antibody

IR (Phospho-Thr1375) Antibody

MBS852561

0.1 mg

215 USD

polyclonal

rabbit

nonconjugated

human, mouse, rat

western blot, ELISA, enzyme immunoassay

Antibody

IR (Phospho-Thr1375) Antibody

IR

CD220 antigen; EC 2.7.10.1; insulin receptor; IR; kinase InsR

insulin receptor isoform Long preproprotein; Insulin receptor; insulin receptor; IR; insulin receptor; CD_antigen: CD220Cleaved into the following 2 chains:Insulin receptor subunit alpha; Insulin receptor subunit beta

IR

INSR; INSR; HHF5; CD220; IR

INSR_HUMAN

Rabbit

Human, Mouse, Rat

1382

INSR (Phospho-Thr1375) antibody detects endogenous levels of INSR only when phosphorylated at threonine 1375.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Store at -20 degree C for 1 year

Western Blot (WB), ELISA (EIA)

WB: 1:500~1:1000, ELISA: 1:5000

Reactivity Note: Human (Identities = 100%, Positives = 100%); Mouse (Identities = 92%, Positives = 100%); Rat (Identities = 92%, Positives = 100%)

Immunogen: The antiserum was produced against synthesized phosphopeptide derived from human INSR around the phosphorylation site of threonine 1375 (I-L-TP-L-P). All Sites: Human: Thr1375; Mouse: Thr1365; Rat: Thr1376. Pathway: Phospho-specific

Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells; Autophagy antibody

Ebina Y., Cell 40:747-758(1985). Ullrich A., Nature 313:756-761(1985). Seino S., Diabetes 39:123-128(1990).

119395736

NP_000199.2

NM_000208.2

P06213

155,146 Da

AGE/RAGE Pathway (698754); AMPK Signaling Pathway (198868); AMPK Signaling Pathway (989139); AMPK Signaling Pathway (992181); Adherens Junction Pathway (83070); Adherens Junction Pathway (481); Aldosterone-regulated Sodium Reabsorption Pathway (130626); Aldosterone-regulated Sodium Reabsorption Pathway (130590); DNA Damage Response (only ATM Dependent) Pathway (198827); FoxO Signaling Pathway (921162)

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. [provided by RefSeq, Jul 2008]

INSR: a receptor tyrosine kinase that mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). The holoenzyme is cleaved into two chains, the alpha and beta subunits. The active complex is a tetramer containing 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains constitute the ligand- binding domain, while the beta chains carry the kinase domain. Interacts with SORBS1 but dissociates from it following insulin stimulation. Familial mutations associated with insulin resistant diabetes, acanthosis nigricans, pineal hyperplasia, and polycystic ovary syndrome. SNP variants may be associated with polycystic ovary syndrome, atypical migraine and diabetic hyperlipidemia. Mutations also cause leprechaunism, a severe insulin resistance syndrome causing growth retardation and death in early infancy. Two isoforms of the human protein are produced by alternative splicing. The Short isoform has a higher affinity for insulin than the longer. Isoform Long and isoform Short are predominantly expressed in tissue targets of insulin metabolic effects: liver, adipose tissue and skeletal muscle but are also expressed in the peripheral nerve, kidney, pulmonary alveoli, pancreatic acini, placenta vascular endothelium, fibroblasts, monocytes, granulocytes, erythrocytes and skin. Isoform Short is preferentially expressed in fetal cells such as fetal fibroblasts, muscle, liver and kidney. Found as a hybrid receptor with IGF1R in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta. Overexpressed in several tumors, including breast, colon, lung, ovary, and thyroid carcinomas. Protein type: Protein kinase, tyrosine (receptor); EC 2.7.10.1; Kinase, protein; Membrane protein, integral; Protein kinase, TK; TK group; InsR family. Chromosomal Location of Human Ortholog: 19p13.3-p13.2. Cellular Component: membrane; intracellular membrane-bound organelle; integral to plasma membrane; plasma membrane; endosome membrane; caveola; receptor complex. Molecular Function: GTP binding; PTB domain binding; receptor signaling protein tyrosine kinase activity; insulin-like growth factor II binding; insulin binding; insulin-like growth factor receptor binding; protein binding; insulin-like growth factor I binding; insulin receptor substrate binding; protein-tyrosine kinase activity; phosphoinositide 3-kinase binding; ATP binding; insulin receptor activity. Biological Process: heart morphogenesis; epidermis development; positive regulation of nitric oxide biosynthetic process; peptidyl-tyrosine phosphorylation; activation of MAPK activity; protein amino acid autophosphorylation; regulation of embryonic development; positive regulation of glycogen biosynthetic process; exocrine pancreas development; glucose homeostasis; positive regulation of glucose import; positive regulation of MAPKKK cascade; regulation of transcription, DNA-dependent; male sex determination; positive regulation of cell proliferation; protein heterotetramerization; positive regulation of developmental growth; positive regulation of mitosis; activation of protein kinase B; G-protein coupled receptor protein signaling pathway; positive regulation of protein kinase B signaling cascade; cellular response to insulin stimulus; positive regulation of glycolysis; carbohydrate metabolic process; insulin receptor signaling pathway; activation of protein kinase activity; positive regulation of protein amino acid phosphorylation; positive regulation of DNA replication; positive regulation of cell migration; transformation of host cell by virus. Disease: Diabetes Mellitus, Insulin-resistant, With Acanthosis Nigricans; Hyperinsulinemic Hypoglycemia, Familial, 5; Pineal Hyperplasia, Insulin-resistant Diabetes Mellitus, And Somatic Abnormalities; Donohue Syndrome

0.1 mg

215 USD