mDia1 (a.a. 66-77) 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). The mDia1 protein is activated by Rho and leads to ROCK-dependent stress fiber formation. Rho-activated mDia1 regulates serum response factor-dependent transcription. In cancers, mDia1 has been implicated in ras-mediated transformation, metastasis, and invasion. Thus, mDia1 is a Rho-activated formin with both cytoskeletal- and transcription-reguatling activities.

Immunogen: mDia1 synthetic peptide corresponding to amino acids 66-77 in the N-terminal region of human mDia1 (Diap1). This peptide sequence is highly conserved in rat and mouse mDia1, and has low homology to other formins.

Specificity: This antibody was affinity purified using mDia1 (a.a. 66-77) peptide (without carrier). The antibody detects a 140 kDa* protein corresponding to the apparent molecular mass of mDia1 on SDS-PAGE immunoblots of human K562, 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.