Calbindin-2 contains five active and one inactive calcium-binding domains . The protein plays a crucial role in regulating intracellular calcium levels, which is vital for various cellular processes. The sequence of the calbindin-2 cDNA reveals an open reading frame of 271 codons coding for a protein of approximately 31,520 Da .
Calbindin-2 is highly conserved across species, indicating its essential role in biological functions . In mice, the calbindin-2 message is predominantly detected in the brain, while it is absent from other tissues such as heart muscle, kidney, liver, lung, spleen, stomach, and thyroid gland . This specific expression pattern suggests that calbindin-2 has specialized functions in the nervous system.
There are two additional forms of alternatively spliced calbindin-2 mRNAs that encode C-terminally truncated proteins . These truncated proteins, known as calretinin-20k and calretinin-22k, are still capable of binding calcium. The alternative splicing results in different functional forms of the protein, which may have distinct roles in cellular processes.
Calbindin-2 is used in various research applications, particularly in neuroscience, to study its role in calcium signaling and neuronal function. The recombinant form of calbindin-2 (mouse) is often utilized in experimental settings to investigate its biochemical properties and interactions with other proteins.