antibody

Anti-Insulin Receptor/INSR Antibody Picoband™

PB10072

100μg/vial

polyclonal

domestic rabbit

nonconjugated

human, rat

Anti-Insulin Receptor/INSR Antibody Picoband™

100μg/vial

Polyclonal

Rabbit

Human, Rat

Bovine, Canine, Horse, Monkey, Rabbit

WB

Western blot, 0.1-0.5µg/ml, Human, Rat.

Tested Species: In-house tested species with positive results. Other applications have not been tested. Optimal dilutions should be determined by end users.

Boster Bio Anti-Insulin Receptor/INSR Antibody Picoband™ catalog # PB10072. Tested in WB applications. This antibody reacts with Human, Rat.

Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.

INSR

P06213

A synthetic peptide corresponding to a sequence at the N-terminus of human Insulin Receptor (38-76aa MDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDL), identical to the related mouse and rat sequences.

Lyophilized

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.

Immunogen affinity purified.

No cross reactivity with other proteins.

Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles.

Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

Insulin receptor

Insulin receptor; IR; 2.7.10.1; CD220; Insulin receptor subunit alpha; Insulin receptor subunit beta; INSR;

Insulin receptor

156333 MW

Receptor tyrosine kinase which 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/PKB 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. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol- (3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti- apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K- AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.

Cell membrane; Single-pass type I membrane protein.

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 (at protein level). Overexpressed in several tumors, including breast, colon, lung, ovary, and thyroid carcinomas.

Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.

INSR (INSULIN RECEPTOR) is a tetramer of 2 alpha and 2 beta subunits that are coded by a single gene and are joined by disulfide bonds, a mechanism parallel to that of its ligand, insulin. It belongs to the large class of tyrosine kinase receptors. The insulin receptor gene is mapped to 19p13.2. The insulin receptor mediates their activity by causing the addition of a phosphate group to particular tyrosines on certain proteins within a cell. The INSR gene spans more than 120 kb and has 22 exons. Functional studies of the INSR SNPs show no effect on mRNA levels or splicing in peripheral blood leukocytes or on binding of insulin to mononuclear cells.

Adapters, Cancer, Cytoplasmic, Neuroscience, Neurotransmission, Protein Phosphorylation, Receptor Tyrosine Kinases, Receptors / Channels, Signal Transduction, Tyrosine Kinases