Isolectin B4 (IB4) is one of a family of five alpha-D-galactose-binding lectins from Griffonia (Bandeiraea) simplicifolia. Recombinant IB4* was expressed in E. coli and purified using affinity chromatography. In one important application rIB4-SAP specifically eliminates the IB4-positive c-fiber nociceptor neurons, while sparing the peptidergic neurons. Upon binding the alpha-D-galactopyranoside residues expressed on the cell surface, rIB4-SAP becomes internalized and saporin inhibits protein synthesis, resulting in elimination of the neurons.
The cytotoxin is extremely potent, with an EC50 in the low picomolar range for some alpha-D-galactopyranoside-expressing cells in vitro. rIB4-SAP is an excellent tool for the study of pain transmission and the biological roles of IB4+ cells in vivo.
rIB4-SAP eliminates a-D-galactosyl-positive cells. All other cells are left untouched.
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