Date published: 2025-12-13

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FKBP14 Inhibitors

FKBP14 inhibitors belong to a class of compounds that interact with and inhibit the function of the protein FKBP14, which is encoded by the FKBP14 gene. FKBP14, a member of the immunophilin protein family, is known for its peptidyl-prolyl cis-trans isomerase (PPIase) activity, which plays a critical role in the folding of proteins, particularly those with proline residues. The inhibitors of FKBP14 are designed to specifically bind to the active site or allosteric sites of the protein, thereby preventing its interaction with target polypeptides. This inhibition can have a profound impact on various cellular processes, including protein folding and trafficking, as well as the modulation of signaling pathways that are vital for cell survival, differentiation, and metabolism. FKBP14 inhibitors often exploit the conserved nature of the PPIase domain to achieve selectivity and high-affinity binding, which makes them particularly effective in exerting their inhibitory action. The inhibition of FKBP14 by these chemical agents can lead to the disruption of normal cellular homeostasis since FKBP14 is involved in the proper folding and functioning of several proteins within the endoplasmic reticulum. By blocking the PPIase activity of FKBP14, these inhibitors can induce a stress response within the cell due to the accumulation of misfolded proteins, which in turn can activate cellular pathways like the unfolded protein response (UPR). This response is a complex cellular mechanism that aims to restore homeostasis but can lead to cell cycle arrest or apoptosis if the protein misfolding is extensive and cannot be resolved. The specificity of FKBP14 inhibitors allows for a targeted approach in studying the physiological roles of FKBP14 and the pathways it influences. These compounds are useful tools in biomedical research, providing insights into the fundamental cellular processes that FKBP14 regulates and offering a means to dissect the protein's role in various biological contexts.

Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Rapamycin

53123-88-9sc-3504
sc-3504A
sc-3504B
1 mg
5 mg
25 mg
$62.00
$155.00
$320.00
233
(4)

Rapamycin binds to FKBP12 and inhibits mTOR pathway. As the FKBP14 protein shares high homology with FKBP12, rapamycin could indirectly inhibit FKBP14's peptidyl-prolyl isomerase activity due to competitive binding.

Cyclosporin A

59865-13-3sc-3503
sc-3503-CW
sc-3503A
sc-3503B
sc-3503C
sc-3503D
100 mg
100 mg
500 mg
10 g
25 g
100 g
$62.00
$90.00
$299.00
$475.00
$1015.00
$2099.00
69
(5)

Cyclosporin A inhibits calcineurin by binding to cyclophilins. As FKBP14 is a member of the immunophilin protein family, which includes cyclophilins, it's likely that Cyclosporin A might also bind to FKBP14, thereby inhibiting its activity.

Pioglitazone

111025-46-8sc-202289
sc-202289A
1 mg
5 mg
$54.00
$123.00
13
(1)

Pioglitazone, a PPAR-gamma agonist, alters the mitochondrial function and may affect proteins involved in mitochondrial-associated pathways, including FKBP14, by altering the protein folding environment.

Geldanamycin

30562-34-6sc-200617B
sc-200617C
sc-200617
sc-200617A
100 µg
500 µg
1 mg
5 mg
$38.00
$58.00
$102.00
$202.00
8
(1)

Geldanamycin binds to Hsp90, inhibiting its chaperone function. As FKBP14 is a chaperone that assists in protein folding, the inhibition of Hsp90 could disrupt the protein folding process, indirectly affecting FKBP14's function.

Tunicamycin

11089-65-9sc-3506A
sc-3506
5 mg
10 mg
$169.00
$299.00
66
(3)

Tautomycin is a PP1 and PP2A phosphatase inhibitor, and since phosphatase activity affects numerous signaling pathways, FKBP14's role in protein folding and cellular signaling could be indirectly inhibited by the disruption of phosphatase function.

MG-132 [Z-Leu- Leu-Leu-CHO]

133407-82-6sc-201270
sc-201270A
sc-201270B
5 mg
25 mg
100 mg
$56.00
$260.00
$980.00
163
(3)

MG132 is a proteasome inhibitor that could increase the levels of misfolded proteins, indirectly affecting FKBP14's role in proteostasis by overwhelming the protein folding machinery that FKBP14 is a part of.

Mitomycin C

50-07-7sc-3514A
sc-3514
sc-3514B
2 mg
5 mg
10 mg
$65.00
$99.00
$140.00
85
(5)

Mitomycin C is a DNA crosslinker that triggers the DNA damage response. FKBP14's potential involvement in cellular stress responses could be indirectly inhibited by the activation of DNA damage pathways and the resulting cellular arrest.

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$30.00
$52.00
$122.00
$367.00
25
(3)

Brefeldin A disrupts ER to Golgi transport. FKBP14, being localized to the ER, might have its function affected by the disruption in trafficking and protein processing within the ER.

Thapsigargin

67526-95-8sc-24017
sc-24017A
1 mg
5 mg
$94.00
$349.00
114
(2)

Thapsigargin is a non-competitive inhibitor of the SERCA pump, leading to ER stress. FKBP14's chaperone activity within the ER might be indirectly inhibited by the ER stress and unfolded protein response initiated by thapsigargin.

Curcumin

458-37-7sc-200509
sc-200509A
sc-200509B
sc-200509C
sc-200509D
sc-200509F
sc-200509E
1 g
5 g
25 g
100 g
250 g
1 kg
2.5 kg
$36.00
$68.00
$107.00
$214.00
$234.00
$862.00
$1968.00
47
(1)

Curcumin has been shown to disrupt multiple cellular signaling pathways including the inhibition of transcription factors and kinases. This broad-spectrum activity could indirectly affect FKBP14's role in cellular signaling and protein folding.