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Recombinant Human CNN1 protein (His tag)
SKU: PDEH100414-100
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Recombinant Human CNN1 protein (His tag)
| SKU # | PDEH100414 |
| Expression Host | E. coli |
Description
| Synonyms | Calponin-1;CNN1;Calponin H1;smooth muscle |
| Species | Human |
| Expression_host | E.coli |
| Sequence | Met 1-Ala 297 |
| Accession | P51911 |
| Mol_Mass | 32.6 kDa |
| AP_Mol_Mass | 35 kDa |
| Tag | N-His |
| Bio_Activity | Not validated for activity |
Propertie
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin level | Please contact us for more information. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis |
Background
CNN-1 (Calponin 1 [calcium and calmodulin-binding troponin T-like protein]; also Calponin basic, CaP and Calponin H1) is a 32-36 kDa cytoplasmic member of the calponin family of proteins. Although reportedly expressed in fibroblasts and endothelial cells, it actually appears to be restricted to smooth muscle and smooth muscle-like cells such as myoepithelium and myofibroblasts in the adult. CNN-1 interacts with F-actin in a phosphorylation-dependent manner. When nonphosphorylated, CNN-1 blocks actomyosin ATPase activity, contributing to the stabilization of actin stress fiber bundles. Thus, CNN-1 expression inhibits cell motility and the formation of podosomes. Human CNN-1 is 297 amino acids (aa) in length. It contains one CH/calponin homology domain (aa 30-127), and three consecutive calponin-like repeats (aa 164-268). The repeats are suggested to mediate actin binding. There are five potential Ser/Thr phosphorylation sites. Full-length human CNN-1 shares 97% aa sequence identity with mouse CNN-1.