CALML3 Human

CALML3 contains four EF-hand domains, which are crucial for its ability to bind calcium ions. The protein’s structure allows it to interact with various cellular substrates, influencing numerous cellular processes. The EF-hand domains are characterized by a loop of 12 amino acids rich in acidic residues, which coordinate calcium ions and link two α-helical segments in a perpendicular manner .

CALML3 is expressed in several normal tissues, including mammary, prostate, cervical, and epidermal tissues . This widespread expression suggests that CALML3 plays a significant role in various physiological processes across different tissue types.

Recombinant human CALML3 protein is produced using Escherichia coli (E. coli) as the expression system. The recombinant protein is typically fused to a His-tag at the N-terminus, which facilitates its purification through conventional chromatography techniques . The amino acid sequence of the recombinant protein includes the His-tag and corresponds to the amino acids 1-149 of human CALML3 .

Recombinant CALML3 is used in various research applications to study its role in calcium signaling and its interactions with other cellular proteins. It is particularly useful in understanding how CALML3 competes with calmodulin and its potential regulatory functions in different tissues .

For optimal stability, recombinant CALML3 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 integrity. The protein is typically stored in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, and 10% glycerol .