mDia3 (C-terminus) polyclonal, anti-human, mouse, rat

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). mDia3 is activated by Cdc42 and regulates the attachment of microtubules to the kinetochore during mitosis. Aurora B kinase phosphorylates Ser-196 and Thr-882 in vitro, and phosphorylation of Ser-196 increases during mitosis in vivo. A multisite mutant mDia3 with nonphosphorylatable T66A, S196A, S880A and T882A leads to misalignment of chromosomes at the metaphase plate. Thus, phosphorylation may be an important regulator of mDia3 activity during mitosis.

Immunogen: mDia3 synthetic peptide (coupled to KLH) corresponding to amino acid residues near the C-terminus of human mDia3 (Diap2). This peptide sequence is highly conserved in rat and mouse mDia3, and has low homology to other formins.

Specificity: This antibody was affinity purified using mDia3 (C-terminus) peptide (without carrier). The antibody detects a 130 kDa* protein corresponding to the apparent molecular mass of mDia3 on SDS-PAGE immunoblots of human Jurkat and mouse C2C12 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.