S100 Calcium Binding Protein G, also known as calbindin-D9k, is a member of the S100 protein family. This family consists of low-molecular-weight proteins characterized by their ability to bind calcium ions. The S100 proteins play crucial roles in various cellular processes, including cell cycle progression, differentiation, and regulation of intracellular calcium levels.
S100G, or calbindin-D9k, is a small cytosolic protein with a molecular weight of approximately 9 kDa. It contains two EF-hand motifs, which are helix-loop-helix structures capable of binding calcium ions. The binding of calcium induces conformational changes in the protein, which are essential for its function.
S100G is predominantly expressed in the intestine, where its expression is regulated by vitamin D. The protein is involved in the active transport of calcium across the intestinal epithelium, playing a critical role in calcium homeostasis. Additionally, S100G is found in other tissues, including the kidneys and placenta, where it may have similar functions related to calcium transport and regulation.
Recombinant S100G (Rat) is produced using molecular cloning techniques. The gene encoding the rat S100G protein is inserted into an expression vector, which is then introduced into a host organism, typically Escherichia coli. The host cells express the protein, which is subsequently purified using various chromatographic techniques. Recombinant production allows for the generation of large quantities of the protein for research and therapeutic purposes.
S100G has been extensively studied for its role in calcium metabolism and its potential implications in various diseases. Research has shown that alterations in S100G expression are associated with conditions such as osteoporosis, chronic kidney disease, and certain cancers. The protein is also used as a marker in studies investigating calcium absorption and metabolism.