|Western Blot (WB)||1:1000|
|Flow Cytometry (Flow)||See 1 publications below|
|Miscellaneous PubMed (MISC)||See 1 publications below|
|ELISA (ELISA)||See 1 publications below|
|Western Blot (WB)||See 2 publications below|
|Species reactivity||Human, Mouse, Rat|
|Published species||Human, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of human Insulin Receptor that contains tyrosine 1334.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 1mg/ml BSA, 50% glycerol|
|Contains||0.05% sodium azide|
This antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated Insulin Receptor. The final product is generated by affinity chromatography using a Insulin Receptor-derived peptide that is phosphorylated at tyrosine 1334.
This antibody recognizes human insulin receptor phosphorylated at tyrosine 1334 as well as the human IR Isoform B phosphorylated at tyrosine 1332.
Western blot positive control used was insulin-treated CHO-T cells expressing Human Insulin Receptor.
Insulin Receptor (IR) and Insulin-like Growth Factor Receptor (IGF-1R) are transmembrane tyrosine kinase receptors that play critical roles in development, cell growth, and metabolism. Biological actions of insulin and IGF-1 are mediated by their respective cell surface receptor tyrosine kinases, which regulate multiple signaling pathways through activation of a series of phosphorylation cascades. Both receptors are composed of alpha subunits which contain ligand binding sites, and beta subunits which are hormone stimulated, tyrosine-specific protein kinases. The beta subunits contain several autophosphorylation sites located in three major domains: the juxtamembrane domain, the activation domain, and the carboxyl domain. These two receptors differ in sequence in regions that confer specificity for the designated ligand as well as in certain intracellular signaling domains, resulting in significant differences in the functional consequences of activation of each receptor. Insulin/IGF-1 binding to the extracellular domain leads to activation of the tyrosine kinase activity of IR results in immediate autophosphorylation of six tyrosine residues followed by the serine sites in the beta subunit (98 kDa) and tyrosine and serine phosphorylation of the intracellular substrates of the receptor. Tyrosine autophosphorylation within the activation loop is correlated with full activation of the receptor. The C-terminus of the beta-subunit of the Insulin Receptor contains two tyrosine residues in the distal region (tyrosine 1328 and tyrosine 1334) that are phosphorylated in response to insulin. Phosphorylation of tyrosines 1328 and 1334 is required for the insulin-stimulated tyrosine dephosphorylation of pp125FAK and plays an inhibitory role of insulin-induced mitogenic signaling. Defects in IR are the cause of various insulin resistance syndromes and IGF-1R defects may cause some forms of growth retardation. Both these signaling cascades are also important for the development of cancer.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: CD220; CD220 beta; HHF5; Insulin receptor; Insulin Receptor beta; insulin receptor preproprotein; IR; IR beta
Gene Aliases: 4932439J01Rik; CD220; D630014A15Rik; HHF5; INSR; IR; IR-A; IR-B
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