I9266
Insulin Receptor from rat liver
buffered aqueous glycerol solution
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About This Item
biological source
rat liver
Quality Level
form
buffered aqueous glycerol solution
packaging
vial of 250 units
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
rat ... Insr(24954)
Biochem/physiol Actions
IR (insulin receptor) protein is a heterotetrameric receptor tyrosine kinase having α subunits for ligand binding and β subunits for tyrosine kinase activity. Insulin works thriought IR. IR is present in the cytoplasm and the nucleus.[3]
Unit Definition
One unit will catalyze the incorporation of 1 pmol per min of phosphate from γ-32P-ATP into poly(Glu,Tyr), 4:1, at 30 °C.
Physical form
Solution in 50% glycerol containing 50 mM HEPES, pH 7.6, 150 mM NaCl, and 0.1% Triton.
Preparation Note
Purified by affinity chromatography on wheat germ agglutinin.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
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Y Zick et al.
The Journal of biological chemistry, 258(1), 75-80 (1983-01-10)
Insulin stimulates phosphorylation of both alpha- and beta- subunits of its own receptor in a cell-free system. A solubilized lectin-purified preparation of insulin receptors from rat liver membranes was preincubated with or without insulin at 4 degrees C and labeled
Maria J Amaya et al.
Hepatology (Baltimore, Md.), 59(1), 274-283 (2013-07-11)
Insulin's metabolic effects in the liver are widely appreciated, but insulin's ability to act as a hepatic mitogen is less well understood. Because the insulin receptor (IR) can traffic to the nucleus, and Ca(2+) signals within the nucleus regulate cell
Zi-Jian Lan et al.
Cellular and molecular life sciences : CMLS, 77(8), 1623-1643 (2019-08-06)
The pathophysiology of type 2 diabetes mellitus (T2D) is characterized by reduced or absent insulin receptor (INSR) responsiveness to its ligand, elevated hepatic glucose output and impaired glucose uptake in peripheral tissues, particularly skeletal muscle. Treatments to reduce hyperglycemia and
Stephen A Whelan et al.
The Journal of biological chemistry, 285(8), 5204-5211 (2009-12-19)
Increased O-linked beta-N-acetylglucosamine (O-GlcNAc) is associated with insulin resistance in muscle and adipocytes. Upon insulin treatment of insulin-responsive adipocytes, O-GlcNAcylation of several proteins is increased. Key insulin signaling proteins, including IRS-1, IRS-2, and PDK1, are substrates for OGT, suggesting potential
Stephen A Whelan et al.
The Journal of biological chemistry, 283(31), 21411-21417 (2008-06-04)
O-Linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) onto serine and threonine residues in response to stimuli or stress analogous to phosphorylation by Ser/Thr-kinases. Like protein phosphatases, OGT appears to be targeted to myriad specific substrates
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