Rabbit anti-Rat INSR Polyclonal Antibody | anti-INSR antibody

INSR Antibody (C-term)

Cat. Num. AAA9213931

• Gene Names: INSR; HHF5; CD220
• Reactivity: Rat
• Applications: Western Blot, ELISA
• Purity: Purified Rabbit Polyclonal Antibody (Pab)
• Synonyms: INSR; Polyclonal Antibody; INSR Antibody (C-term); Insulin receptor; IR; CD220; Insulin receptor subunit alpha; Insulin receptor subunit beta; anti-INSR antibody

• Host: Rabbit
• Reactivity: Rat
• Clonality: Polyclonal
• Isotype: Rabbit Ig
• Specificity: This INSR antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 1362-1395 amino acids from the C-terminal region of human INSR.
• Purity/Purification: Purified Rabbit Polyclonal Antibody (Pab)
• Form/Format: Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
• Concentration: Vial Concentration: 0.369 (varies by lot)
• Sequence Length: 1382

• Applicable Applications for anti-INSR antibody: Western Blot (WB), ELISA (EIA)
• Application Notes: WB~~1:1000
• Antigen Source: HUMAN
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Western Blot (WB)

(Western blot analysis of lysate from rat liver tissue lysate, using INSR Antibody (C-term). MBS9213931 was diluted at 1:1000. A goat anti-rabbit IgG H&L(HRP) at 1:10000 dilution was used as the secondary antibody. Lysate at 20ug.)

Related Product Information for anti-INSR antibody

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.

Product Categories/Family for anti-INSR antibody

Cancer; Cardiovascular; Metabolism; Signal transduction

References

Ebina Y.,et al.Cell 40:747-758(1985).
Ullrich A.,et al.Nature 313:756-761(1985).
Chen E.Y.,et al.Submitted (JUL-1985) to the EMBL/GenBank/DDBJ databases.
Seino S.,et al.Diabetes 39:123-128(1990).
Grimwood J.,et al.Nature 428:529-535(2004).

NCBI and Uniprot Product Information

• NCBI GI #: 119395736
• NCBI GeneID: 3643
• NCBI Accession #: NP_000199.2
• NCBI GenBank Nucleotide #: NM_000208.2
• UniProt Accession #: P06213; Q17RW0; Q59H98; Q9UCB7; Q9UCB8; Q9UCB9
• Molecular Weight: 156333
• NCBI Official Full Name: insulin receptor isoform Long preproprotein
• NCBI Official Synonym Full Names: insulin receptor
• NCBI Official Symbol: INSR
• NCBI Official Synonym Symbols: HHF5; CD220
• NCBI Protein Information: insulin receptor
• UniProt Protein Name: Insulin receptor
• Protein Family: Insulin receptor
• UniProt Gene Name: INSR
• UniProt Synonym Gene Names: IR
• UniProt Entry Name: INSR_HUMAN

NCBI Description

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]

Uniprot Description

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: Kinase, protein; EC 2.7.10.1; Protein kinase, TK; Membrane protein, integral; Protein kinase, tyrosine (receptor); 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: insulin binding; insulin-like growth factor receptor binding; protein binding; insulin-like growth factor I binding; GTP binding; insulin receptor substrate binding; protein-tyrosine kinase activity; PTB domain binding; phosphoinositide 3-kinase binding; receptor signaling protein tyrosine kinase activity; insulin-like growth factor II binding; ATP binding; insulin receptor activity

Biological Process: heart morphogenesis; epidermis development; peptidyl-tyrosine phosphorylation; positive regulation of nitric oxide biosynthetic process; 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; carbohydrate metabolic process; positive regulation of glycolysis; activation of protein kinase activity; insulin receptor signaling pathway; 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