Date published: 2026-5-30

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SLA Activators

SLA Activators encompasses a variety of chemical agents that indirectly modulate the activity of the Src-like-adaptor protein (SLA). These activators function by perturbing the phosphorylation state of SLA or by influencing the cellular signaling pathways to which SLA is a contributory component. This group,such as PP2, which target Src family kinases, maintaining the phosphorylation status necessary for the active conformation of SLA. Similarly, sodium stibogluconate works by inhibiting tyrosine phosphatases, thereby preserving the phosphorylated form of SLA, which is essential for its activity as an adapter in signaling processes. Agents like forskolin and isoproterenol function by increasing intracellular cAMP levels, consequently modulating protein kinase A (PKA) activity that can phosphorylate proteins within the T-cell receptor (TCR) signaling pathway, affecting the adapter role of SLA. Phorbol esters such as PMA directly activate protein kinase C (PKC), leading to the phosphorylation of proteins within the TCR pathway and influencing SLA's interaction with its associated signaling molecules.

Further in the class are compounds like ionomycin, which elevates intracellular calcium levels, thereby activating kinases such as calcineurin that can change the activation state of proteins in the TCR signaling pathway, impacting SLA's function. Piceatannol and dasatinib alter the phosphorylation landscape of the B-cell receptor (BCR) and other pathways by targeting Syk kinase and a spectrum of tyrosine kinases, respectively. Inhibition of ZAP-70 kinase, for which no specific CAS number is provided, could result in enhanced activity of SLA by allowing it to remain phosphorylated and active. LY294002 and U0126 intervene in the PI3K/Akt and ERK pathways, respectively, pathways downstream of TCR signaling, which could, in turn, modulate the role of SLA. Lastly, prostratin activates PKC, which can lead to modifications in the phosphorylation states of signaling proteins, altering how SLA functions within these pathways.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Sodium stibogluconate

16037-91-5sc-202815
1 g
$188.00
6
(2)

This compound can increase the phosphorylated state of SLA by inhibiting tyrosine phosphatases, thus potentially enhancing SLA's interaction with other signaling proteins.

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 raises cAMP levels, which can modulate protein kinase A (PKA) activity. PKA can phosphorylate proteins in the TCR signaling pathway, potentially affecting SLA's role in this pathway.

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)

As an activator of PKC, PMA can promote the phosphorylation of proteins within the TCR pathway, thereby influencing the adapter function of SLA.

Ionomycin, free acid

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

Ionomycin increases intracellular calcium, activating kinases like calcineurin that can alter the activation state of proteins in the TCR signaling pathway, impacting SLA's function.

Isoproterenol Hydrochloride

51-30-9sc-202188
sc-202188A
100 mg
500 mg
$28.00
$38.00
5
(0)

By raising cAMP levels, isoproterenol can affect PKA activity. PKA can then phosphorylate components of the TCR pathway, which could alter SLA's adapter functions.

Piceatannol

10083-24-6sc-200610
sc-200610A
sc-200610B
1 mg
5 mg
25 mg
$51.00
$71.00
$199.00
11
(2)

Inhibiting Syk kinase could modify the phosphorylation landscape of the BCR signaling pathway, which may change how SLA interacts with its partners in the pathway.

LY 294002

154447-36-6sc-201426
sc-201426A
5 mg
25 mg
$123.00
$400.00
148
(1)

By inhibiting PI3K, LY294002 can affect downstream signaling pathways, such as Akt, which could impact the role of SLA in the TCR signaling pathway.

Prostratin

60857-08-1sc-203422
sc-203422A
1 mg
5 mg
$141.00
$541.00
24
(2)

Activation of PKC by prostratin can lead to changes in the phosphorylation states of signaling proteins, potentially altering how SLA functions within these pathways.