Figure 1.
Figure 1. Kinase domain-independent and SLP-65-independent function of Btk. (A) K430R-Btk stimulates calcium flux in response to BCR activation. Indo-1 AM-loaded splenic B cells of the indicated mice were stimulated with anti-IgM F(ab′)2 fragments and calcium flux was monitored. The plots are representative for 2 to 4 mice of each genotype. (B) Btk phosphorylation in the absence of SLP-65. Cultured cells from 2 different SLP-65- pre-B-cell lymphomas (BL no. 1 and BL no. 2) were either not stimulated or stimulated for 1 or 5 minutes with polyclonal anti-IgM F(ab′)2 fragments. The presence of Btk in antiphosphotyrosine immunoprecipitates from total cellular lysates was analyzed by Western blotting using Btk-specific antibodies.

Kinase domain-independent and SLP-65-independent function of Btk. (A) K430R-Btk stimulates calcium flux in response to BCR activation. Indo-1 AM-loaded splenic B cells of the indicated mice were stimulated with anti-IgM F(ab′)2 fragments and calcium flux was monitored. The plots are representative for 2 to 4 mice of each genotype. (B) Btk phosphorylation in the absence of SLP-65. Cultured cells from 2 different SLP-65- pre-B-cell lymphomas (BL no. 1 and BL no. 2) were either not stimulated or stimulated for 1 or 5 minutes with polyclonal anti-IgM F(ab′)2 fragments. The presence of Btk in antiphosphotyrosine immunoprecipitates from total cellular lysates was analyzed by Western blotting using Btk-specific antibodies.

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