IgGZERO™
IgGZERO™ is a very efficient endoglucosidase with high specificity for IgG. The enzyme cleaves the chitobiose core of the glycan on IgG from various origin, such as human, rabbit, mouse, monkey, goat and sheep.
IgGZERO™ Features
- IgGZERO™ is the first known bacterial enzyme with a unique specificity for native IgG.
- IgGZERO™ has the ability to hydrolyze human, Rhesus monkey, mouse, rat, rabbit, horse, goat, dog and porcine native and denaturated IgG.
- Removal of IgGZERO™ is extreamly easy by the included histidine tag in the amino terminal of the recombinant enzyme.
- IgGZERO™ efficiently strip bound IgG from FcgRs without producing additional damage to native cells.
IgGZERO™ Function
The Fc portion of IgG contains a conserved carbohydrate attached to the asparagine 297 residue in the CH2 domain of each heavy chain. The presence of this carbohydrate is crucial for proper antibody structure and interactions with cellular IgG Fc gamma receptors (FcgR) and the complement system.
IgGZERO™ has a specific endoglycosidase activity on native IgG by hydrolyzing the conserved glycans attached to the asp 297 residue on the IgG heavy chains. The activities of other known endoglycosidases require or are enhanced by denaturation of the glycoprotein substrate.
Removal of IgG from Primary Cells Using IgGZERO™
The effects mediated by FcgRs are of great interest in the study of immunology. In vivo evaluation of such effects is complicated because cells isolated from subjects or individuals are typically pre-loaded with IgG bound to their FcgRs. Accordingly the receptors are blocked, preventing furhter analysis. To remove the IgG from the receptors IgGZERO™ can be used. The high efficiency of IgGZERO™ quickly removes the IgG molecules from the FcgRs on primary cells. The enzyme is easy to use and allows further modification and conjugation of the IgG molecule after removal of the oligosaccharides.
