R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
IGF-I Receptor β (D4O6W) Rabbit mAb #14534
Filter:
- WB
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 95, 200 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| IHC Leica Bond | 1:50 - 1:200 |
| Immunohistochemistry (Paraffin) | 1:400 |
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.
Protocol
Specificity / Sensitivity
IGF-I Receptor β (D4O6W) Rabbit mAb recognizes endogenous levels of total IGF-I receptor β protein, which includes both unprocessed and processed forms of the protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to human IGF-I receptor β protein.
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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