Mouse Anti-BCHE Recombinant Antibody (clone B2 18-5) (CAT#: FAMAB-0030CQ)

Figure 2 BChE immunopurified from 1.5 mL plasma by binding to immobilized monoclonal mAb2 or B2 18-5.

BChE was dissociated from the washed beads with 1% trifluoroacetic acid. The Coomassie stained SDS PAGE gel shows a monomer band for pure BChE at 85 kDa and a dimer band at 170 kDa in lanes 5 and 10. The BChE protein captured by mAb2 in lanes 1–4, and by B2 18-5 in lanes 5–9 has an intense band at 85 kDa for the BChE monomer and a band at 170 kDa for the BChE dimer. The immunopurified BChE has contaminating bands at 55 and 25 kDa. Differences in band intensities are explained by handling losses of 20 μL beads.

Onder, S., Tacal, O., & Lockridge, O. (2018). Delipidation of plasma has minimal effects on human butyrylcholinesterase. Frontiers in pharmacology, 9, 117.

Figure 3 Comparison of BChE purity following one-step purification on Hupresin or on immobilized monoclonal beads.

The precast 4–20% gradient SDS gel was stained with Coomassie blue. Lanes 1 and 5, BChE eluted from Hupresin with 0.1 M TMA pH 7.5. Lane 2, BChE eluted from monoclonal mAb2 with 1% TFA. Lanes 3 and 7, pure human BChE. Lane 6, BChE eluted from monoclonal B2 18-5 with 1% TFA. Lane 4, molecular weight markers.

Onder, S., David, E., Tacal, O., Schopfer, L. M., & Lockridge, O. (2017). Hupresin retains binding capacity for butyrylcholinesterase and acetylcholinesterase after sanitation with sodium hydroxide. Frontiers in pharmacology, 8, 713.