Anti-INSR antibody (900-950) {FITC} (STJ501476)

SKU:
STJ501476-100

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Host: Rabbit
Applications: ELISA/IP/WB
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-INSR (900-950) is suitable for use in ELISA, Immunoprecipitation and Western Blot research applications.
Clonality: Polyclonal
Conjugation: FITC
Isotype: IgG
Purification: Affinity Purified
Concentration: 0.55-0.75 µg/µl
Dilution Range: WB: 1:500
ELISA: 1:10, 000
IP: 1:200
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: INSR
Gene ID: 3643
Uniprot ID: INSR_HUMAN
Immunogen Region: 900-950
Immunogen: Synthetic peptide taken within amino acid region 900-950 on human Insulin receptor, transcript variant 2 protein. Cross reactive with both Insulin receptor alpha and insulin receptor beta variants.
Tissue Specificity 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.
Post Translational Modifications 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.
Function 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 phosphotyrosine 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. In adipocytes, inhibits lipolysis.
Protein Name Insulin Receptor
Ir
Cd Antigen Cd220 Cleaved Into - Insulin Receptor Subunit Alpha - Insulin Receptor Subunit Beta
Database Links Reactome: R-HSA-6811558
Reactome: R-HSA-74713
Reactome: R-HSA-74749
Reactome: R-HSA-74751
Reactome: R-HSA-74752
Reactome: R-HSA-77387
Cellular Localisation Cell Membrane
Single-Pass Type I Membrane Protein
Late Endosome
Lysosome
Binding Of Insulin To Insr Induces Internalization And Lysosomal Degradation Of The Receptor
A Means For Down-Regulating This Signaling Pathway After Stimulation
In The Presence Of Sorl1
Internalized Insr Molecules Are Redirected Back To The Cell Surface
Thereby Preventing Their Lysosomal Catabolism And Strengthening Insulin Signal Reception
Alternative Antibody Names Anti-Insulin Receptor antibody
Anti-Ir antibody
Anti-Cd Antigen Cd220 Cleaved Into - Insulin Receptor Subunit Alpha - Insulin Receptor Subunit Beta antibody
Anti-INSR antibody

Information sourced from Uniprot.org

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