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If you encounter problems while ordering, please contact us at BDBCustomerService@bd.com
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.If you encounter problems while ordering, please contact us at BDBCustomerService@bd.com
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Western blot analysis of FKBP12 on a SW-13 cell lysate (Human adrenal gland carcinoma; ATCC CCL-105). Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-FKBP12 antibody.
Western blot analysis of FKBP12 on a SW-13 cell lysate (Human adrenal gland carcinoma; ATCC CCL-105). Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-FKBP12 antibody.
Immunofluorescence staining of HS 766T cells (Human pancreatic carcinoma; ATCC HTB-134).
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Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
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.
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