Date published: 2025-12-8

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scc-112 Activators

Activators of scc-112 function by engaging various cellular mechanisms to enhance its role in the cohesin complex, which is crucial for sister chromatid cohesion and proper chromosome segregation during cell division. These compounds primarily exert their effects through modulation of signaling pathways that affect the phosphorylation states within the cell. For instance, some activators work by increasing intracellular levels of secondary messengers such as cAMP, which subsequently activates protein kinase A (PKA). PKA then phosphorylates target proteins that may include those directly interacting with scc-112, thereby strengthening its association with chromatin and enhancing its activity. Other activators may inhibit protein phosphatases, leading to an overall increase in phosphorylation, which can indirectly benefit the function of scc-112 by maintaining or promoting its active state within the cohesin complex, ensuring accurate chromatid cohesion.

In addition to influencing phosphorylation cascades, some scc-112 activators interact with the wider regulatory network of cellular signaling by modifying the activity of kinases and phosphatases that are not directly involved with scc-112 but impact its function. Compounds that inhibit protein kinase C (PKC) can shift cellular signaling towards other pathways that favor scc-112 activation, such as those that might involve PKA or other kinases that scc-112 potentially interacts with. Similarly, inhibitors of key signaling pathways, like the MAPK/ERK and PI3K/AKT pathways, can cause a reconfiguration of cellular phosphorylation patterns that indirectly enhance scc-112's role in maintaining sister chromatid cohesion. Furthermore, changes in calcium signaling, either through disruption of homeostasis or by direct elevation of intracellular calcium levels, could also affect scc-112 activity. This is because such fluctuations can activate calcium-dependent signaling cascades that may intersect with the pathways regulating scc-112 function. Additionally, some activators indirectly promote an open chromatin state, either by inhibiting DNA methyltransferases or histone deacetylases, potentially increasing the accessibility of scc-112 to its chromosomal targets and facilitating its engagement with the cohesin complex.

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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Forskolin

66575-29-9sc-3562
sc-3562A
sc-3562B
sc-3562C
sc-3562D
5 mg
50 mg
1 g
2 g
5 g
$76.00
$150.00
$725.00
$1385.00
$2050.00
73
(3)

This diterpene acts by directly stimulating adenylate cyclase, thereby increasing cyclic AMP (cAMP) levels in cells. Elevated cAMP activates PKA (protein kinase A), which can phosphorylate various targets that could enhance the chromatid cohesion function of scc-112 by facilitating its association with chromatin.

8-Bromo-cAMP

76939-46-3sc-201564
sc-201564A
10 mg
50 mg
$97.00
$224.00
30
(1)

A cell-permeable cAMP analog that resists degradation by phosphodiesterases, thus mimicking the action of endogenous cAMP. This compound would activate PKA, potentially promoting phosphorylation events that strengthen the function of scc-112 in maintaining sister chromatid cohesion.

Bisindolylmaleimide I (GF 109203X)

133052-90-1sc-24003A
sc-24003
1 mg
5 mg
$103.00
$237.00
36
(1)

This compound is a potent and specific inhibitor of PKC (protein kinase C). By inhibiting PKC, it can shift the equilibrium towards other signaling pathways such as PKA, which may indirectly enhance the functional activity of scc-112 in its role of chromatid segregation during cell division.

Okadaic Acid

78111-17-8sc-3513
sc-3513A
sc-3513B
25 µg
100 µg
1 mg
$285.00
$520.00
$1300.00
78
(4)

A potent inhibitor of protein phosphatases PP1 and PP2A, leading to increased phosphorylation levels within the cell. This may indirectly promote the phosphorylation state of proteins associated with scc-112, potentiating its role in cohesin complex function.

(−)-Epigallocatechin Gallate

989-51-5sc-200802
sc-200802A
sc-200802B
sc-200802C
sc-200802D
sc-200802E
10 mg
50 mg
100 mg
500 mg
1 g
10 g
$42.00
$72.00
$124.00
$238.00
$520.00
$1234.00
11
(1)

A polyphenol found in green tea that has been shown to inhibit DNA methyltransferases. This could lead to changes in chromatin structure, potentially enhancing the accessibility of scc-112 to its sites of action during the cell cycle.

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)

An inhibitor of histone deacetylases (HDACs) which leads to hyperacetylation of histones, generally associated with open chromatin and active transcription. This could indirectly facilitate scc-112 function by promoting a chromatin environment amenable to its cohesin-related activities.

PD 98059

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

A selective inhibitor of MEK, which blocks the activation of MAPK/ERK pathway. This inhibition could lead to alterations in phosphorylation patterns that indirectly enhance the role of scc-112 in chromosome cohesion and segregation.

LY 294002

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

A selective inhibitor of PI3K, which alters the AKT signaling pathway. This modulation could affect a variety of downstream cellular processes, possibly including those that scc-112 is involved in, such as the maintenance of sister chromatid cohesion.

Thapsigargin

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

A sesquiterpene lactone that disrupts calcium homeostasis by inhibiting the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). Altered calcium signaling could have downstream effects on cellular pathways influencing scc-112 activity in cohesin complex stabilization.

Ionomycin

56092-82-1sc-3592
sc-3592A
1 mg
5 mg
$76.00
$265.00
80
(4)

A calcium ionophore that increases intracellular calcium levels, which could activate calcium-dependent signaling pathways, potentially impacting the phosphorylation status and function of scc-112 in cohesin complex dynamics.