Ficin Separopore® 4B-CL

Ficin is a cysteine protease enzyme that is isolated from the latex of fig trees. It has activity similar to other cysteine protease enzymes including endopeptidases, aminopeptidases, and dipeptidyl peptidases. Ficin cleaves mouse immunoglobulin (IgG1) molecules in the hinge region of the protein. This cleavage is dependant of the concentration of cysteine. A F(ab')2 fragment is formed in the presence of 1mM cysteine. The F(ab')2 fragments are smaller than whole IgG molecules and better penetrate cells for antigen recognition. In the presence of 10mM cysteine, 2 Fab fragments are produced instead. F(ab) fragments block background from primary antibody binding.
Ficin Separopore® (Agarose) 4B-CL offers a convenient solution to the production of F(ab')2 and Fab fragments while eliminating autolysis and protease contamination. It also removes the enzymes following digestion. Fab and F(ab')2 can be further separated from whole IgG with Protein A (Agarose) chromatography.
Ficin Separopore is provided as lyophilized product, 1g will swell to approximately 10 mL of reconstituted beads.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.