Profilin (C-terminal region) Antibody

Profilins are small actin-binding proteins that have functions in cell motility, cytokinesis, gene transcription, endocytosis and neuronal plasticity. Four profilin isoforms have been identified in mammals. Profilin-1 (PFN1) and profilin-2a (PFN2a) isoforms are highly conserved in structure, but PFN1 is ubiquitously expressed while PFN2a is preferentially enriched in brain. In addition, there are two testis-specific profilins, PFN3 and PFN4, that significantly differ in primary sequence and function compared to PFN1 and PFN2a. Profilin is phosphorylated at both tyrosine and serine residues in vivo. Tyr-129 is phosphorylated in response to VEGF-A stimulation, and this promotes profilin actin binding and polymerization. Tyr-129 phosphorylation may be important for angiogenesis induced by injuries. Ser-138 is phosphorylated by ROCK and dephosphorylated by PP1. This serine phosphorylation inhibits G-actin binding, as well as decreases profilin's aggregation suppressor activity by inhibiting binding to huntingtin. Thus, Tyr-129 phosphorylation may activate while Ser-138 phosphorylation may inhibit profilin activity.

The antibody detects a 15 kDa band corresponding to the apparent molecular mass of Profilin-1 in human umbilical vein endothelial cells (HUVEC) and Jurkat cells. This sequence is well conserved in rat and mouse Profilin-1, has some homology to Profilin-2a and Profilin-2b, and low homology to Profiin-3 and Profilin-4.