Calmodulin, human recombinant

≥95% Pure active Human recombinant Calmodulin which can bind to and regulate a multitude of protein targets.
Catalog #: 7838 | abID:

Product Details

Cat # +Size 7838-500
Size 500 μg
Alternate Name CaM, CALM Phosphodiesterase 3':5'-cyclic nucleotide activator, CALM2, PHKD, CAMII, PHKD2, phosphorylase kinase delta.
Gene Symbol CALM1
Gene ID 801
Accession # P62158
Source E. coli
Appearance Lyophilized
Physical Form Description Lyophilized from a salt free solution.
Molecular Weight 16.8 kDa
Purity by SDS-PAGE ≥95%
Biological Activity The Ca2+ binding affinity of rh Calmodulin was evidenced by the electrophoretic mobility shift of Calmodulin in the presence of calcium and EDTA. Calmodulin has been shown to migrate differently in the presence and absence of Calcium. Ref.: Proc Natl Acad
Reconstitution Instructions Reconstitute in water or an appropriate buffer (TBS, PBS, etc)
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans


Calmodulin (CaM) is a ubiquitous, calcium-binding protein that can bind to and regulate a multitude of different protein targets, thereby affecting many different cellular functions. CaM mediates processes such as inflammation, metabolism, apoptosis, muscle contraction, intracellular movement, short-term and long-term memory, nerve growth and the immune response. Calmodulin is expressed in many cell types and can have different subcellular locations, including the cytoplasm, within organelles, or associated with the plasma or organelle membranes. Many of the proteins that CaM binds are unable to bind calcium themselves, and as such use CaM as a calcium sensor and signal transducer. Calmodulin can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum. CaM undergoes a conformational change upon binding to calcium, which enables it to bind to specific proteins for a specific response. CaM can bind up to four calcium ions, and can undergo post-translational modifications, such as phosphorylation, acetylation, methylation and proteolytic cleavage, each of which can potentially modulate its actions.

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