PathScan® Phospho-Insulin Receptor β (panTyr) Sandwich ELISA Kit #7082
Filter:
- ELISA
Supporting Data
| REACTIVITY | H |
Application Key:
- ELISA-ELISA
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
The PathScan® Phospho-Insulin Receptor β (panTyr) Sandwich ELISA Kit from Cell Signaling Technology is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects transfected levels of tyrosine-phosphorylated insulin receptor β protein. An Insulin Receptor β Rabbit mAb has been coated on the microwells. After incubation with cell lysates, Insulin receptor β protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a phospho-tyrosine mouse mAb is added to detect captured tyrosine-phosphorylated insulin receptor β protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of insulin receptor β protein phosphorylated on tyrosine.
*Antibodies in this kit are custom formulations specific to kit.
*Antibodies in this kit are custom formulations specific to kit.
Protocol
Specificity / Sensitivity
PathScan® Phospho-Insulin Receptor β (panTyr) Sandwich ELISA Kit #7082 detects transfected levels of human Insulin Receptor β protein phosphorylated at tyrosine, as shown in Figure 1. The kit sensitivity is shown in Figure 2. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity:
Human
Background
Insulin receptor (INSR) is a membrane receptor tyrosine kinase. The receptor molecule consists of a disulfide linked heterodimer. The α subunit is a 135 kDa extracellular fragment, and the β subunit is a 95 kDa fragment containing an extracellular domain, a single transmembrane domain, and an intracellular tyrosine kinase domain (1). Insulin ligand binding to this receptor results in receptor autophosphorylation and tyrosine kinase activation. INSR catalyzes the tyrosine phosphorylation of molecules such as IRS, Gab1, Shc, and Cbl, which further activate the downstream MAPK, PI3K, and TC10 pathways. This eventually leads to increases in glucose uptake and metabolism as well as cell growth (2,3). INSR has peptide substrate specificity similar to other receptor tyrosine kinase members, preferring acidic residues at the -1 to -4 positions and large hydrophobic amino acids at positions +1 and +3 (4).
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