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Recombinant Human Insulin R/CD220 (aa 28-944) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Human Insulin R/CD220 (aa 28-944) Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When 15 ng/mL of biotinylated recombinant human Insulin is added to serially diluted Recombinant Human Insulin R/CD220, the concentration of Recombinant Human Insulin R/CD220 that produces 50% of the optimal binding response is 0.03‑0.15 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human Insulin R/CD220 protein
His28-Arg750 ( alpha subunit) & Ser751-Lys944 with a C-terminal 10-His tag ( beta subunit)
Accession #
N-terminal Sequence
His28 ( alpha subunit) & Ser751( beta subunit)
Structure / Form
Tetramer; disulfide-linked homodimer of disulfide-linked heterodimers ( alpha & beta )
Protein/Peptide Type
Recombinant Proteins
Gene
INSR
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
82.9 kDa ( alpha subunit), 22.9 kDa ( beta subunit).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
122-135 kDa and 33-43 kDa, reducing conditions
Publications
Read Publications using
1544-IR/CF in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Insulin R/CD220 (aa 28-944) Protein, CF

  • CD 220
  • CD220 antigen
  • CD220
  • EC 2.7.10
  • EC 2.7.10.1
  • HHF5
  • INSR
  • Insulin R
  • insulin receptor
  • InsulinR
  • IR

Background

The Insulin Receptor (gene name INSR, designated CD220) is a type I transmembrane glycoprotein in the Insulin/IGF Receptor family of receptor tyrosine kinases that share structural similarity and overlapping intracellular signaling events (1-3). The 1370 amino acid (aa) human Insulin R preproprotein (A isoform) is processed by proteolysis to remove the signal peptide and produce an extracellular alpha portion (aa 28-750), and an extracellular/transmembrane/cytoplasmic beta subunit (aa 751-1370) (4). The extracellular domain (ECD) contains two homologous globular domains separated by a cysteine-rich domain and followed by three fibronectin type III domains. The intracellular region contains insulin-receptor substrate (IRS) docking sites, the kinase domain, and a phosphotyrosine-containing linker region. The human Insulin R ECD shares 96% aa sequence identity with mouse, rat, equine and canine Insulin R. As a result of alternative splicing, two INSR isoforms that differ by the absence (IR-A) or presence (IR-B) of a 12 aa residue sequence in the carboxyl terminus of the alpha subunit exist (4). IR-A expression is highest in fetal tissues and cancer cells, while IR-B is concentrated in adult differentiated cells (2-5). IR-A and IR-B may homodimerize, or heterodimerize with the IGF-I receptor (1, 3, 4). All receptor combinations bind insulin, IGF-I or IGF-II, but with differing affinities; for example, IR-A has considerably higher affinity for IGF-II as compared to IR-B (2-5). This system allows fine tuning of signaling pathways according to the concentrations of insulin, IGF-I and IGF-II, and expression of receptor subunits on the cell surface (2, 3). Insulin R signaling regulates glucose uptake and metabolism, but also contributes to cell growth, differentiation and apoptosis (2, 3, 5, 6). Mutations in the Insulin R gene have been linked severe insulin resistance (type A and Rabson-Mendenhall syndrome) that may include type II diabetes mellitus and, rarely, leprechaunism (Donohue syndrome) that also includes growth delays and endocrine system abnormalities (1, 7). The R&D Systems human Insulin R consists of the entire ECD of the IR-A isoform.

  1. Nakae, J. et al. (2001) Endoc. Rev. 22:818.
  2. Sciacca, L. et al. (2003) Endocrinology 144:2650.
  3. Belfiore, A. et al. (2009) Endocrine Rev. 30:586.
  4. Lawrence, M.C. et al. (2007) Curr. Opin. Struct. Biol. 17:699.
  5. Sacco, A. et al. (2009) Endocrinology 150:3594.
  6. Kitamura, T. et al. (2004) J. Clin. Invest. 113:209.
  7. Musso, C. et al. (2004) Medicine (Baltimore) 83:209.

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Publications for Insulin R/CD220 (1544-IR/CF)(7)

We have publications tested in 4 confirmed species: Human, Mouse, Hamster, N/A.

We have publications tested in 3 applications: Bioassay, Cell Culture, ELISA (Standard).


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Bioassay
(5)
Cell Culture
(1)
ELISA (Standard)
(1)
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Human
(1)
Mouse
(1)
Hamster
(1)
N/A
(1)
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Showing Publications 1 - 7 of 7.
Publications using 1544-IR/CF Applications Species
NO Yunn, J Lee, HS Lee, EJ Oh, M Park, S Park, SY Jin, E Shin, JWY Lee, Y Kim, SS Bae, SH Ryu An aptamer agonist of the insulin receptor acts as a positive or negative allosteric modulator, depending on its concentration Experimental & Molecular Medicine, 2022-04-27;54(4):531-541. 2022-04-27 [PMID: 35478209] (Bioassay, N/A) Bioassay N/A
NO Yunn, M Park, S Park, J Lee, J Noh, E Shin, SH Ryu A hotspot for enhancing insulin receptor activation revealed by a conformation-specific allosteric aptamer Nucleic Acids Research, 2021-01-25;49(2):700-712. 2021-01-25 [PMID: 33410883] (Bioassay, Human) Bioassay Human
LL Lee, AY Khakoo, V Chintalgat Cardiac pericytes function as key vasoactive cells to regulate homeostasis and disease FEBS Open Bio, 2020-12-14;0(0):. 2020-12-14 [PMID: 33135334] (Cell Culture, Mouse) Cell Culture Mouse
G Scapin, VP Dandey, Z Zhang, W Prosise, A Hruza, T Kelly, T Mayhood, C Strickland, CS Potter, B Carragher Structure of the Insulin Receptor-Insulin Complex by Single Particle CryoEM analysis Nature, 2018-02-28;0(0):. 2018-02-28 [PMID: 29512653] (Bioassay) Bioassay
S Mukherjee, M Chattopadh, S Bhattachar, S Dasgupta, S Hussain, SK Bharadwaj, D Talukdar, A Usmani, BS Pradhan, SS Majumdar, P Chattopadh, S Mukhopadhy, TK Maity, MK Chaudhuri, S Bhattachar A Small Insulinomimetic Molecule Also Improves Insulin Sensitivity in Diabetic Mice PLoS ONE, 2017-01-10;12(1):e0169809. 2017-01-10 [PMID: 28072841] (Bioassay) Bioassay
Corbin , John A, Bhaskar , Vinay, Goldfine , Ira D, Issafras , Hassan, Bedinger , Daniel H, Lau , Angela, Michelson , Kristen, Gross , Lisa M, Maddux , Betty A, Kuan , Hua F, Tran , Catarina, Lao , Llewelyn, Handa , Masahisa, Watson , Susan R, Narasimha , Ajay J, Zhu , Shirley, Levy , Raphael, Webster , Lynn, Wijesuriya , Sujeewa, Liu , Naichi, Wu , Xiaorong, Chemla-Vogel , David, Lee , Steve R, Wong , Steve, Wilcock , Diane, Rubin , Paul, White , Mark L Inhibition of insulin receptor function by a human, allosteric monoclonal antibody: a potential new approach for the treatment of hyperinsulinemic hypoglycemia. MAbs, 2014-01-01;6(1):262-72. 2014-01-01 [PMID: 24423625] (Bioassay, Hamster) Bioassay Hamster
Umehara A, Nishioka M, Obata T A novel ultra-sensitive enzyme immunoassay for soluble human insulin receptor ectodomain and its measurement in urine from healthy subjects and patients with diabetes mellitus. Clin. Biochem., 2009-06-25;42(13):1468-75. 2009-06-25 [PMID: 19560451] (ELISA (Standard)) ELISA (Standard)

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Bioinformatics

Gene Symbol INSR
Uniprot