| Overview |
| bs-70445r |
| mDia1 (N-terminal region) Antibody |
| WB |
| 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. This peptide sequence is highly conserved in rat and mouse mDia1, and has low homology to other formins. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Rabbit |
| mDia1 synthetic peptide corresponding to amino acids from the N-terminal region of human mDia1 (Diap1). |
| Polyclonal |
| #REF! |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| O60610 |
| Dia1, Diaph1, DRF-1, Diap1, p140Dia, formin |
| 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 whole antiserum 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. |
| Application Dilution |
| WB |
1:300-5000 |
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