Technical Data
C0132-14R
Caldesmon, phosphorylated (Thr730) (CDM, Caldesmon 1, Caldesmon-1, CALD1, H CAD, H-CAD, L-CAD)
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 Western Blot and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:500-1:1000
Immunoprecipitation: 1:10
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.

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
TypeIsotypeCloneGrade
MabIgG9H308Supernatant
SizeStorageShippingSourceHost
100ul-20°CBlue IceHumanRabbit
Concentration:
Not determined
Immunogen:
A phospho-specific peptide corresponding to residues surrounding Threonine 730 of human Caldesmon.
Purity:
Supernatant
Form
Supplied as a liquid in 50mM Tris-glycine, pH 7.4, 0.15M sodium chloride, 40% glycerol, 0.01% sodium azide, 0.05% BSA.
Specificity:
Recognizes human Caldesmon when phosphorylated at Thr730.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Humphrey MB, et al. Gene 112:197 2. Bryan J, et al. J Biol Chem 264:13873 3. Bryan J, et al. Ann N Y Acad Sci 599:100 4. Fraser ID, et al. Biochem 36:5483