Date published: 2026-5-30

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SSH2 Inhibitors

SSH2 (Slingshot-2) is an enzyme that plays a pivotal role in the regulation of actin dynamics within the cellular environment. Actin, a key component of the cell's cytoskeleton, undergoes dynamic reorganization, which is crucial for numerous cellular processes such as cell migration, division, and signaling. SSH2 is involved in dephosphorylating and hence activating another protein called cofilin, which subsequently facilitates the disassembly of actin filaments. Given the significant role of actin dynamics in cellular functions, modulating the activity of SSH2 has garnered interest among researchers, leading to the exploration and characterization of SSH2 inhibitors.

The chemical class of SSH2 inhibitors comprises molecules that can inhibit or reduce the activity of the SSH2 enzyme. These inhibitors may act by different mechanisms such as interfering with the active site of the enzyme, disrupting its conformation, or impeding its interaction with other essential proteins. Structure-activity relationship (SAR) studies have been instrumental in providing insights into the specific chemical features necessary for potent inhibition. The chemical diversity of this class of compounds has expanded over time, encompassing a variety of scaffolds and functional groups. High-throughput screening, molecular docking, and in silico modeling have further facilitated the discovery and optimization of potent SSH2 inhibitors. As our understanding of the biochemistry and structure of SSH2 continues to grow, the refinement of these inhibitors will be essential in ensuring their specificity and minimizing off-target effects.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

PP 2

172889-27-9sc-202769
sc-202769A
1 mg
5 mg
$94.00
$227.00
30
(1)

PP2 selectively inhibits Src family tyrosine kinases by targeting the ATP binding site. The SH2 domain of Src family kinases, including Lck and Fyn, plays a critical role in kinase activation.

Tyrphostin B42

133550-30-8sc-3556
5 mg
$26.00
4
(1)

Tyrphostin B42 (AG-490) is a tyrosine kinase inhibitor that specifically targets JAK2. It prevents SH2 domain-mediated JAK2 activation, thereby inhibiting downstream STAT signaling pathways.

NSC 87877

56990-57-9sc-204139
50 mg
$137.00
12
(1)

NSC-87877 is a SHP-1 and SHP-2 phosphatase inhibitor. It prevents the binding of SH2 domains to phosphorylated tyrosine residues, inhibiting downstream signaling pathways.

Dasatinib

302962-49-8sc-358114
sc-358114A
25 mg
1 g
$70.00
$145.00
51
(1)

Dasatinib is a potent inhibitor of multiple tyrosine kinases, including Src family kinases. By binding to the kinase domain, it indirectly prevents SH2 domain-mediated activation and signaling.

Imatinib

152459-95-5sc-267106
sc-267106A
sc-267106B
10 mg
100 mg
1 g
$26.00
$119.00
$213.00
27
(1)

Imatinib targets Bcr-Abl tyrosine kinase. It binds to the kinase domain, preventing its activation. The SH2 domain of Abl is essential for kinase activity, and its function is inhibited by Imatinib.

Lavendustin A

125697-92-9sc-200539
sc-200539A
1 mg
5 mg
$116.00
$456.00
(1)

Lavendustin A inhibits various tyrosine kinases by blocking the ATP binding site. This indirect action can impact SH2 domain functionality by preventing kinase activation.

Doramapimod

285983-48-4sc-300502
sc-300502A
sc-300502B
25 mg
50 mg
100 mg
$149.00
$281.00
$459.00
2
(1)

BIRB 796 targets multiple kinases, including p38 MAP kinase. By binding to kinases, it can indirectly affect the role of SH2 domains in kinase activation and signaling.

WHI-P 154

211555-04-3sc-204395
sc-204395A
10 mg
50 mg
$153.00
$643.00
3
(1)

WHI-P154 is a JAK3 inhibitor that prevents its activation by targeting the kinase domain. This indirectly impacts SH2 domain-mediated activation and subsequent signaling pathways.

Stat3 inhibitor V, stattic

19983-44-9sc-202818
sc-202818A
sc-202818B
sc-202818C
sc-202818D
sc-202818E
sc-202818F
25 mg
100 mg
250 mg
500 mg
1 g
2.5 g
5 g
$130.00
$196.00
$274.00
$512.00
$731.00
$1408.00
$2091.00
114
(3)

Stattic selectively inhibits STAT3 activation by preventing SH2 domain binding to phosphorylated tyrosine residues, thus inhibiting dimerization and downstream signaling.