Date published: 2025-10-25

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UNCL Inhibitors

Chemical inhibitors of UNCL can modulate the protein's activity through a variety of molecular interactions and pathways. Bromocriptine, a dopamine agonist, reduces the activity of UNCL by activating dopamine receptors that lead to decreased levels of intracellular cAMP. This reduction in cAMP levels diminishes the activity of protein kinase A, which is responsible for the phosphorylation and regulation of proteins including UNCL. This results in a lower functional activity of UNCL. Similarly, the action of rapamycin involves binding to FKBP12, and the resulting complex inhibits the mTOR pathway. This inhibition suppresses protein synthesis including potentially those proteins that interact with or constitute UNCL, thus decreasing UNCL's functional availability.

Other inhibitors like Wortmannin and LY294002, both target phosphoinositide 3-kinases, leading to downstream effects that can reduce the functional activity of UNCL. By preventing the activation of Akt, a kinase involved in cell survival and protein synthesis, these inhibitors can decrease the phosphorylation and activation of proteins that interact with UNCL. Trichostatin A, on the other hand, changes gene expression patterns by inhibiting histone deacetylase, which can indirectly affect the activity of proteins such as UNCL. Staurosporine broadly inhibits protein kinases, potentially affecting the phosphorylation state of UNCL or its regulatory proteins, thereby reducing UNCL activity. Inhibitors of signaling pathways such as U0126 and PD98059, which target MEK, and SB203580, which inhibits p38 MAP kinase, can decrease the phosphorylation and subsequent activation of proteins that regulate the function of UNCL. Similarly, SP600125's inhibition of JNK alters signaling that may involve UNCL, leading to decreased function of the protein. Lastly, PP2 targets Src family kinases, which are involved in complex signaling cascades that can influence the activity of proteins such as UNCL. By disrupting these pathways, these inhibitors can lead to a reduction in UNCL's functional activity.

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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Bromocriptine

25614-03-3sc-337602A
sc-337602B
sc-337602
10 mg
100 mg
1 g
$56.00
$260.00
$556.00
4
(1)

Bromocriptine, a dopamine agonist, inhibits the protein UNCL by activating dopamine receptors which can lead to decreased intracellular cAMP levels. Lower cAMP levels reduce the activity of protein kinase A (PKA), which is known to phosphorylate proteins like UNCL, thereby reducing its functional activity.

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 the complex inhibits mTOR (mammalian target of rapamycin). mTOR is a key kinase that regulates protein synthesis and cell growth. Inhibition of mTOR can decrease the translation of a subset of mRNAs, potentially including those that code for UNCL, thus functionally inhibiting the protein through reduced synthesis.

Wortmannin

19545-26-7sc-3505
sc-3505A
sc-3505B
1 mg
5 mg
20 mg
$66.00
$219.00
$417.00
97
(3)

Wortmannin is an inhibitor of phosphoinositide 3-kinases (PI3K). By inhibiting PI3K, it prevents the phosphorylation and activation of downstream effectors such as Akt. Since Akt can modulate protein synthesis and cellular survival pathways that may involve UNCL, inhibiting Akt through PI3K inhibition can lead to decreased functional activity of UNCL.

LY 294002

154447-36-6sc-201426
sc-201426A
5 mg
25 mg
$121.00
$392.00
148
(1)

LY294002 is another PI3K inhibitor, working similarly to Wortmannin. By preventing PI3K from activating Akt, it can indirectly lead to reduced phosphorylation and activation of proteins that may interact with or regulate UNCL, thus inhibiting UNCL function.

Trichostatin A

58880-19-6sc-3511
sc-3511A
sc-3511B
sc-3511C
sc-3511D
1 mg
5 mg
10 mg
25 mg
50 mg
$149.00
$470.00
$620.00
$1199.00
$2090.00
33
(3)

Trichostatin A is a histone deacetylase inhibitor. By altering the acetylation status of histones, it can change the expression of genes and the activity of proteins involved in cell cycle and survival. These changes can affect multiple proteins, potentially including UNCL, thereby reducing its activity through changes in the cellular environment.

Staurosporine

62996-74-1sc-3510
sc-3510A
sc-3510B
100 µg
1 mg
5 mg
$82.00
$150.00
$388.00
113
(4)

Staurosporine is a potent inhibitor of protein kinases. It inhibits a wide range of kinases, which could lead to decreased phosphorylation of UNCL or its regulatory proteins, thus inhibiting UNCL's function.

U-0126

109511-58-2sc-222395
sc-222395A
1 mg
5 mg
$63.00
$241.00
136
(2)

U0126 is an inhibitor of MEK, which is upstream of the ERK pathway. ERK is often involved in the regulation of protein functions and their interactions. By inhibiting MEK, U0126 can decrease the activation of ERK and potentially reduce the phosphorylation and activity of proteins that are involved in the same pathway as UNCL or that regulate UNCL, leading to its functional inhibition.

SB 203580

152121-47-6sc-3533
sc-3533A
1 mg
5 mg
$88.00
$342.00
284
(5)

SB203580 is an inhibitor of p38 MAP kinase. The p38 MAPK pathway is involved in stress responses and apoptosis. Inhibition of p38 MAPK can affect the phosphorylation state and activity of various proteins that could interact with or regulate UNCL, resulting in an inhibition of UNCL's function.

PD 98059

167869-21-8sc-3532
sc-3532A
1 mg
5 mg
$39.00
$90.00
212
(2)

PD98059 is an inhibitor of MEK, which is part of the MAPK/ERK pathway. By inhibiting MEK, PD98059 can prevent the activation of ERK, which in turn can lead to decreased regulation of proteins that interact with or control the activity of UNCL, inhibiting its function.

SP600125

129-56-6sc-200635
sc-200635A
10 mg
50 mg
$40.00
$150.00
257
(3)

SP600125 is an inhibitor of the c-Jun N-terminal kinase (JNK). JNK is implicated in the control of a number of cellular processes, including cell growth and apoptosis. Inhibition of JNK could affect signaling pathways that regulate or involve UNCL, leading to its functional inhibition.