Profilin (a.a. 132-140) polyclonal, anti-human, mouse, rat

Background:
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.

Immunogen: Profilin synthetic peptide (coupled to carrier protein) that includes amino acids 132 to 140 in human Profilin-1. 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.

Specificity: This antibody was affinity purified using Profilin (a.a. 132-140) peptide (without carrier). The antibody detects a 15 kDa band corresponding to the apparent molecular mass of Profilin-1 in human Jurkat and A431 cells, as well as rat PC12 cells.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.