Orazem et al., 2018 “Epitope mapping of commercial antibodies that detect myocilin” (www.ncbi.nlm.nih.gov/pubmed/29752947)