Date published: 2025-10-15

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MIPP Inhibitors

Chemical inhibitors of MIPP include a range of compounds that interfere with the protein's phosphatase activity. NSC 87877, for example, is a selective inhibitor of the protein tyrosine phosphatase Shp2. The inhibition of Shp2 leads to a disruption of the phosphorylation balance within the cell, which can indirectly lead to the inhibition of MIPP by altering substrate availability. Similarly, Sodium orthovanadate, a general inhibitor of protein tyrosine phosphatases, can increase cellular phosphorylation levels, which in turn can inhibit MIPP by reducing its substrates or altering its regulatory state. Suramin, which is known to inhibit various enzymes and receptor interactions, can bind to the active site or allosteric sites of MIPP, preventing the natural substrates from accessing the catalytic domain of MIPP.

Other inhibitors like Phenylarsine oxide target thiol-dependent enzymes and can interact with cysteine residues in MIPP that are critical for its catalytic mechanism. Cantharidin and Calyculin A, both inhibitors of protein phosphatases PP1 and PP2A, can bind to the active site of MIPP, preventing the dephosphorylation of substrates. Similarly, Okadaic Acid can block the access of substrates to the catalytic residues of MIPP by binding to its active site. Tautomycetin, known to inhibit PP1, could inhibit MIPP by binding to its active site or interacting with catalytically important residues. Endothall, an organophosphate herbicide that inhibits PP2A, can phosphorylate MIPP at the active site, which would prevent substrate access and catalytic activity. Fostriecin, which selectively inhibits PP2A and PP4, can obstruct substrate binding and phosphatase activity of MIPP. Microcystin-LR, a cyanobacterial toxin, can inhibit MIPP by binding irreversibly to the active site, thereby preventing substrate dephosphorylation. Lastly, Demecolcine disrupts microtubule polymerization, and although not a direct inhibitor of MIPP, this disruption can interfere with cellular transport processes and could lead to functional inhibition of MIPP.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

NSC 87877

56990-57-9sc-204139
50 mg
$134.00
12
(1)

NSC 87877 is a selective inhibitor of Shp2, a protein tyrosine phosphatase. MIPP, being a phosphatase, relies on the balance of phosphorylation within the cell. Inhibition of Shp2 by NSC 87877 disrupts this balance, leading to inhibition of MIPP by altering substrate availability.

Sodium Orthovanadate

13721-39-6sc-3540
sc-3540B
sc-3540A
5 g
10 g
50 g
$45.00
$56.00
$183.00
142
(4)

Sodium orthovanadate is a general inhibitor of protein tyrosine phosphatases. By inhibiting these phosphatases, it can increase the overall phosphorylation level inside the cell, which in turn can inhibit MIPP by reducing its substrates or altering its regulatory state.

Suramin sodium

129-46-4sc-507209
sc-507209F
sc-507209A
sc-507209B
sc-507209C
sc-507209D
sc-507209E
50 mg
100 mg
250 mg
1 g
10 g
25 g
50 g
$149.00
$210.00
$714.00
$2550.00
$10750.00
$21410.00
$40290.00
5
(1)

Suramin is known to inhibit various enzymes and receptor interactions. It could inhibit MIPP through competitive inhibition by binding to the active site or allosteric sites, thus preventing the access of natural substrates to the catalytic domain of MIPP.

Phenylarsine oxide

637-03-6sc-3521
250 mg
$40.00
4
(1)

Phenylarsine oxide is an inhibitor of thiol-dependent enzymes. MIPP, as a phosphatase, could be inhibited by this chemical through the interaction with cysteine residues that are often critical for the enzyme's catalytic mechanism.

Cantharidin

56-25-7sc-201321
sc-201321A
25 mg
100 mg
$81.00
$260.00
6
(1)

Cantharidin inhibits protein phosphatases 1 (PP1) and 2A (PP2A). Given that MIPP is a member of the protein phosphatase family, cantharidin could inhibit MIPP by a similar mechanism of action, which involves covalent modification of the active site.

Calyculin A

101932-71-2sc-24000
sc-24000A
sc-24000B
sc-24000C
10 µg
100 µg
500 µg
1 mg
$160.00
$750.00
$1400.00
$3000.00
59
(3)

Calyculin A, like cantharidin, is an inhibitor of PP1 and PP2A. It could inhibit MIPP by binding to its active site, preventing the dephosphorylation of substrates.

Okadaic Acid

78111-17-8sc-3513
sc-3513A
sc-3513B
25 µg
100 µg
1 mg
$285.00
$520.00
$1300.00
78
(4)

Okadaic Acid is a potent inhibitor of PP1 and PP2A. Its mode of inhibiting MIPP could involve the binding to the phosphatase active site, thereby blocking the access of substrates to the catalytic residues.

Endothall

145-73-3sc-201325
sc-201325A
20 mg
100 mg
$48.00
$199.00
1
(1)

Endothall is an organophosphate herbicide that inhibits PP2A. MIPP could be inhibited by endothall through its phosphorylation at the active site, which would prevent substrate access and catalytic activity.

Fostriecin

87860-39-7sc-202160
50 µg
$260.00
9
(1)

Fostriecin selectively inhibits PP2A and PP4. It could inhibit MIPP by interacting with the active site, which would obstruct substrate binding and phosphatase activity.

Colcemid

477-30-5sc-202550A
sc-202550
sc-202550B
sc-202550C
sc-202550D
sc-202550E
1 mg
5 mg
10 mg
50 mg
100 mg
500 mg
$67.00
$159.00
$312.00
$928.00
$1856.00
$6706.00
7
(1)

Demecolcine disrupts microtubule polymerization. Although not a direct inhibitor of MIPP, by disrupting microtubules, it could interfere with cellular transport processes, potentially leading to a functional inhibition of MIPP within its intracellular context.