CALM2 Human

Calmodulin-2 is composed of 149 amino acids and has a molecular weight of approximately 16 kDa . It can bind up to four Ca²⁺ ions, which induces a conformational change in the protein. This change allows calmodulin to interact with and regulate various target proteins, including protein kinases, phosphatases, ion channels, and receptors . The binding of Ca²⁺ to calmodulin is essential for its role in cellular signaling pathways, particularly those involved in the regulation of the cell cycle and cytokinesis .

Recombinant human calmodulin-2 is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The recombinant protein is often produced without any tags to maintain its native structure and function. The purity of the recombinant calmodulin-2 is usually greater than 90%, as determined by SDS-PAGE .

Calmodulin-2 is involved in various cellular processes, including the regulation of enzyme activity, ion channel function, and signal transduction pathways. It plays a critical role in the centrosome cycle and progression through cytokinesis . Additionally, calmodulin-2 is a substrate for various protein tyrosine kinases and is expected to be phosphorylated at specific sites, such as Thr 44 by CaMK4 .

Recombinant human calmodulin-2 is widely used in research to study calcium signaling pathways and the regulation of target proteins. It is also utilized in various biochemical assays to investigate the interactions between calmodulin and its binding partners. The recombinant protein is valuable for understanding the molecular mechanisms underlying calcium-mediated cellular processes and for developing potential therapeutic interventions targeting calmodulin-regulated pathways.

Recombinant human calmodulin-2 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain the protein’s stability and activity .