07-724 | Anti-α-Insulin Receptor Antibody, β subunit

100 µL  
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      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, M, R, ChpIP, WBRbAffinity PurifiedPolyclonal Antibody
      Catalogue Number07-724
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionAnti-α-Insulin Receptor Antibody, β subunit
      Alternate Names
      • CD220 antigen
      • insulin receptor
      Background InformationThe insulin receptor is a tyrosine kinase receptor that when bound to insulin, initiates multiple signal transduction pathways, including JNK, PI 3-kinase, Akt and PKC. Pharmacological intervention of these Insulin R-dependent pathways is of great interest for the treatment of insulin resistance, obesity and diabetes. The Insulin Receptor (IR) is synthesized as a single polypeptide, which is subsequently cleaved to generate an extracellular α-chain and a transmembrane and intracellular β-chain, tethered together by disulfide bonds. The β-chain has multiple tyrosine phosphorylation sites, including three autophosphorylation sites at its activation loop. The overall structure of the IR is highly homologous to the IGF-I Receptor, except in their c-termini, where the two proteins diverge somewhat. The IR signals primarily by phosphorylating the Insulin Receptor Substrate (IRS) family of proteins, which creates docking sites for SH2-domain containing proteins. Insulin signaling is highly dependent on the PI3 Kinase pathway and Akt, which appear to mediate the functions of insulin.
      Product Information
      FormatAffinity Purified
      • Human brain tissue lysate
      PresentationPurified rabbit polyclonal serum in buffer containing 0.1 M Tris-glycine, pH 7.4, 150 mM NaCl and 0.05% sodium azide.
      ApplicationAnti-α-Insulin Receptor Antibody, β subunit is an antibody against a-Insulin Receptor for use in IP & WB.
      Key Applications
      • Immunoprecipitation
      • Western Blotting
      Application NotesImmunoprecipitation Analysis:
      Biological Information
      ImmunogenGST-fusion protein corresponding to the last 100 C-terminal amino acid residues of the human insulin receptor β chain
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificityThis antibody recognizes α-Insulin Receptor, β subunit.
      Species Reactivity
      • Human
      • Mouse
      • Rat
      • Chimpanzee
      Species Reactivity NoteProven to react with human, mouse, and rat. Predicted to react with chimpanzee based on sequence homology.
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryAfter 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.
      Gene Symbol
      • INSR
      • CD220
      • HHF5
      • IR
      Purification MethodAffinity Purfied
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P06213 # This receptor binds insulin and has a tyrosine-protein kinase activity. Isoform Short has a higher affinity for insulin. Mediates the metabolic functions of insulin. Binding to insulin stimulates association of the receptor with downstream mediators including IRS1 and phosphatidylinositol 3'-kinase (PI3K). Can activate PI3K either directly by binding to the p85 regulatory subunit, or indirectly via IRS1.
      SIZE: 1382 amino acids; 156307 Da
      SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand- binding domain, while the beta chains carry the kinase domain. Interacts with SORBS1 but dissociates from it following insulin stimulation. Binds SH2B2. Interacts with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues. The sequences surrounding the phosphorylated NPXY motif contribute differentially to either IRS1 or SHC1 recognition. Interacts with the SH2 domains of the 85 kDa regulatory subunit of PI3K (PIK3R1) in vitro, when autophosphorylated on tyrosine residues. Interacts with SOCS7.
      SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
      TISSUE SPECIFICITY: Isoform Long and isoform Short are expressed in the peripheral nerve, kidney, liver, striated muscle, fibroblasts and skin. Isoform Short is expressed also in the spleen and lymphoblasts.
      PTM: 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 IRS1- and SHC1- binding.
      DISEASE: SwissProt: P06213 # Defects in INSR are the cause of insulin resistance (Ins resistance) [MIM:125853]. & Defects in INSR are the cause of Rabson-Mendenhall syndrome [MIM:262190]; also known as Mendenhall syndrome. It is a severe insulin resistance syndrome characterized by insulin- resistant diabetes mellitus with pineal hyperplasia and somatic abnormalities. Typical features include coarse, senile-appearing facies, dental and skin abnormalities, abdominal distension, and phallic enlargement. Inheritance is autosomal recessive. & Defects in INSR are the cause of leprechaunism [MIM:246200]; also known as Donohue syndrome. Leprechaunism represents the most severe form of insulin resistance syndrome, characterized by intrauterine and postnatal growth retardation and death in early infancy. Inheritance is autosomal recessive. & Defects in INSR may be associated with noninsulin- dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type 2. & Defects in INSR are the cause of familial hyperinsulinemic hypoglycemia 5 (HHF5) [MIM:609968]. Familial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. & Defects in INSR are the cause of insulin-resistant diabetes mellitus with acanthosis nigricans type A (IRAN type A) [MIM:610549]. This syndrome is characterized by the association of severe insulin resistance (manifested by marked hyperinsulinemia and a failure to respond to exogenous insulin) with the skin lesion acanthosis nigricans and ovarian hyperandrogenism in adolescent female subjects. Women frequently present with hirsutism, acne, amenorrhea or oligomenorrhea, and virilization. This syndrome is different from the type B that has been demonstrated to be secondary to the presence of circulating autoantibodies against the insulin receptor.
      SIMILARITY: SwissProt: P06213 ## Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. & Contains 2 fibronectin type-III domains. & Contains 1 protein kinase domain.
      Molecular Weight97 kDa
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceEvaluated by Western Blot in Human brain tissue lysate.
      Western Blot Analysis: : 1:1,000 dilution of this antibody detected α-Insulin Receptor, β subunit in human brain tissue lysate.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain refrigerated at 2-8°C for for 1 year from date of receipt.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      Anti-Insulin Receptor, subunit (rabbit immunoaffinity purified IgG) - DAM1411337 DAM1411337
      Anti-Insulin Receptor, subunit (rabbit immunoaffinity purified IgG) - DAM1413946 DAM1413946
      Anti-Insulin Receptor, beta; subunit - 0612047214 0612047214
      Anti-Insulin Receptor, beta; subunit - 30474 30474
      Anti-Insulin Receptor, beta; subunit - 33460 33460
      Anti-a-Insulin Receptor, subunit - DAM1749943 DAM1749943
      Anti-a-Insulin Receptor, subunit - NG1624968 NG1624968
      Anti-α-Insulin Receptor, β subunit 3079707
      Anti-α-Insulin Receptor, β subunit - 2383144 2383144
      Anti-α-Insulin Receptor, β subunit - 2436418 2436418


      Reference overviewApplicationPub Med ID
      Role of protein farnesylation in burn-induced metabolic derangements and insulin resistance in mouse skeletal muscle.
      Nakazawa, H; Yamada, M; Tanaka, T; Kramer, J; Yu, YM; Fischman, AJ; Martyn, JA; Tompkins, RG; Kaneki, M
      PloS one  10  e0116633  2015

      Show Abstract
      Western Blotting25594415 25594415
      Reversing the reduced level of endometrial GLUT4 expression in polycystic ovary syndrome: a mechanistic study of metformin action.
      Li, X; Cui, P; Jiang, HY; Guo, YR; Pishdari, B; Hu, M; Feng, Y; Billig, H; Shao, R
      American journal of translational research  7  574-86  2015

      Show Abstract
      26045896 26045896
      Insulin responsiveness in metabolic syndrome after eight weeks of cycle training.
      Stuart, CA; South, MA; Lee, ML; McCurry, MP; Howell, ME; Ramsey, MW; Stone, MH
      Medicine and science in sports and exercise  45  2021-9  2013

      Show Abstract
      23669880 23669880
      Hepatic STAMP2 decreases hepatitis B virus X protein-associated metabolic deregulation.
      Kim, HY; Cho, HK; Yoo, SK; Cheong, JH
      Experimental & molecular medicine  44  622-32  2012

      Show Abstract
      23095254 23095254
      Insulin receptor and IRS-1 co-immunoprecipitation with SOCS-3, and IKKα/β phosphorylation are increased in obese Zucker rat skeletal muscle.
      Zolotnik, IA; Figueroa, TY; Yaspelkis, BB
      Life sciences  91  816-22  2012

      Show Abstract
      22982470 22982470
      Expression of the IGF axis is decreased in local prostate cancer but enhanced after benign prostate epithelial differentiation and TGF-β treatment.
      Massoner, P; Ladurner Rennau, M; Heidegger, I; Kloss-Brandstätter, A; Summerer, M; Reichhart, E; Schäfer, G; Klocker, H
      The American journal of pathology  179  2905-19  2011

      Show Abstract
      Western Blotting21983635 21983635
      Aerobic training reverses high-fat diet-induced pro-inflammatory signalling in rat skeletal muscle.
      Ben B Yaspelkis,Ilya A Kvasha,Sarah J Lessard,Donato A Rivas,John A Hawley
      European journal of applied physiology  110  2010

      Show Abstract
      20596724 20596724
      Hepatitis B virus X protein impairs hepatic insulin signaling through degradation of IRS1 and induction of SOCS3.
      Kim, K; Kim, KH; Cheong, J
      PloS one  5  e8649  2010

      Show Abstract
      20351777 20351777
      Oxidative stress contributes to aging by enhancing pancreatic angiogenesis and insulin signaling.
      Gaëlle Laurent,Florence Solari,Bogdan Mateescu,Melis Karaca,Julien Castel,Brigitte Bourachot,Christophe Magnan,Marc Billaud,Fatima Mechta-Grigoriou
      Cell metabolism  7  2008

      Show Abstract
      18249171 18249171
      Phosphoinositide 3-kinase p110beta activity: key role in metabolism and mammary gland cancer but not development.
      Ciraolo, E; Iezzi, M; Marone, R; Marengo, S; Curcio, C; Costa, C; Azzolino, O; Gonella, C; Rubinetto, C; Wu, H; Dastrù, W; Martin, EL; Silengo, L; Altruda, F; Turco, E; Lanzetti, L; Musiani, P; Rückle, T; Rommel, C; Backer, JM; Forni, G; Wymann, MP; Hirsch, E
      Science signaling  1  ra3  2008

      Show Abstract
      18780892 18780892

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