recombinant gelonin

Recombinant gelonin (rGel) is a 30 kDa recombinant version of the Type I ribosome-inactivating protein (RIP) originally isolated from the seeds of *Gelonium multiflorum*. As a Type I RIP, it consists of a single polypeptide chain that possesses potent N-glycosidase activity but lacks the cell-binding B-chain found in Type II RIPs like ricin. This structural characteristic renders rGel relatively non-toxic to cells unless it is specifically internalized via a targeting moiety, such as a monoclonal antibody, single-chain Fv fragment, or growth factor. Once inside the cytosol, rGel specifically cleaves a single adenine residue (A4324) from the sarcin/ricin loop of the 28S ribosomal RNA. This action irreversibly inhibits protein synthesis by preventing the binding of elongation factors, ultimately leading to cell death via apoptosis. It is primarily developed as a cytotoxic payload for targeted cancer therapies, including immunotoxins and fusion proteins.

Other names

rGeloninrecombinant gelonin toxin