- CITATIONS: 1
|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||16838 Da|
|Other Names||Calmodulin, CaM, CALM1, CALM, CAM, CAM1|
|Target/Specificity||A synthetic peptide corresponding to residues in the C-terminus of human Calmodulin was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Calmodulin Antibody (CaM) (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||CALM, CAM, CAM1|
|Function||Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.|
|Cellular Location||Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules|
Provided below are standard protocols that you may find useful for product applications.
Calmoduin (CaM) is a calcium modulator protein and a transducer of calcium signals (1-2). Upon calcium binding, calmodulin undergoes conformational changes and binds and modulates a diverse array of proteins. Calcium-bound CaM (Ca2+-CaM) can assume a variety of shapes depending on the target (3). Ca2+-CaM binds many kinases, phosphatases, signaling proteins, and structural proteins affecting a wide variety of processes including neurotransmitter release, muscle contraction, metabolism, apoptosis, inflammation, membrane protein organization, and cytoskeleton movement (2, 4-5).
1. Sasagawa T, Ericsson LH, Walsh KA, Schreiber WE, Fischer EH, Titani K. Biochemistry. 1982 May 11;21(10):2565-9.
2. Eldik L.V. and Watterson,D.M. (1998) Academic Press, San Diego, CA
3. Finn B.E., Evenas,J., Drakenberg,T., Waltho,J.P., Thulin,E. and Forsen,S. (1995) Nat. Struct. Biol., 2, 777
4. DeMaria C.D., Soong,T.W., Alseikhan,B.A., Alvania,R.S. and Yue,D.T. (2001) Nature, 411, 484
5. Deisseroth K., Heist,E.K. and Tsien,R.W. (1998) Nature, 392, 198
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