Insulin and insulin-like growth factors (IGFs) are small peptide hormones that play essential roles in regulating metabolism and growth in the body. They bind to specific receptors on the cell surface, initiating signalling cascades that influence various cellular processes. Insulin is produced and released by the beta cells of the pancreas in response to elevated blood glucose levels and acts primarily on cells in the liver, muscle, and adipose tissue. In these tissues insulin promotes glucose uptake, enhances glycogen synthesis in the liver and muscle, and inhibits glucose production in the liver. In addition, insulin stimulates the storage of glucose as glycogen and promotes the synthesis of proteins and lipids and inhibits the breakdown of stored glycogen, proteins, and fats, helping to maintain optimal blood glucose levels. The insulin receptor (InR) is a transmembrane tyrosine kinase receptor located on the surface of target cells and consists of two extracellular alpha subunits and two transmembrane beta subunits. Binding of insulin to the receptor causes a conformational change, activating the receptor's intracellular tyrosine kinase domains. This activation leads to phosphorylation of tyrosine residues on the receptor and subsequent recruitment and activation of downstream signalling molecules. The activated insulin receptor signalling pathway regulates glucose transporters, glycogen synthesis, protein synthesis, and lipid metabolism. Insulin-like growth factors (IGFs) are a family of hormones related to insulin that includes IGF-1 and IGF-2. They are produced by various tissues in the body, including the liver, muscle, and bone. IGFs share structural similarities with insulin and bind to the IGF receptors which are also receptor tyrosine kinases. IGF-1 is primarily involved in promoting tissue growth and development, particularly during childhood and adolescence, whilst IGF-2 plays a role in foetal development and has diverse functions in adult tissues, including regulating cell growth, differentiation, and survival. IGF receptors are transmembrane proteins with tyrosine kinase activity, like the insulin receptor and consist of two alpha subunits and two transmembrane beta subunits. Both IGF-1 and IGF-2 can bind to and activate these receptors. Activation of IGF receptors initiates signalling pathways that promote cell proliferation, survival, and growth. Insulin and insulin-like growth factors (IGFs) play important roles in cancer development and progression. Insulin resistance often occurs in obesity, is associated with increased insulin levels in the blood and has been linked to an increased risk of developing several types of cancers, including colorectal, pancreatic, breast, and endometrial cancer. Insulin and IGFs can also stimulate cell growth and proliferation. They bind to specific receptors on the surface of cells, activating signalling pathways that promote cell division and survival. Insulin and IGFs can also protect cancer cells from undergoing apoptosis. By activating signalling pathways that suppress apoptosis, insulin and IGFs can contribute to the survival and growth of cancer cells. Insulin and IGFs also play a role in promoting angiogenesis, the formation of new blood vessels. Insulin and IGFs can stimulate the production of vascular endothelial growth factor (VEGF), a protein that promotes angiogenesis and facilitates the growth of blood vessels towards the tumour. We offer a large product range of research tools for studying insulin and insulin like growth factors, including Chromogranin A antibodies, IGF1 Receptor antibodies, PDX1 antibodies, IGF1 Receptor ELISA Kits, and IGF2 ELISA Kits. Explore our full insulin and insulin like growth factors product range below and discover more, for less.