Calcium ions (Ca²⁺) play extremely important roles, especially, as a second messenger in the cells. In excitable cells, Ca²⁺ permeable ligand-gated channels and voltage-gated Ca²⁺ channels pass Ca²⁺ into the cell. In non-excitable cells, Ca²⁺ Release-Activated Ca²⁺ (CRAC) channel is one of the pathways which Ca²⁺ can enter the cells through. CRAC channel is activated by depletion of Ca²⁺ stores, and has extremely high Ca²⁺ permeability. The B cell receptor (BCR) stimulation activates CRAC channel in rat basophil leukemia (RBL) cells. We examined the inhibition of the CRAC channel by a TRPV1 agonist and its antagonist in RBL cells using patch-clamp technique. The CRAC channel was activated by adding 10-µM IP₃ in the pipette solution instead of BCR stimulation. We applied the voltage-ramp from -120 mV to 80 mV during 50 ms every 3 s at a holding potential of 0 mV. The membrane current showed the inward rectification, and its polarity reversed at >50 mV. These properties are hallmarks of the CRAC channel. Capsaicin and capsazepine inhibited the CRAC channel in a concentration dependent manner with the IC₅₀ of 75 and 27 µM, respectively. These values are higher concentration than those for activation and inhibition of the TRPV1 channel.