Rendomab B4

Rendomab B4 (0.15-100 nM; overnight-1 h) binds specifically and with high affinity (apparent K_d*=0.15 nM) to human endothelin B receptor expressed on CHO-ET_B cells, and does not cross-react with rodent endothelin B receptor or human endothelin A receptor^[1].
Rendomab B4 (10 nM; overnight) does not compete with endothelin-1 or endothelin-3 for binding to human endothelin B receptor on CHO-ETB cells, indicating distinct binding sites^[1].
Rendomab B4 (1 μg/mL; 90 min) recognizes a discontinuous conformational epitope formed by two non-contiguous sequences in the N-terminal domain of human endothelin B receptor, spanning residues 28-38 and 70-77^[1].
Rendomab B4 (0.14-10 nM; overnight) binds specifically to human endothelin B receptor expressed on multiple melanoma cell lines, with the highest affinity for UACC-257 cells (apparent K_d=0.14 nM), and does not bind to endothelin B receptor on non-cancerous HEK293T or HUVEC cells^[1].
Rendomab B4 (150 nM; 2 h 30 min) potently inhibits endothelin-1 and endothelin-3-induced phospholipase C activation in UACC-257 melanoma cells, reducing activity by approximately 75%^[1].
Rendomab B4 (150 nM; 2 h 5 min) does not inhibit endothelin-1 or endothelin-3-induced ERK1/2 phosphorylation in UACC-257 melanoma cells, demonstrating a biased inhibitory effect on endothelin B receptor signaling pathways^[1].
Rendomab B4 (150 nM; 22 h) completely inhibits endothelin-1-induced migration of UACC-257 melanoma cells, without affecting baseline cell migration^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.