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Fkbp51

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FKBP51 is a protein that belongs to the FK506-binding protein (FKBP) family. It functions as a co-chaperone, assisting in the folding and regulation of other proteins within the cell. FKBP51 plays a role in the regulation of steroid hormone receptors and is involved in cellular stress response pathways.

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Lab products found in correlation

Lamin b, by Cell Signaling Technology (2 mentions) Stard13, by Merck Group (1 mentions) Fkbp51, by Abcam (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Cytiva (1 mentions) Enhanced chemiluminescence, by Thermo Fisher Scientific (1 mentions) β actin, by Merck Group (1 mentions) Redd1 10638 1 ap, by Proteintech (1 mentions) Azd8055, by Merck Group (1 mentions) Gapdh g9545, by Merck Group (1 mentions) Nvp bez235, by Merck Group (1 mentions) Mk2206, by Merck Group (1 mentions) 5 bromo 2 deoxyuridine brdu, by Merck Group (1 mentions) Wortmannin, by Merck Group (1 mentions) Fluocinolone acetonide, by Merck Group (1 mentions) Phospho iκb ser32, by Santa Cruz Biotechnology (1 mentions) Phospho rps6, by Cell Signaling Technology (1 mentions) Phospho 4ebp1, by Cell Signaling Technology (1 mentions) Phospho p70s6k, by Cell Signaling Technology (1 mentions) Redd1, by Proteintech (1 mentions) Phospho rps6ser240 244, by Cell Signaling Technology (1 mentions)

4 protocols using fkbp51

1

Immunoprecipitation and Western Blotting

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Immunoprecipitation and Western blotting were performed as previously described.32 The following antibodies were used for immunoprecipitation: FKBP51 (sc‐271547; Santa Cruz Biotechnology), StARD13 (HPA035535; Sigma), and Halo (G9281; Promega). The following primary antibodies were used for immunoblotting: FKBP51 (ab126715; Abcam, Cambridge, UK and A301‐430A; Bethyl Laboratories, Inc., Montgomery, TX, USA), StARD13 (HPA035535; Sigma), Halo (G9281; Promega), and β‐actin (Sigma). Horseradish peroxidase‐conjugated secondary antibodies (Amersham Biosciences, Amersham, UK) were used to detect immunoreactive proteins by enhanced chemiluminescence (Thermo Scientific, Waltham, MA, USA).
Takaoka M., Ito S., Miki Y, & Nakanishi A. (2017). FKBP51 regulates cell motility and invasion via RhoA signaling. Cancer Science, 108(3), 380-389.
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2

Signaling Pathway Regulation in Cells

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Fluocinolone acetonide (FA), croton oil (CO), Wortmannin (WM), AZD8055 (AZD), NVP-BEZ235 (NVP), MK-2206 (MK), and 5-bromo-2′-deoxyuridine (BrdU), were from Sigma Aldrich (St. Louis, MO), LY294002 (LY) was from LC Laboratories (Woburn, MA). TNF-α and cytoplasmic and nuclear fractionation kit were from Thermo Fisher Scientific (Waltham, MA).
We used antibodies to GR (sc-8992, RRID:AB_2155784), RelA/p65 (sc-8008, RRID:AB_628017), phospho-RelA/p65 (Ser536) (sc-136548, RRID:AB_10610391), IκB (sc-1643, RRID:AB_627772), phospho-IκB (Ser32) (sc-8404, RRID:AB_627773), FKBP51 (sc-271547, RRID:AB_10649040) (Santa Cruz Biotechnology, Dallas, TX); GAPDH (G9545, RRID:AB_796208, Sigma Aldrich); phospho-GR (Ser211) (4161, RRID:AB_2155797), phospho-rpS6 (Ser235/236) (4856S, RRID:AB_2181037), phospho-4E-BP1 (Thr37/46) (9459L, RRID:AB_2262165), phospho-P70S6K (Thr389) (9234, RRID:AB_2269803), phospho-AKT (Thr308 and Ser473) (9266S, RRID:AB_659801 and 9271, RRID:AB_329825), lamin B (12586, RRID:AB_2650517) and tubulin (2148, RRID:AB_2288042) (Cell Signaling, San Jose, CA), REDD1 (10638-1-AP, RRID,AB_2245711, Proteintech Group, Rosemont, IL).
Agarwal S., Mirzoeva S., Readhead B., Dudley J.T, & Budunova I. (2019). PI3K inhibitors protect against glucocorticoid-induced skin atrophy. EBioMedicine, 41, 526-537.
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3

Western Blot Analysis of Protein Signaling

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Whole cell protein extracts were prepared as described [27 (link)]. Separate cytoplasmic and nuclear protein fractions were isolated with NE-PER Nuclear and Cytoplasmic Extraction Kit according to manufacturer protocol (ThermoFisher Scientific, Waltham, MA). The proteins were resolved by SDS-PAGE and transferred to nitrocellulose membranes (LI-COR Biosciences; Lincoln, NE). After blocking, membranes were incubated with primary antibodies overnight at 4°C, followed by IRDye® secondary antibodies (LI-COR Biosciences). LI-COR Odyssey Imager was used for the band visualization. The antibodies against FKBP51, GR, RelA/p65, p65Ser536 (Santa Cruz Biotechnology, Dallas, TX), Redd1 (Proteintech; Chicago, IL), phospho-GRSer211, Akt, phospho-AktSer473, phospho-rpS6Ser240/244, phospho-p70/S6KThr389, lamin B, tubulin (Cell Signaling, Danvers, MA), and GAPDH (Sigma, St Louis, MO) were used at concentrations recommended by their manufacturers. The multi-band pattern of FKBP51 signal on Western blots (Figure 1a) may reflect FKBP51 post-translational modifications such as phosphorylation [41 (link)].
ImageJ (http://rsb.info.nih.gov/ij/index.html) was used for densitometry. The intensity of bands was normalized to the corresponding loading control and expressed as fold of change vs vehicle-treated WT or Cas9-only control.
Baida G., Bhalla P., Yemelyanov A., Stechschulte L.A., Shou W., Readhead B., Dudley J.T., Sánchez E.R, & Budunova I. (2018). Deletion of the glucocorticoid receptor chaperone FKBP51 prevents glucocorticoid-induced skin atrophy. Oncotarget, 9(78), 34772-34783.
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4

Histological Analysis of Skin Samples

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Freshly excised dorsal skin pieces were immersed in 4% paraformaldehyde for 24 h and embedded in paraffin after dehydration through graded ethanol and xylene solutions. Sections were prepared at a thickness of 4 µm. Hematoxylin and eosin staining was performed for histological analysis. Immunohistochemical analysis was used to detect the numbers of cells labeled with TUNEL staining (Beyotime Biotechnology, China), and antibodies against Ki67 (Abcam, Cambridge, UK), 8-OHdG (JaICA, Japan), Tyr (Santa Cruz Biotechnology, Santa Cruz, CA, USA), Dct (LifeSpan BioSciences, Seattle, WA, USA), Fkbp51 (Santa Cruz Biotechnology), NF-κB p65 and Bcl-2 (Cell Signaling Technology, Danvers, MA, USA) were used to detect the expression of these proteins. Images were captured using a biological microscope (DM40008, Leica, Germany). The numbers of hyperchromatic cells and the numbers of positively stained cells were counted per unit area. Cell counts and quantitation of western blotting data were performed using ImageJ software.
Wang P., Hu G., Zhao W., Du J., You M., Xv M., Yang H., Zhang M., Yan F., Huang M., Wang X., Zhang L., & Chen Y. (2021). Continuous ZnO nanoparticle exposure induces melanoma-like skin lesions in epidermal barrier dysfunction model mice through anti-apoptotic effects mediated by the oxidative stress–activated NF-κB pathway.
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