Learn More
Description
Transforming growth factor-β binds to the TGFβ family of heteromeric serine/threonine transmembrane receptors (type I and type II). Following binding of TGFβ, the type II receptor (TβR-II) phosphorylates the type I receptor (TβR-I) which, in turn, conveys the signal. Since TβR-I and TβR-II can interact without the stimulation of TGFβ, leading to unwanted activation, a regulatory mechanism exists. In a yeast genetic screen, immunophilin FKBP12 was associated with the type I receptor. Studies including co-immunoprecipiation, deletion, and point mutations confirmed this interaction. FKBP12 inhibits TβR-II mediated phosphorylation of TβR-I, inhibiting activation. FKBP12 binds via its rapamycin/Leu-Pro binding pocket to the Leu-Pro sequence adjacent to the phosphorylation site of TβR-I. This interaction is blocked by
the addition of macrolides, rapamycin, and FK506. Furthermore, mutations in the binding sites of FKBP12 and TβR-I abrogates the binding and results in activation of the receptor without the addition of TGFβ. Thus, FKBP12 is a regulatory protein for TβR-I and TβR-II-mediated signaling.
Immunofluorescence, Immunoprecipitation, Western Blotting
Specifications
Specifications
| Antigen | FKBP12 |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 8 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Description | FK506 Binding Protein 1A |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Human FKBP12 aa. 1-108 |
| Show More |
Safety and Handling
By clicking Submit, you acknowledge that you may be contacted by Fisher Scientific in regards to the feedback you have provided in this form. We will not share your information for any other purposes. All contact information provided shall also be maintained in accordance with our Privacy Policy.