Technical Data
C0132-15C
Caldesmon, phosphorylated, Ser789
Description:
Caldesmon is a smooth muscle and nonmuscle regulatory protein that interacts with actin, myosin, tropomyosin, and calmodulin (1,2). Smooth muscle caldesmon is an elongated molecule with a calmodulin, tropomyosin, and actin-binding region at the C-terminus and a myosin-binding domain at the N-terminus (3). Caldesmon stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, caldesmon inhibits the actomyosin ATPase by binding to F-actin. This inhibition is reduced by calcium-calmodulin and is promoted by tropomyosin (4).

Applications:
Suitable for use in Flow Cytometry, Western Blot, Immunoprecipitation, Immunohistochemistry and Immunocytochemistry. Other applications not tested.

Recommended Dilutions:
Flow Cytometry: 1:20
Western Blot: 1:10,000-1:20,000
Immunohistochemistry: 1:250
Immunocytochemistry: 1:250
Immunoprecipitation: 1:80
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
MabIgG6k64Supernatant
SizeStorageShippingSourceHost
100ul4°C (-20°C Glycerol)Blue IceHumanRabbit
Concentration:
Not Determined
Immunogen:
A synthetic phospho-peptide corresponding to residues surrounding Ser789 of human Caldesmon.
Purity:
Supernatant
Form
Supplied as a liquid in 50mM Tris-Glycine, pH 7.4, 0.15M sodium chloride, 0.01% sodium azide, 0.05% BSA , 40% glycerol.
Specificity:
Recognizes human Caldesmon. This antibody is not phospho-specific, and will recognize total endogenous protein. Species Crossreactivity: mouse and rat
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Humphrey, M.B., et al. Gene 112: 197–204 (1992).2. Bryan, J., et al. . J Biol Chem. 264: 13873–9 (1989). 3. Bryan, J. Ann N Y Acad Sci. 599: 100–10 (1990). 4. Fraser, I.D., et al. Biochemistry 36: 5483–92 (1997).