Date published: 2026-5-30

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p-Thr Activators

Common p-Thr Activators include, but are not limited to Insulin CAS 11061-68-0, PMA CAS 16561-29-8, Forskolin CAS 66575-29-9, Okadaic Acid CAS 78111-17-8 and Anisomycin CAS 22862-76-6.

Phosphorylation is a vital post-translational modification in which a phosphate group is added to an amino acid residue of a protein, predominantly on serine, threonine (Thr), or tyrosine residues. The addition of this phosphate group can modulate the activity, localization, or interaction capabilities of the targeted protein. When threonine residues, in particular, undergo phosphorylation (resulting in the p-Thr designation), it can have profound implications for cellular signaling pathways and the regulation of various cellular processes. Kinases are the enzymes responsible for this phosphorylation, and their activity is counterbalanced by phosphatases, which can remove the phosphate group. The interplay between kinases and phosphatases ensures the precise modulation of protein function, with p-Thr serving as a dynamic marker of this regulatory process.

Activators of p-Thr are molecules or compounds that promote the phosphorylation of threonine residues on target proteins. These activators can function by either enhancing the activity of specific kinases, inhibiting the activity of phosphatases, or stabilizing the phosphorylated state of the protein. The presence of p-Thr activators can amplify specific cellular signaling events, influencing a myriad of processes ranging from gene expression and metabolism to cell cycle progression and apoptosis. Delving into the intricacies of p-Thr activators provides a window into the dynamic world of protein phosphorylation and its pivotal role in orchestrating cellular responses. As the scientific community continues to explore the vast landscape of cellular regulation, the significance of threonine phosphorylation and its activators is underscored, reflecting the complexity and precision of molecular signaling events.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Insulin

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

Insulin activates the insulin receptor, leading to activation of several downstream kinases that can phosphorylate threonine residues.

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 phosphorylate proteins on threonine residues.

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 adenylyl cyclase leading to cAMP production, which can activate PKA, a kinase that phosphorylates threonine residues.

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, leading to increased levels of phosphorylated proteins, including threonine residues.

Anisomycin

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

Anisomycin activates the MAPK pathway, leading to activation of downstream kinases that can phosphorylate proteins, including on threonine residues.

Ionomycin, free acid

56092-81-0sc-263405
sc-263405A
1 mg
5 mg
$96.00
$264.00
2
(2)

Ionomycin increases intracellular calcium, which can activate calcium-dependent kinases, leading to threonine phosphorylation.

Calyculin A

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

Similar to okadaic acid, calyculin A inhibits protein phosphatases, leading to increased levels of phosphorylated proteins.

Cycloheximide

66-81-9sc-3508B
sc-3508
sc-3508A
100 mg
1 g
5 g
$41.00
$84.00
$275.00
127
(6)

Known to activate the JNK pathway, which can result in increased threonine phosphorylation of target proteins.

Staurosporine

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

A broad-spectrum kinase inhibitor that, paradoxically, can lead to changes in phosphorylation patterns, including threonine residues, due to its effects on various kinases.