Mouse Anti-INSR Recombinant Antibody (clone 83-14) (CAT#: PABZ-083)

Figure 1 Insulin- and antibody-stimulated glucose uptake.

Antibody-stimulated glucose uptake. Insulin (30 nM), the indicated monoclonal antibodies (30 nM), or a polyclonal antibody (B-10, diluted 1:150) was added to the transfected CHO cells and incubated 30 min at 370C; deoxyglucose uptake was then measured. Results are expressed as percent stimulation over control cells that did not receive insulin.

Ebina, Y., Araki, E., Taira, M., Shimada, F., Mori, M., Craik, C. S., ... & Rutter, W. J. (1987). Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin-and antibody-stimulated glucose uptake and receptor kinase activity. Proceedings of the National Academy of Sciences, 84(3), 704-708.

Figure 2 Species specificity of antibodies reacting in the ¹²⁵I-insulin-receptor co-precipitation assay.

Co-precipitation assays were carried out by preincubating wheatgerm agglutinin-Sepharose-purified receptors from human (p), bovine (r) or rabbit (¡) liver with '251-insulin (20000 c.p.m.) before addition of various concentrations of antibodies 83-7 (a), 18-40 (b), 18-24 (c), 18-44 (d), 18-14 (e) or 18-28 (f). Results are expressed as a percentage of receptor-bound radioactivity (human, 1500 c.p.m.; bovine, 1800 c.p.m.; rabbit, 2500 c.p.m.) determined by precipitation with poly(ethylene glycol) at the time of addition of antibody.

Soos, M. A., Siddle, K., Baron, M. D., Heward, J. M., Luzio, J. P., Bellatin, J., & Lennox, E. S. (1986). Monoclonal antibodies reacting with multiple epitopes on the human insulin receptor. Biochemical Journal, 235(1), 199-208.

Figure 3 Effects of anti-insulin receptor antibodies on BRET signal.

Top, graph, partially purified fusion receptors were incubated for 45 min in the presence of insulin (100 nM), 83-14 antibody (1 ng/l), or both. BRET signal was measured as described under Materials and Methods. Results are the mean S.E.M. of seven to nine experiments. *p<0.05 compared with insulin alone (Student's t test). Blot, autophosphorylation of partially purified fusion receptors was performed as described under Materials and Methods in presence of insulin (100 nM), 83-14 antibody (1 ng/l), or both.

Boute, N., Pernet, K., & Issad, T. (2001). Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer. Molecular pharmacology, 60(4), 640-645.

Figure 4 The binding to the human brain capillaries of [ ¹²⁵I] TAYD chimeric HIRMAb

The binding to the human brain capillaries of [ ¹²⁵I] TAYD chimeric HIRMAb is plotted versus the time of incubation and is expressed as % bound per mg of capillary protein. Each tube contained approximately 0.05 mgp, indicating about 20% of the total antibody was bound per tube. The binding increased with time in the presence of buffer, but was nearly completely suppressed by the addition of 10 μg/mL murine 83-14 HIRMAb.

Coloma, M. J., Lee, H. J., Kurihara, A., Landaw, E. M., Boado, R. J., Morrison, S. L., & Pardridge, W. M. (2000). Transport across the primate blood-brain barrier of a genetically engineered chimeric monoclonal antibody to the human insulin receptor. Pharmaceutical research, 17(3), 266-274.