Date published: 2026-6-6

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SRPK2 Activators

Serine/Arginine-Rich Protein Specific Kinase 2 (SRPK2) activators encompass a range of chemicals that directly or indirectly enhance the kinase's activity. This kinase is integral to RNA splicing and various cellular processes, making its regulation significant in cellular signaling and homeostasis. Direct activators like ATP and magnesium ions are crucial for the enzymatic functionality of SRPK2, facilitating its kinase activity by aiding in substrate and ATP binding. Indirect activators, such as sodium orthovanadate and okadaic acid, function by inhibiting phosphatases, thereby maintaining the phosphorylation status of SRPK2 and its substrates.

The indirect activators of SRPK2 reveal the interconnectivity of cellular signaling pathways. Compounds like forskolin and EGF demonstrate how upstream signaling molecules can impact SRPK2 activity. Forskolin elevates cAMP levels, influencing numerous kinases and phosphatases, while EGF activates receptor tyrosine kinases, triggering cascades that can modulate SRPK2. Insulin and PMA highlight the role of major signaling pathways like PI3K/Akt and PKC in regulating SRPK2, either by direct phosphorylation or by altering the kinase's regulatory environment. Staurosporine and zinc ions illustrate the complexity of kinase regulation, where broad-spectrum effects on multiple kinases can indirectly affect SRPK2 activity.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

ADP

58-64-0sc-507362
5 g
$54.00
(0)

ATP acts as a substrate for SRPK2, facilitating its kinase activity. By binding to the ATP-binding site, it enables the transfer of a phosphate group to the serine/threonine residues of substrate proteins.

Sodium Orthovanadate

13721-39-6sc-3540
sc-3540B
sc-3540A
5 g
10 g
50 g
$49.00
$57.00
$187.00
142
(4)

As a phosphatase inhibitor, sodium orthovanadate indirectly upregulates SRPK2 activity by preventing dephosphorylation of the kinase and its substrates, thus maintaining its active state.

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 inhibits protein phosphatases PP1 and PP2A, indirectly maintaining the phosphorylation status and activation of SRPK2 and its downstream targets.

Forskolin

66575-29-9sc-3562
sc-3562A
sc-3562B
sc-3562C
sc-3562D
5 mg
50 mg
1 g
2 g
5 g
$78.00
$153.00
$740.00
$1413.00
$2091.00
73
(3)

Forskolin activates adenylate cyclase, increasing cAMP levels, which can indirectly influence SRPK2 activity by modulating cellular signaling pathways that affect SRPK2 phosphorylation status.

Insulin

11061-68-0sc-29062
sc-29062A
sc-29062B
100 mg
1 g
10 g
$156.00
$1248.00
$12508.00
82
(1)

Insulin signaling can indirectly affect SRPK2 activity through the PI3K/Akt pathway, influencing various kinases and phosphatases that modulate SRPK2's phosphorylation and activity.

Calyculin A

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

By inhibiting protein phosphatases, Calyculin A indirectly maintains the phosphorylated, active state of SRPK2 and its substrates, similar to okadaic acid.

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 can influence SRPK2 activity indirectly through downstream signaling cascades that modulate its phosphorylation status.

H-89 dihydrochloride

130964-39-5sc-3537
sc-3537A
1 mg
10 mg
$94.00
$186.00
71
(2)

H-89, primarily a PKA inhibitor, can indirectly affect SRPK2 activity through cAMP-dependent pathways, altering the kinase's activity by changing the cellular signaling environment.

Staurosporine

62996-74-1sc-3510
sc-3510A
sc-3510B
100 µg
1 mg
5 mg
$82.00
$153.00
$396.00
113
(4)

While known as a broad-spectrum kinase inhibitor, Staurosporine can also modulate kinase activity indirectly, including SRPK2, through complex signaling pathways.

Zinc

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

Zinc ions can modulate the activity of various kinases including SRPK2. They may influence the conformation and activity of the kinase indirectly by affecting its structural integrity.