Monoclonal Anti- Caldesmon
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Catalog# BMA1049
Lot # Check on the product label
Size 100 μg
Isotype IgG
Host Rabbit
Reactivity
Human, mouse, rat
Product Form Liquid
Purification Protein A affinity purified
Immunogen
A synthetic peptide within C-terminal human Caldesmon.
Recommend Application
Western Blot, WB (1:500-1:1,000)
Immunohistochemistry, IHC-P (1:20-1:100)
Immunocytochemistry, ICC/IF (1:20-1:100)
Flow Cytometry, Flow-Cyt (1:20-1:50)
Other applications have not been tested.
The optimal dilutions should be determined by end user.
Storage Buffer
1*PBS (pH7.4), 0.2% BSA, 40% Glycerol and 0.05% Sodium Azide.
Storage Instruction
Store at 4°C after thawing (1 week). Aliquot and store at -20°C for long term (at least one year).
Avoid repeated freeze and thaw cycles.
Background
Caldesmon is a protein that in humans is encoded by the CALD1 gene. Caldesmon (CDM) is a potential actomyosin regulatory protein found in smooth muscle and nonmuscle cells. Domain mapping and physical studies suggest that CDM is an elongated molecule with an N-terminal myosin/calmodulin-binding domain and a C-terminal tropomyosin/actin/calmodulin-binding domain separated by a 40-nm-long central helix.1 The high molecular weight caldesmon (h-CaD) is predominantly expressed in smooth muscles, whereas the low molecular weight caldesmon (l-CaD) is widely distributed in nonmuscle tissues and cells.2 The conserved domain of this protein possesses the binding activities to Ca++-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca++-dependent inhibition of smooth muscle contraction.
Reference
1. Humphrey, M. B., Herrera-Sosa, H., Gonzalez, G., Lee, R., Bryan, J. Cloning of cDNAs encoding human caldesmons. Gene 112: 197-204, 1992.
2. Hayashi, K., Yano, H., Hashida, T., Takeuchi, R., Takeda, O., Asada, K., Takahashi, E., Kato, I., Sobue, K. Genomic structure of the human caldesmon gene. Proc. Nat. Acad. Sci. 89: 12122-12126, 1992.
Details
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