bs-70628R

DATASHEET

Host: Rabbit

Target Protein: Profilin (Ser-138)

Specificity: This antibody was cross-adsorbed to unphosphorylated Profilin (Ser-138) then Affinity purification using Profilin (Ser-138) 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.

Modification Site: Tyr-138

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P07737

Source: Phospho-Profilin (Ser-138) synthetic peptide (coupled to carrier protein) that includes amino acids surrounding Ser-138 in human Profilin-1.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

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.