Insulin R/CD220 Antibody (243522) [Alexa Fluor® 700]


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Product Details

Reactivity HuSpecies Glossary
Applications Flow
Alexa Fluor 700

Insulin R/CD220 Antibody (243522) [Alexa Fluor® 700] Summary

Mouse myeloma cell line NS0-derived recombinant human Insulin R/CD220
Accession # P06213
Detects human Insulin R/CD220 in direct ELISAs.
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  • Flow Cytometry 0.25-1 ug/10^6 cells

Packaging, Storage & Formulations

Protect from light. Do not freeze.
  • 12 months from date of receipt, 2 to 8 °C as supplied.
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.


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

Alternate Names for Insulin R/CD220 Antibody (243522) [Alexa Fluor® 700]

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


The Insulin Receptor (INS R) and insulin-like growth factor-1 receptor (IGF-1 R) constitute a subfamily of receptor tyrosine kinases (1‑4). The two receptors share structural similarity as well as overlapping intracellular signaling events, and are believed to have evolved through gene duplication from a common ancestral gene. INS R cDNA encodes a type I transmembrane single chain preproprotein with a putative 27 amino acid residues (aa) signal peptide. The large INS R extracellular domain is organized into two successive homologous globular domains, which are separated by a Cysteine-rich domain, followed by three fibronectin type III domains. The intracellular region contains the kinase domain sandwiched between the juxtamembrane domain used for docking insulin-receptor substrates (IRS), and the carboxy-terminal tail that contains two phosphotyrosine-binding sites. After synthesis, the single chain INS R precursor is glycosylated, dimerized and transported to the Golgi apparatus where it is processed at a furin-cleavage site within the middle fibronectin type III domain to generate the mature disulfide-linked  alpha 2 beta 2 tetrameric receptor. The alpha subunit is localized extracellularly and mediates ligand binding while the transmembrane beta subunit contains the cytoplasmic kinase domain and mediates intracellular signaling. As a result of alternative splicing, two INS R isoforms (A and B) that differ by the absence or presence, respectively, of a 12 aa residue sequence in the carboxyl terminus of the alpha subunit exist. Whereas the A isoform is predominantly expressed in fetal tissues and cancer cells, the B isoform is primarily expressed in adult differentiated cells. Both the A and B isoforms bind insulin with high-affinity, but the A isoform has considerably higher affinity for IGF‑I and IGF-II. Ligand binding induces a conformational change of the receptor, resulting in ATP binding, autophosphorylation, and subsequent downstream signaling. INS R signaling is important in metabolic regulation, but may also contribute to cell growth, differentiation and apoptosis. Mutations in the INS R gene have been linked to insulin-resistant diabetes mellitus, noninsulin-dependent diabetes mellitus and leprechaunism, an extremely rare disorder characterized by abnormal resistance to insulin that results in a variety of distinguishing characteristics, including growth delays and abnormalities affecting the endocrine system. INS R is highly conserved between species, rat INS R shares 94% and 97% aa sequence homology with the human and mouse receptor, respectively.

  1. Nakae, J. et al. (2001) Endoc. Rev. 22:818.
  2. De Meyts, P. and J. Whittaker (2002) Nature Rev. Drug Disc. 1:769.
  3. Kim, J.J. and D. Accili (2002) Growth Hormone and IGF Res. 12:84.
  4. Sciacca, L. et al. (2003) Endocrinology 144:2650.


This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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