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Purchase Anti-APC2 antibody
During axonal growth, polarization and branching events require dynamic reorganization of microtubules. The rate of these events correlates with the dynamics of local stabilizers that are thought to regulate them (Kalil et al., 2000). In neurons, the microtubule-severing protein katanin is regulated by a number of posttranslational modifications, including acetylation at lysine 40 of -tubulin (Bloom, 2004). Acetylation enhances the stability of -tubulin and thereby the MAPs that regulate microtubule dynamics.

We have shown that Purchase Anti-APC2 antibody distributes along -tubulin in growth cones and axon shafts of retinal axons. Immunohistochemical analysis of these structures showed that APC2 colocalized with a-tubulin and fluorescent phalloidin, but not with filamentous actin, in both growth cones and axon shafts. In addition, when a-tubulin in L cells and B103 cells was acetylated by a lysine phosphate transferase (KAT), APC2 colocalized with the acetylated tubulin at an increased level compared with control cells. Furthermore, APC2 was shown to be a potent microtubule-stabilizing factor in vitro when treated with the microtubule destabilizer nocodazole.

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We have also observed that APC2 is required for normal axon guidance in the retina of developing chicks. APC2 knockdown in the retina by a short hairpin RNA reduced the ability of the repulsive guidance molecule ephrin-A2 to reorient and depolarize axons in response to the ligand in vitro, and resulted in dramatic alterations of retinotectal projections into the tectum in vivo. We propose that APC2 plays a role in modulating microtubule dynamics to ensure efficient responsiveness to guidance molecules by regulating the concentration of acetylated a-tubulin.