Date published: 2026-2-22

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CCDC130 Activators

CCDC130 function through various mechanisms to increase its activity. Forskolin, by directly stimulating adenylyl cyclase, raises intracellular cAMP levels, which in turn activate protein kinase A (PKA). PKA is known to phosphorylate a myriad of proteins, and in the context of CCDC130, this activation is likely to lead to phosphorylation that enhances its activity. Similarly, IBMX also acts to elevate cAMP levels but does so by inhibiting phosphodiesterases, which are enzymes responsible for cAMP breakdown. The resultant high levels of cAMP contribute to sustaining PKA activity and, consequently, CCDC130 activation. PGE2 adds to this cAMP-mediated pathway by binding to its own receptors and triggering adenylyl cyclase, further supporting the cascade leading to PKA activation and subsequent action on CCDC130. Epinephrine adds to the list of activators through its interaction with beta-adrenergic receptors, which indirectly causes an increase in cAMP and activation of PKA that can target CCDC130.

Cholera toxin permanently activates adenylyl cyclase by ADP-ribosylation of the Gs alpha subunit, persistently increasing cAMP levels and PKA activity, which would lead to sustained phosphorylation and activation of CCDC130. PACAP, through its receptor, also activates adenylyl cyclase and consequently PKA, suggesting another route to CCDC130 activation. Anisomycin, through its ability to stimulate JNK, may influence CCDC130 activity by phosphorylating proteins that interact with or regulate CCDC130. Likewise, okadaic acid prevents dephosphorylation of proteins by inhibiting protein phosphatases PP1 and PP2A, possibly maintaining CCDC130 in an active state. Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which may phosphorylate CCDC130, leading to its activation. H-89, primarily known as a PKA inhibitor, can affect CCDC130 activity by inhibiting other kinases that may suppress CCDC130 when active. Calyculin A, similar to okadaic acid, inhibits protein phosphatases, potentially keeping CCDC130 phosphorylated and active. Lastly, zinc pyrithione modulates cellular pathways by increasing intracellular zinc levels, which can activate enzymes and transcription factors that may interact with or regulate CCDC130.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

IBMX

28822-58-4sc-201188
sc-201188B
sc-201188A
200 mg
500 mg
1 g
$260.00
$350.00
$500.00
34
(1)

Isobutylmethylxanthine (IBMX) inhibits phosphodiesterases, thus preventing the breakdown of cAMP. By maintaining high levels of cAMP, IBMX indirectly supports the activation of PKA, which may phosphorylate CCDC130 or interact with its regulatory components to enhance its activity.

PGE2

363-24-6sc-201225
sc-201225C
sc-201225A
sc-201225B
1 mg
5 mg
10 mg
50 mg
$57.00
$159.00
$275.00
$678.00
37
(1)

Prostaglandin E2 (PGE2) interacts with its G-protein-coupled receptors, leading to the activation of adenylyl cyclase and an increase in cAMP levels, which then activate PKA. Activated PKA might directly phosphorylate CCDC130 or modulate its function through phosphorylation of associated regulatory proteins.

(−)-Epinephrine

51-43-4sc-205674
sc-205674A
sc-205674B
sc-205674C
sc-205674D
1 g
5 g
10 g
100 g
1 kg
$41.00
$104.00
$201.00
$1774.00
$16500.00
(1)

Epinephrine binds to beta-adrenergic receptors, which are coupled to Gs proteins that activate adenylyl cyclase, resulting in increased cAMP and subsequent activation of PKA. PKA may then activate CCDC130 through direct phosphorylation or by phosphorylating related regulatory proteins.

PACAP(6-38)

137061-48-4sc-391136
sc-391136A
500 µg
1 mg
$540.00
$932.00
(0)

Pituitary adenylate cyclase-activating polypeptide (PACAP) binds to its GPCR, leading to the activation of adenylyl cyclase and increased cAMP production. The cAMP-dependent pathway involves PKA, which could phosphorylate and activate CCDC130.

Anisomycin

22862-76-6sc-3524
sc-3524A
5 mg
50 mg
$99.00
$259.00
36
(2)

Anisomycin activates JNK (c-Jun N-terminal kinase), which may phosphorylate substrates that interact with CCDC130, promoting its functional activation through post-translational modifications or changes in the interaction with other cellular components.

Okadaic Acid

78111-17-8sc-3513
sc-3513A
sc-3513B
25 µg
100 µg
1 mg
$291.00
$530.00
$1800.00
78
(4)

Okadaic acid is a potent inhibitor of protein phosphatases PP1 and PP2A, leading to increased phosphorylation levels of cellular proteins. By inhibiting the dephosphorylation, it could maintain CCDC130 in a phosphorylated, active state if CCDC130 is regulated by phosphorylation.

PMA

16561-29-8sc-3576
sc-3576A
sc-3576B
sc-3576C
sc-3576D
1 mg
5 mg
10 mg
25 mg
100 mg
$41.00
$132.00
$214.00
$500.00
$948.00
119
(6)

PMA activates protein kinase C (PKC), which is known to phosphorylate a wide range of cellular targets. If CCDC130 activity is regulated by phosphorylation, PKC activation could result in the phosphorylation and activation of CCDC130.

Calyculin A

101932-71-2sc-24000
sc-24000A
10 µg
100 µg
$163.00
$800.00
59
(3)

Calyculin A is an inhibitor of protein phosphatases like PP1 and PP2A. By preventing dephosphorylation, calyculin A could keep CCDC130 in a phosphorylated and activated state if CCDC130 is subject to regulation by phosphorylation.

Zinc

7440-66-6sc-213177
100 g
$48.00
(0)

Zinc pyrithione can modulate multiple cellular pathways through its ability to shuttle zinc ions into cells. Zinc is a critical cofactor for many enzymes and transcription factors. If CCDC130 requires zinc for its activity, or if zinc influences the activity of a kinase or phosphatase that regulates CCDC130, zinc pyrithione could lead to the activation of CCDC130.