Insulin
Insulin is a secreted peptide hormone of the insulin family that regulates carbohydrate and lipid metabolism and lowers blood glucose concentration. The INS gene, also known as IDDM2 or IDDM1, encodes the precursor from which mature insulin is produced. Browse Assay Genie's current range of Insulin research reagents below, or read on for the biology behind the target.
Insulin decreases blood glucose concentration and plays a vital role in the regulation of carbohydrate and lipid metabolism. It increases cell permeability to monosaccharides, amino acids and fatty acids, and in liver it accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake, which makes the insulin–INSR axis a central reference point for studies of metabolic signalling.
The INS gene encodes a precursor that is processed after removal of the signal peptide. The resulting proinsulin is post-translationally cleaved into three peptides: the B chain and A chain, which are covalently linked by two disulphide bonds to form mature insulin, and C-peptide. Insulin is a secreted protein and belongs to the insulin family, which HGNC also places within the neuropeptides gene group.
Many mutant alleles of INS with phenotypic effects have been identified. These include insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10 and hyperproinsulinemia. The gene carries the aliases IDDM2 and IDDM1, reflecting its historical name, insulin-dependent diabetes mellitus 2. A read-through gene, INS-IGF2, overlaps INS at its 5' region and the IGF2 gene at its 3' region, which is worth bearing in mind when designing and interpreting gene-level experiments.
Mutant INS alleles are linked to insulin-dependent diabetes mellitus, permanent neonatal diabetes and maturity-onset diabetes of the young type 10.
Insulin lowers blood glucose concentration and, through INSR, stimulates glucose uptake, making it central to carbohydrate metabolism research.
Insulin raises cell permeability to monosaccharides, amino acids and fatty acids, supporting work on cellular nutrient handling.
Proinsulin is cleaved into the A chain, B chain and C-peptide, and defects can cause hyperproinsulinemia.
Insulin is a peptide hormone that decreases blood glucose concentration and regulates carbohydrate and lipid metabolism. It increases cell permeability to monosaccharides, amino acids and fatty acids, and accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver. Its binding to INSR stimulates glucose uptake.
The INS gene is also known as IDDM2 and IDDM1, and was previously named insulin-dependent diabetes mellitus 2. Proinsulin loses its signal peptide and is cleaved into the B chain, A chain and C-peptide; the A and B chains are joined by two disulphide bonds.
Yes. Mutant INS alleles have been associated with insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10 and hyperproinsulinemia. Check the datasheet of any product for its validated reactivity before using it in a disease model.
Insulin-like peptides and insulin-related proteins with research reagents at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P01308; product specifications from Assay Genie datasheets.