mDia2 (C-terminal region) 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. The FH1 region contains poly-proline stretches that promote interactions with profilin. The FH2 domain, located C-terminally to the FH1 domain, is highly conserved in formin proteins and possesses actin nucleation and polymerization activities. 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, as well as bind and stabilize microtubules. mDia2 may also have functions in the nucleus, since it is continually shuttled between the cytoplasm and nucleus.

Immunogen: mDia2 synthetic peptide (coupled to KLH) corresponding to amino acid residues in the C-terminal region of mouse mDia2 (Diap3). This peptide sequence is highly conserved in rat and human mDia2, and has low homology to other formins.

Specificity: This antibody was affinity purified using mDia2 (C-terminal region) peptide (without carrier). The antibody detects a 135 kDa* protein corresponding to the apparent molecular mass of mDia2 on SDS-PAGE immunoblots of various cells and tissues, including human A431 and HeLa cells, mouse brain tissue and C2C12 cells, rat PC12 cells, and rabbit spleen fibroblasts.

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.