208697
Calmodulin, Biotinylated, Bovine Brain
Synonym(s):
Biotin-CaM
form
liquid
General description
A ubiquitous Ca2+-binding protein that serves as a physiological effector of a wide range of biological processes. Useful for the study of calmodulin-binding proteins immobilized on nitrocellulose, by Western blot or dot blot. Calmodulin purified from bovine brain and biotinylated.
Calmodulin, Biotinylated, Bovine Brain, is a ubiquitous Ca2+-binding protein. Useful for the study of calmodulin-binding proteins.
Useful for the detection of calmodulin-binding proteins immobilized on nitrocellulose in Western blot or dot blot protocols. Biotin-CaM is detectable with streptavidin-alkaline phosphatase conjugate (Cat. No. 189732). Calmodulin purified from bovine brain and biotinylated.
Physical form
In PBS, 1 mg/ml BSA, 0.02% NaN₃.
Preparation Note
Following initial thaw, store in the refrigerator (4°C).
Other Notes
This product is not to be used for animal treatment, in vivo research or in any other contact procedure with livestock.
Storage Class Code
10-13 - German Storage Class 10 to 13
Regulatory Information
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E O Hernández et al.
Tissue & cell, 26(6), 849-865 (1994-12-01)
Calmodulin has been suggested as the Ca(2+)-mediator in diverse cellular functions via its interaction with a number of proteins in a calcium-dependent manner. Its participation in the acrosome reaction has been suggested based on its localization in the acrosome region
M J Hubbard et al.
The Journal of biological chemistry, 262(31), 15062-15070 (1987-11-05)
The interaction of calmodulin with calcineurin, a calcium- and calmodulin-stimulated protein phosphatase, was investigated using a solid-phase assay. Binding of 125I-calmodulin by calcineurin immobilized on nitrocellulose membrane filters was of high affinity, reversible, and calcium-dependent. Complex binding kinetics reflected a
Preparation of fluorescent, cross-linking, and biotinylated calmodulin derivatives and their use in studies of calmodulin-activated phosphodiesterase and protein phosphatase.
R L Kincaid et al.
Methods in enzymology, 159, 605-626 (1988-01-01)
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