Saporin is obtained from the seeds of the Soapwort plant (Saponaria officinalis), a plant that grows wildly in Britain and other parts of Europe. Saporin is a plant enzyme with N-glycosidase activity that depurinates a specific nucleotide in the ribosomal RNA 28S, thus irreversibly blocking protein synthesis. It belongs to the well-characterized family of ribosome-inactivating proteins (RIPs). There are two types of RIPs: type I, which are much less cytotoxic due to the lack of the B chain and type II, which are distinguished from type I RIPs by the presence of the B chain and their ability to enter cells on their own. However, type I RIPs can still be internalized by fluid-phase endocytosis. Upon internalization, the ribosomes are inactivated, resulting in cell death.
This antibody recognizes saporin. The antibody was first protein-A-purified followed by affinity-purification against saporin attached to a CnBr-Sepharose support column. This antibody is routinely tested by Western Blot.
Applications include immunoblotting.
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