mDia2 (Thr-1061), phospho-specific polyclonal, anti-human, mouse, rat, chicken, fish

Background:
Formins include several families of proteins that regulate actin cytoskeletal dynamics via two conserved formin homology domains, FH1 and FH2. Through cooperation of FH1 and FH2, formins construct actin-based structures comprising linear, unbranched filaments that are used in stress fibers, actin cables, microspikes, and contractile rings. A subgroup of the formins is the diaphanous (Dia) family, which includes mDia1 (Diap1), mDia2 (Diap3), and mDia3 (Diap2). The mDia2 protein has been implicated in cell migration and cytokinesis. This Dia protein can nucleate actin polymerization and stabilize microtubules. mDia2 may also function in the nucleus as the protein continually shuttles between the cytoplasm and nucleus. Regulation of mDia2 activity may occur through ROCK phosphorylation of Thr-1061 and Ser-1070. This phosphorylation disrupts inhibitory interactions between the DAD and DID domains leading to enhanced mDia2 activation of RhoA.

Immunogen: Phospho-mDia2 (Thr-1061) synthetic peptide (coupled to KLH) corresponding to amino acid residues surrounding Thr-1061 in mouse mDia2 (Diap3). This peptide sequence is identical in rat and has 2 amino acid differences to human mDia2. The sequence has low homology to other formins.

Specificity: This antibody was affinity purified using mDia2 (Thr-1061) peptide (without carrier). The antibody detects a 135 kDa* protein corresponding to mDia2 in immunoblots of human A7r5 and mouse C2C12 cells treated with calyculin A. The antibody detects transfected mDia2 after treatment with calyculin A, but this reactivity is removed after phosphatase treatment. In addition, the antibody does not detect mDia2 (T1061A) mutant.

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.