CALM2 Human 135 a.a

Calmodulin-2 is composed of 135 amino acids and has a molecular weight of approximately 16 kDa . The protein contains four functional Ca²⁺-binding sites, known as EF-hands, which are crucial for its ability to bind calcium ions . These binding sites are located at the following amino acid positions:

• aa 20-31
• aa 56-67
• aa 93-104
• aa 129-140

Upon binding to Ca²⁺, calmodulin undergoes a conformational change that allows it to interact with and regulate a variety of target proteins and enzymes. Some of the key enzymes activated by calmodulin include:

• Myosin Light Chain Kinase (MLCK)
• Cyclic Nucleotide-Dependent Phosphodiesterase
• Calcineurin
• ATPase
• CAM Kinase

Calmodulin-2 is involved in numerous cellular processes, including muscle contraction, cell division, and signal transduction. It acts as an intracellular receptor for Ca²⁺ ions, translating calcium signals into cellular responses. This makes it a crucial component in the regulation of various physiological functions.

Recombinant human calmodulin-2 is typically expressed in Escherichia coli (E. coli) and purified for research and therapeutic applications . The recombinant protein is often tagged with a His•Tag sequence at the N-terminus to facilitate purification and detection . It is available in various forms, including full-length proteins and specific fragments, depending on the research requirements.

Recombinant calmodulin-2 is widely used in biochemical and biophysical studies to understand its interaction with target proteins and its role in cellular processes. It is also employed in drug discovery and development, particularly in the context of diseases where calcium signaling is disrupted.

Recombinant calmodulin-2 should be stored at -20°C to -80°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles to prevent degradation . When stored properly, the protein remains stable for up to 12 months.