S100 Calcium Binding Protein G, also known as calbindin D9K, is a member of the S100 protein family. This family consists of more than 20 low-molecular-weight calcium-binding proteins characterized by the presence of EF-hand motifs, which are helix-loop-helix structures that bind calcium ions. The S100 proteins play crucial roles in various cellular processes, including cell cycle regulation, differentiation, and signal transduction .
S100 Calcium Binding Protein G is a cytosolic protein that binds calcium ions in a vitamin D-dependent manner. It is primarily found in the intestine, where its expression correlates with calcium transport activity. The protein has a molecular weight of approximately 10-14 kDa and contains two EF-hand motifs that allow it to bind two calcium ions with different affinities .
The binding of calcium ions induces a conformational change in the protein, exposing hydrophobic regions that facilitate interactions with target proteins. These interactions are essential for the protein’s role in calcium signal transduction and regulation of various cellular processes .
The expression of S100 Calcium Binding Protein G is regulated by several transcription factors, including c-Myc, P53, NF-κB, USF, and Nrf2. The expression level varies depending on the specific cell type and the physical and chemical environment. Additionally, epigenetic modifications such as histone acetylation and DNA methylation also play a role in regulating the expression of this protein .
Altered expression of S100 Calcium Binding Protein G has been associated with various pathological conditions. For instance, its expression is often dysregulated in cancers, where it may play a role in tumor progression and metastasis. The protein’s involvement in calcium-dependent cellular processes makes it a potential biomarker for differential diagnosis and prognosis evaluation in various diseases .
The human recombinant form of S100 Calcium Binding Protein G is produced using recombinant DNA technology. This involves inserting the gene encoding the protein into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. The recombinant protein is then purified and used for various research and therapeutic applications.