Human Insulin R/CD220 Antibody Summary
His28-Lys956
Accession # P06213
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Insulin R/CD220 in NS0 Mouse Cell Line Transfected with Human Insulin R/CD220 by Flow Cytometry. NS0 mouse myeloma cell line transfected with human Insulin R/CD220 (filled histogram), or irrelevant transfectant (open histogram) were stained with Mouse Anti-Human Insulin R/CD220 Monoclonal Antibody (Catalog # MAB15442) or Mouse IgG2B Isotype Control (Catalog # MAB0041, data not shown) followed by APC-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B). View our protocol for Staining Membrane-associated Proteins.
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Detection of Insulin R/CD220 in Human PBMC lymphocytes by Flow Cytometry. Human PBMC lymphocytes were stained with Mouse Anti-Human Insulin R/CD220 Monoclonal Antibody (Catalog # MAB15442, filled histogram) or Mouse IgG2B Isotype Control (Catalog # MAB0041, open histogram) followed by APC-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B). View our protocol for Staining Membrane-associated Proteins.
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Insulin R/CD220 in RT‑4 Human Cell Line. Insulin R/CD220 was detected in immersion fixed RT-4 human urinary bladder transitional cell papilloma cell line using Mouse Anti-Human Insulin R/CD220 Monoclonal Antibody (Catalog # MAB15442) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cell membrane. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
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Detection of Insulin R/CD220 in PBMC cells by Flow Cytometry. PBMC were stained with Mouse Anti-Human CD14 PE‑conjugated Monoclonal Antibody (Catalog # FAB3832P) and either (A) Mouse Anti-Human Insulin R/CD220 Monoclonal Antibody (Catalog # MAB15442) or (B) Mouse IgG2B Isotype Control (Catalog # MAB004) followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B). View our protocol for Staining Membrane-associated Proteins.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Insulin R/CD220
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.
- Nakae, J. et al. (2001) Endoc. Rev. 22:818.
- De Meyts, P. and J. Whittaker (2002) Nature Rev. Drug Disc. 1:769.
- Kim, J.J. and D. Accili (2002) Growth Hormone and IGF Res. 12:84.
- Sciacca, L. et al. (2003) Endocrinology 144:2650.
Product Datasheets
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