The antibody hCP (also cited as CALP), localizes calponin in mammalian smooth muscle. In human uterus, an additional band of approximately 27 kDa (l-calponin) may also be stained. The antibody does not cross-react with skeletal, cardiac or non-muscle tissue calponin. Nevertheless, the antibody exhibits cross-reactivity with an epitope (150 kDa range) in human or mouse skeletal muscle. In immunohistochemical staining, the product exhibits smooth muscle specificity. It stains vascular and visceral smooth muscle cells in tissue sections and primary cultured cells (or early passages), but not most cell lines originally derived from smooth muscle. The antibody does not stain epithelial, endothelial or connective tissue fibroblast cells. This product does not cross react with smooth muscle tissue from chicken.
human uterus smooth muscle extract.
Monoclonal Anti-Calponin antibody produced in mouse is suitable for the following applications:
- Immunohistochemistry using formalin-fixed, paraffin-embedded sections
- Western blotting (at a dilution of 1:10,000 using human uterus extract)
- Flow cytometry analysis
Calponin is a calcium binding protein that belongs to a family of actin-associated proteins. Calponin is necessary for autophosphorylation of protein kinase C (PKC) in vascular smooth muscle (VSM). Calponin-1 inhibition can prevent uterine smooth muscle cell migration, cause morphological change and rearrange F-actin without affecting its proliferation and apoptosis. Calponin h1 (CN) is a differentiation marker of smooth muscle cells and is down-regulated in the blood vessels of several human tumors. It can inhibit actomyosin ATPase activity. The h1 and h2 calponins bind F-actin and play a key role in regulating actin filaments in smooth muscle and non-muscle cells.
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