Mouse Anti-VWF Recombinant Antibody (clone NMC-4) (CAT#: PABW-132)

Figure 1 Inhibitory effect of purified MoAb NMC-4 on vWF or AS-vWF binding to platelet GP Ib.

(Top [R + vWF]), Ristocetin-induced vWF binding; (middle [B + vWF1). botrocetin-induced vWF binding; (bottom [AS-vWF]), AS-vWF binding.

Fujimura, Y., Usami, Y., Titani, K., Niinomi, K., Nishio, K., Takase, T., ... & Fukui, H. (1991). Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin-and botrocetin-induced vWF binding to platelet glycoprotein Ib. Blood, 77(1), 113-120.

Figure 2 Immunoreactivity of MoAb NMC-4 with tryptic vWF Frs generated at various E/S ratios.

Western blotting analysis was followed by SDS 5% to 20% PAGE under nonreducing (NR) and reducing IR) conditions. Each lane represents 33 Fg of a whole tryptic digest of vWF (E/S ratio indicated below). C, control (undigested vWF).

Fujimura, Y., Usami, Y., Titani, K., Niinomi, K., Nishio, K., Takase, T., ... & Fukui, H. (1991). Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin-and botrocetin-induced vWF binding to platelet glycoprotein Ib. Blood, 77(1), 113-120.

Figure 3 SDS-PAGE and dot blot analysis of the recombinant vWF fragments. A, dot blot analysis.

An aliquot of each fragment was applied onto a nitrocellulose membrane in a circular area. After drying, the membrane was treated with a solution of the anti-vWF monoclonal antibody NMC-4 (5 mg/ml) followed by fluorographic detection of the bound antibody using an alkaline phosphatase-conjugated rabbit antimouse IgG. Note that the antibody reacts well with the cyclic fragments containing the intact Cys509–Cys695 disulfide bond (C) but only minimally after reduction and alkylation of Cys residues (R/A).

Miyata, S., Goto, S., Federici, A. B., Ware, J., & Ruggeri, Z. M. (1996). Conformational changes in the A1 domain of von Willebrand factor modulating the interaction with platelet glycoprotein Ib. Journal of Biological Chemistry, 271(15), 9046-9053.