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Human/Mouse Insulin R/CD220 Allophycocyanin Affinity Pur PAb  100 TESTS图1

Human/Mouse Insulin R/CD220 Allophycocyanin Affinity Pur PAb 100 TESTS

2024-11-24 17:36IP属地 广东省东莞市 电信00留言

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Flow Cytometry      
     

Detection of Insulin R/CD220 in Human Blood Monocytes by Flow Cytometry. Human peripheral blood monocytes were stained with Goat Anti-Human/Mouse Insulin R/CD220 APC‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB1544A, filled histogram) or isotype control antibody (Catalog # , open histogram). View our protocol for .

Flow Cytometry      
     

Detection of Insulin R/CD220 in Neuro‑2A Mouse Cell Line by Flow Cytometry. Neuro‑2A mouse neuroblastoma cell line was stained with Goat Anti-Human/Mouse Insulin R/CD220 APC‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB1544A, filled histogram) or isotype control antibody (Catalog # , open histogram). View our protocol for .

Preparation and Storage

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.

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