Insulin Receptor β (L55B10) Mouse mAb #3020
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 95 |
| Source/Isotype | Mouse IgG1 |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For a carrier free (BSA and azide free) version of this product see product #60076.
For a carrier free (BSA and azide free) version of this product see product #60076.
Protocol
Specificity / Sensitivity
Insulin Receptor beta (L55B10) Mouse mAb detects endogenous levels of total insulin receptor β.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant human insulin receptor β carboxy-terminal fragments.
Background
Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).
- Adams, T.E. et al. (2000) Cell Mol Life Sci 57, 1050-93.
- Baserga, R. (2000) Oncogene 19, 5574-81.
- Scheidegger, K.J. et al. (2000) J Biol Chem 275, 38921-8.
- Hernández-Sánchez, C. et al. (1995) J Biol Chem 270, 29176-81.
- Lopaczynski, W. et al. (2000) Biochem Biophys Res Commun 279, 955-60.
- Baserga, R. (1999) Exp Cell Res 253, 1-6.
- White, M.F. et al. (1985) J Biol Chem 260, 9470-8.
- White, M.F. et al. (1988) J Biol Chem 263, 2969-80.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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