Technical Data
Calmodulin (CaM) is a 17 kD protein belonging to a structurally homologous family of proteins which includes troponin C, parvalbumin, and S100. Calmodulin is highly conserved among species and all vertebrate CaMs have identical structures (2). Although CaM exists in abundance in many cells, it can be regulated by hormones and neurotransmitters in a variety of tissues and systems. CaM acts as an intracellular calcium sensor that translates the Ca 2+ signal into a variety of cellular processes. Ca 2+ -CaM recognition of a short polypeptide segment in target proteins induces conformational changes in both CaM and the target, enabling the target protein to become functionally active. Phosphorylation of target proteins at sites on or near the CaM-binding region modulates binding of CaM, thereby providing an additional mechanism of functional regulation.

Suitable for use in ELISA, Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
ELISA: 0.1-0.2ug/ml
Immunohistochemistry (paraf n-embedded): 2-5ug/ml
Immunoprecipitation: 2-5ug/IP
Western Blot: 0.5-1ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
MabIgG13G53Affinity Purified
100ug-20CBlue IceBovineMouse
Synthetic peptide corresponding to the C-terminal region of native bovine brain Calmodulin
Purified by affinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.1% sodium azide.
rRecognizes Calmodulin. (1) All vertebrate Calmodulins are known to have the identical amino acid sequence. No crossreactivity is observed with other calcium binding proteins such as troponin, S-100A, S-100B and parvalbumin.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Sacks, D.B., et al; Analytical Biochemistry: 194, 369377 (1991). 2. Cohen, P & Klee, C.B.; Calmodulin, Elsevier, N.Y. (1988). 3. Mathagajasingh, S.N., et al; J. Cell Biol. 145(1):2943 (1999).