Date published: 2026-5-30

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PHLDB2 Inhibitors

PHLDB2 inhibitors represent a diverse class of chemical compounds designed to specifically target and modulate the activity of the PH domain-containing leucine-rich repeat protein phosphatase 2 (PHLDB2). This class of inhibitors is primarily developed for their utility in research settings, aiming to elucidate the intricate signaling pathways in which PHLDB2 plays a crucial role. PHLDB2, also known as LL5β, is a protein with multiple domains, including PH (pleckstrin homology) and LRR (leucine-rich repeat) domains, implicated in cellular processes such as cell adhesion, migration, and intracellular signal transduction. Consequently, PHLDB2 inhibitors serve as invaluable tools for investigating the mechanistic underpinnings of these cellular processes.

The mechanisms of action of PHLDB2 inhibitors are typically centered around the disruption of PHLDB2's normal function within cells. Many inhibitors in this class target the catalytic domain of PHLDB2, which is essential for its enzymatic activity. By binding to this domain, these inhibitors impede PHLDB2's ability to dephosphorylate specific substrates, ultimately affecting downstream signaling cascades. Additionally, some inhibitors may interfere with PHLDB2's interaction with other proteins or cellular structures, disrupting its role in processes such as cell adhesion or cytoskeletal dynamics. Overall, PHLDB2 inhibitors provide a valuable means to dissect the molecular pathways governed by PHLDB2, offering insights into its functional significance in cellular biology and revealing new avenues for intervention, although their specific applications in this regard remain a subject of ongoing investigation.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Enzastaurin

170364-57-5sc-364488
sc-364488A
sc-364488B
10 mg
50 mg
200 mg
$259.00
$612.00
$1721.00
3
(1)

Enzastaurin is a small-molecule inhibitor that targets PHDLB2 by binding to its active site, blocking its phosphorylation and activation. This disruption of PHDLB2 activity leads to reduced cell proliferation and survival in cancer cells.

Sotrastaurin

425637-18-9sc-474229
sc-474229A
5 mg
10 mg
$300.00
$540.00
(0)

Sotrastaurin is an ATP-competitive inhibitor of PHDLB2. It interferes with PHDLB2's kinase activity, inhibiting downstream signaling pathways essential for cell growth and angiogenesis, making it a potential anti-cancer agent.

Gö 6976

136194-77-9sc-221684
500 µg
$227.00
8
(1)

Gö 6976 is a selective inhibitor of PHDLB2, which suppresses its kinase activity by competing with ATP binding. This inhibition hampers cell proliferation and tumor growth by blocking PHDLB2-mediated signaling cascades.

RO-3306

872573-93-8sc-358700
sc-358700A
sc-358700B
1 mg
5 mg
25 mg
$66.00
$163.00
$326.00
37
(1)

RO-3306 is a PHDLB2 inhibitor that targets the ATP binding pocket, blocking PHDLB2 from phosphorylating its substrates. It is commonly used in research to arrest cells in the G2 phase of the cell cycle.

Bisindolylmaleimide I (GF 109203X)

133052-90-1sc-24003A
sc-24003
1 mg
5 mg
$105.00
$242.00
36
(1)

This compound is a pan-kinase inhibitor, including PHDLB2. It functions by binding to the ATP pocket of PHDLB2, leading to the inhibition of its kinase activity and the disruption of cell growth and survival pathways.

Staurosporine

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

Staurosporine is a potent inhibitor of PHDLB2 and various other kinases. It works by binding to the ATP-binding site of PHDLB2, effectively blocking its catalytic activity, which hinders cell proliferation and survival.

PKC-412

120685-11-2sc-200691
sc-200691A
1 mg
5 mg
$52.00
$114.00
10
(1)

PKC412 is a multikinase inhibitor with activity against PHDLB2. It interferes with PHDLB2's ATP-binding domain, impeding its kinase activity and downstream signaling pathways crucial for cell growth and survival.

Ruboxistaurin

169939-94-0sc-507364
25 mg
$1080.00
(0)

Ruboxistaurin inhibits PHDLB2 by interfering with its ATP-binding domain, thereby blocking its phosphorylation of substrates and affecting signaling pathways related to diabetic complications.