Anti-Calponin Antibody, clone CALP

Evaluated by Western Blotting in human aortic smooth muscle tissue lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected Calponin in human aortic smooth muscle tissue lysate.

Anti-Calponin, clone CALP , Cat. No. MABT1504, is a mouse monoclonal antibody that detects Calponin-1 and has been tested for use in Immunohistochemistry (Paraffin) and Western Blotting.

Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution from a representative lot detected Calponin in human uterus and human prostate tissue sections.

Research Category
Cell Structure

Clone CALP specifically detects human Calponin-1.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Calponin-1 (UniProt: P51911; also known as Basic calponin, Calponin H1 smooth muscle) is encoded by the CNN1 gene (Gene ID:1264) in human. Calponin is an actin filament-associated regulatory protein that is expressed in smooth muscle and non-muscle cells of vertebrates. Three isoforms of Calponin have been reported that inhibit actin-activated myosin ATPase activity and stabilize the actin cytoskeleton. Calponin 1 is specifically expressed in smooth muscle cells is involved in fine-tuning of smooth muscle contractility. Calponin-2 is found in multiple cell types, including developing smooth muscles and Calponin-3 is found in the neurons, astrocytes and glial cells. Calponin-1 can bind to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 (and other calponins) has a calponin homology (CH) domain at its N-terminal (aa 28-131) that can function either as a part of actin-binding site or serve as a regulatory structure for actin-binding activity. It also has three calponin-like domains (aa 164-189; 204-229; and 243-268) next to the C-terminal region that are conserved in all calponins. The C-terminal segment varies among different calponins and has differentiated effects on weakening the binding of calponin to F-actin. Deletion of the C-terminal tail segment is shown to enhance the actin-binding and bundling activities of calponins. (Ref.: Liu, R., and Jin, J-P (2016). Gene 585(1); 143-153).

~36 kDa observed; 33.17 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Crude human uterine muscle extract.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.