Anti-Insulin Receptor Antibody, Non-Fucosylated (BioBet-1111ZP) (CAT#: BioBet-1111ZP) Datasheet

INSR

insulin receptor

After removal of the precursor signal peptide, the insulin receptor precursor is post-translationally cleaved into two chains (alpha and beta) that are covalently linked. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Two transcript variants encoding different isoforms have been found for this gene.

INSR; insulin receptor; HHF5; CD220; IR

Plasma membrane, Endosome, Lysosome

Diseases associated with INSR include Donohue Syndrome and Hyperinsulinemic Hypoglycemia, Familial, 5.

Its related pathways are RET signaling and Folate Metabolism.

Receptor tyrosine kinase mediates the pleiotropic effects of insulin. The binding of insulin leads to the phosphorylation of several substrates in the cell, including insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins acts as a docking protein for other signal proteins. These signal proteins contain Src-homology-2 domains (SH2 domains), which can specifically recognize different phosphotyrosine residues. Including PI3K and SHP2 p85 regulatory subunits. The phosphorylated protein of the IRS leads to the activation of two main signal pathways: PI3K-AKT/PKB pathway, responsible for the metabolic behavior of insulin, Ras-MAPK pathway, regulating the expression of certain genes and cooperating with PI3K pathway to control cell growth and differentiation. The SH2 domain of PI3K binds to the phosphotyrosines IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5) triphosphate (PIP3), lipid second messenger, activation of several PIP3-dependent serine/threo Acid kinases such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce the glucose transporter SLC2A4/GLUT4 from the cytoplasmic vesicles to the cell membrane to promote glucose transport. In addition, under insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effects by inducing insulin phosphorylation; regulating the expression of gluconeogenesis and lipase, by controlling winged spiral or forkhead (FOX) transcription Factor activity. Another pathway regulated by PI3K-AKT/PKB activation is the mTORC1 signaling pathway, which regulates cell growth and metabolism and integrates insulin signals. AKT mediates insulin-stimulated protein synthesis through phosphorylation of TSC2, thereby activating the mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating insulin cell growth, survival and cell differentiation. Phosphorylated IRS1 recruits the GRB2/SOS complex and triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can also bind insulin-like growth factors (IGFI and IGFII).

Cancer antibody; Neuroscience antibody; Signaling Transduction antibody

After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. Autophosphorylated on tyrosine residues in response to insulin. Phosphorylation of Tyr-999 is required for binding to IRS1, SHC1 and STAT5B. Dephosphorylated by PTPRE at Tyr-999, Tyr-1185, Tyr-1189 and Tyr-1190. Dephosphorylated by PTPRF and PTPN1. Dephosphorylated by PTPN2; down-regulates insulin-induced signaling.

Protein Based Therapies
Monoclonal antibody (mAb)

IgG

BioBet-1111ZP

Mouse

Human

AGT‑182 is an investigational enzyme replacement therapy (ERT) for the treatment of neurological complications in patients with Hunter syndrome. Currently approved treatments for Hunter syndrome do not penetrate the BBB and therefore do not address the severe and progressive neurological complications of the disease. AGT-182 is a fusion protein of iduronate-2-sulfatase (IDS), engineered to cross the BBB by binding to insulin receptors located on the BBB. AGT‑182 crosses the BBB safely at unprecedented levels.

Hunter Syndrome

Hunter Syndrome