Date published: 2026-2-26

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ARRDC5 Activators

Chemical activators of arrestin domain containing 5 leverage various cellular mechanisms to modulate the protein's activity. Forskolin works by directly stimulating adenylate cyclase, thereby enhancing the production of cyclic AMP (cAMP). This increase in cAMP levels subsequently activates protein kinase A (PKA), which in turn can phosphorylate arrestin domain containing 5, leading to its activation. Similarly, IBMX acts to elevate cAMP levels by inhibiting the action of phosphodiesterases, which normally break down cAMP. The resultant high levels of cAMP further promote PKA activity and the subsequent phosphorylation of arrestin domain containing 5. PMA, on the other hand, activates protein kinase C (PKC), a kinase that can also phosphorylate arrestin domain containing 5, altering its activity. Additionally, Calyculin A and Okadaic Acid, inhibitors of protein phosphatases 1 and 2A, prevent the dephosphorylation of proteins, which can result in sustained or enhanced phosphorylation and consequent activation of arrestin domain containing 5.

Further contributing to the regulation of arrestin domain containing 5 are chemicals that affect signaling pathways through different mechanisms. Zinc Chloride can influence the activity of various kinases and phosphatases, potentially leading to the phosphorylation of arrestin domain containing 5. Epigallocatechin Gallate (EGCG) interacts with these enzymes as well, possibly enhancing the phosphorylation state of arrestin domain containing 5. Sphingosine-1-Phosphate activates its receptors and can initiate downstream signaling that may culminate in the activation of arrestin domain containing 5 through phosphorylation events. Anisomycin, through its action on stress-activated protein kinases, and Phosphatidic Acid, through its role in activating the mTOR signaling pathway, can contribute to the phosphorylation and activation of arrestin domain containing 5. Lastly, Oleic Acid can alter membrane fluidity and the activity of membrane-associated proteins, potentially initiating signaling cascades that result in the phosphorylation and activation of arrestin domain containing 5. Each of these chemicals, through distinct molecular interactions, can lead to the activation of arrestin domain containing 5 by influencing its phosphorylation status.

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Items 1 to 10 of 11 total

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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, which prevents the breakdown of cAMP. Elevated levels of cAMP can enhance PKA activity, which may phosphorylate and activate arrestin domain containing 5, thus promoting its role in cellular processes.

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)

Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which can phosphorylate and influence the function of many proteins. PKC-mediated phosphorylation can lead to the activation of arrestin domain containing 5 by altering its conformation or its interactions with other signaling molecules.

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 phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), which prevents dephosphorylation of proteins. Inhibition of these phosphatases can result in increased phosphorylation levels of proteins, including arrestin domain containing 5, thus potentially leading to its activation.

Okadaic Acid

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

Similar to Calyculin A, Okadaic Acid inhibits protein phosphatases PP1 and PP2A, leading to an accumulation of phosphorylated proteins. This could enhance the phosphorylation state of arrestin domain containing 5, thereby activating it.

Zinc

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

Zinc ions can act as a second messenger in various signaling pathways. Zinc Chloride specifically could alter the activity of phosphatases and kinases, which might result in the phosphorylation and subsequent activation of arrestin domain containing 5.

(−)-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
$43.00
$73.00
$126.00
$243.00
$530.00
$1259.00
11
(1)

Epigallocatechin Gallate (EGCG) is known to influence various signaling pathways, including those involving kinases and phosphatases. By altering the activity of these enzymes, EGCG could promote the phosphorylation and activation of arrestin domain containing 5.

D-erythro-Sphingosine-1-phosphate

26993-30-6sc-201383
sc-201383D
sc-201383A
sc-201383B
sc-201383C
1 mg
2 mg
5 mg
10 mg
25 mg
$165.00
$322.00
$570.00
$907.00
$1727.00
7
(1)

Sphingosine-1-Phosphate (S1P) is a bioactive lipid that activates S1P receptors and can trigger downstream signaling cascades involving MAPK and PI3K pathways, which might lead to phosphorylation and activation of arrestin domain containing 5.

Anisomycin

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

Anisomycin is an inhibitor of protein synthesis but also activates stress-activated protein kinases such as JNK. Activation of these kinases can lead to phosphorylation cascades that may include arrestin domain containing 5, resulting in its activation.

Chelerythrine chloride

3895-92-9sc-3547
sc-3547A
5 mg
25 mg
$90.00
$317.00
17
(1)

Chelerythrine is a potent inhibitor of PKC; however, it can cause transient activation of the kinase before inhibition. This transient activation could theoretically phosphorylate and activate arrestin domain containing 5.

Phosphatidic Acid, Dipalmitoyl

169051-60-9sc-201057
sc-201057B
sc-201057A
100 mg
250 mg
500 mg
$106.00
$244.00
$417.00
(1)

Phosphatidic Acid can act as a lipid second messenger and has been shown to activate mTOR signaling pathway. Activation of mTOR could lead to phosphorylation events that include arrestin domain containing 5, leading to its activation.