Proinsulin (INS) Antibody – Mouse Monoclonal

After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2010]

Insulin: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Heterodimer of a B chain and an A chain linked by two disulfide bonds. Belongs to the insulin family.

Protein type: Secreted, signal peptide; Secreted; Hormone

Chromosomal Location of Human Ortholog: 11p15.5

Cellular Component: endoplasmic reticulum lumen; ER-Golgi intermediate compartment membrane; extracellular region; extracellular space; Golgi lumen; Golgi membrane; transport vesicle

Molecular Function: hormone activity; identical protein binding; insulin receptor binding; insulin-like growth factor receptor binding; protease binding; protein binding

Biological Process: activation of NF-kappaB transcription factor; activation of protein kinase B; acute-phase response; alpha-beta T cell activation; cell-cell signaling; cellular protein metabolic process; endocrine pancreas development; energy reserve metabolic process; ER to Golgi vesicle-mediated transport; fatty acid homeostasis; G-protein coupled receptor protein signaling pathway; glucose homeostasis; glucose metabolic process; glucose transport; insulin receptor signaling pathway; MAPKKK cascade; negative regulation of acute inflammatory response; negative regulation of fatty acid metabolic process; negative regulation of gluconeogenesis; negative regulation of glycogen catabolic process; negative regulation of lipid catabolic process; negative regulation of NAD(P)H oxidase activity; negative regulation of protein catabolic process; negative regulation of protein oligomerization; negative regulation of protein secretion; negative regulation of proteolysis; negative regulation of vasodilation; positive regulation of cell differentiation; positive regulation of cell growth; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of cellular protein metabolic process; positive regulation of cytokine secretion; positive regulation of DNA replication; positive regulation of glucose import; positive regulation of glycogen biosynthetic process; positive regulation of glycolysis; positive regulation of insulin receptor signaling pathway; positive regulation of lipid biosynthetic process; positive regulation of MAPKKK cascade; positive regulation of mitosis; positive regulation of nitric oxide biosynthetic process; positive regulation of nitric-oxide synthase activity; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of protein amino acid autophosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of vasodilation; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine; regulation of amino acid metabolic process; regulation of insulin secretion; regulation of protein localization; regulation of protein secretion; regulation of transcription, DNA-dependent; regulation of transmembrane transporter activity; wound healing

Disease: Diabetes Mellitus, Insulin-dependent, 2; Diabetes Mellitus, Permanent Neonatal; Hyperproinsulinemia; Maturity-onset Diabetes Of The Young, Type 10