CALB2 Human

Calbindin-2 is a 29 kDa protein with 58% homology to calbindin 1 . It contains six EF-hand motifs, which are helix-loop-helix structural domains capable of binding calcium ions. These motifs are essential for the protein’s ability to buffer and sense calcium levels within cells . The EF-hand domains are arranged in pairs, and their cooperative binding enhances the protein’s ability to modulate intracellular calcium signals .

Calbindin-2 is predominantly expressed in specific neurons of the central and peripheral nervous systems. It is also observed in non-neuronal cells during embryonic development and in certain cancer cells, such as mesothelioma . In the brain, calbindin-2 is found in various regions, including the cerebral cortex, hippocampus, and cerebellum . The distribution of calbindin-positive neurons varies across different areas and layers of the cortex, reflecting the protein’s diverse roles in sensory processing, motor control, and cognitive functions .

Calbindin-2 serves multiple functions beyond calcium buffering. It interacts with various proteins, including the pore-forming α1 subunit of the Ca2+ channel CaV2.1 and huntingtin, indicating its role as a calcium sensor . The absence of calbindin-2 in certain neurons can lead to increased excitability and altered firing patterns, which may impair motor coordination . Additionally, calbindin-2 is implicated in neuroprotection, cell proliferation, differentiation, and cell death .

Recombinant calbindin-2 is produced using genetic engineering techniques, where the CALB2 gene is inserted into an expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and interactions with other molecules. It is also employed in the development of therapeutic strategies for neurological disorders and cancer.