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Eurofins DiscoverX Insulin Receptor Protein, Activated
Description
The insulin receptor kinase (IRK) is composed of two extracellular a-subunits (135 kDa), which contain the insulin-binding site, and two intracellular b-subunits (95 kDa), containing the protein tyrosine kinase domain. After insulin binding, the insulin-IRK complex internalizes into muscle and fat cells. The IRK substrates of IRS-1 and IRS-2 form complexes, through Src homology region 2 (SH2) domains, with docking molecules such as phosphoinositde-3-kinase (PI3K). The recruitment of PI3K in turn activates phosphoinositide-dependent kinases, which serve in the activation of protein kinase B (Akt) and atypical isoforms of protein kinase C (PKC). These activated kinases then phosphorylate downstream effectors, ultimately promoting the translocation of insulin-sensitive glucose transporter subtype 4 (GLUT-4) to the plasma membrane, to operate in the coordination of glucose metabolism.
GenBank NM_000208
Specifications
Specifications
| Formulation | mg/mL of enzyme in 50 mM Tris/HCl pH 7.5, 150 mM NaCl, 0.1 mM EGTA, 0.03% Brij-35, 270 mM sucrose, 1 mM benzamidine, 0.2 mM PMSF, 0.1% 2-mercaptoethanol, 5 mM β-glycerophosphate, 1 mM Na3VO4. Frozen solution. |
| Molecular Weight (g/mol) | 36.8 kDa |
| Quantity | 10 μg |
| Species | Human |
| Recombinant | Recombinant |
| Protein Tag | N-terminal 6His |
| Expression System | Recombinant enzyme expressed in Sf21 insect cells |
| Protein Form | Truncated |
| Purity or Quality Grade | ≥79% |
| Protein | Insulin Receptor, activated |
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