Date published: 2026-4-1

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RINT-1 Inhibitors

Chemical inhibitors of RINT-1 target various aspects of the cellular machinery involved in vesicle trafficking, each affecting the protein's function in unique ways. Monastrol directly inhibits the motor protein Eg5, which is crucial for maintaining the organization of the Golgi apparatus during mitosis. The inhibition of Eg5 by Monastrol leads to disruption in mitotic spindle formation, ultimately impairing RINT-1's role in vesicle transport during cell division. Similarly, Nocodazole's binding to tubulin and inhibition of its polymerization disrupts microtubule dynamics, which are essential for RINT-1's associated vesicle transport. The resulting microtubule dysfunction inhibits RINT-1's ability to mediate this trafficking effectively. Paclitaxel, on the other hand, hyper-stabilizes microtubules, preventing their dynamic rearrangement which is necessary for RINT-1's role in vesicle trafficking.

Moreover, actin cytoskeleton disruptors like Cytochalasin D and Latrunculin A inhibit actin polymerization, thereby impairing RINT-1-mediated vesicular movement and fusion, as the actin cytoskeleton is integral to RINT-1's function. Brefeldin A inhibits ADP-ribosylation factor, a small GTPase involved in vesicle formation from the Golgi, disrupting the vesicular transport from the ER to the Golgi and thus inhibiting the function of RINT-1 in this process. Golgicide A targets GBF1, a guanine nucleotide exchange factor for ARF, and its inhibition disrupts Golgi apparatus functionality, which is necessary for RINT-1's role in vesicle trafficking. Dynasore's inhibition of dynamin GTPase activity directly impedes endocytic vesicle formation, thereby indirectly inhibiting RINT-1's function in endocytosis. Pitstop 2 inhibits clathrin-mediated endocytosis, blocking the vesicle formation and trafficking on which RINT-1 relies. Continuing this theme, Endosidin2 disrupts the EXO70 subunit of the exocyst complex, which is involved in the targeting and fusion of vesicles to the plasma membrane, inhibiting RINT-1's role in vesicular transport to the membrane. ML141, a selective inhibitor of Cdc42 GTPase, disrupts actin cytoskeleton organization, essential for RINT-1's function in vesicular trafficking. Lastly, SecinH3 inhibits cytohesins, disrupting ARF GTPase activity, which in turn inhibits RINT-1's role in ER to Golgi transport and overall vesicular trafficking.

SEE ALSO...

Items 1 to 10 of 11 total

Display:

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Monastrol

254753-54-3sc-202710
sc-202710A
1 mg
5 mg
$120.00
$233.00
10
(1)

Monastrol is a cell-permeable small molecule inhibitor known to specifically inhibit the motor protein Eg5 (kinesin-5). RINT-1 is involved in trafficking between the ER and Golgi, and Eg5 is essential for maintaining the organization of the Golgi apparatus during mitosis. Inhibition of Eg5 by Monastrol would disrupt the mitotic spindle formation and thus could lead to an indirect inhibition of RINT-1's function in vesicle transport during cell division.

Nocodazole

31430-18-9sc-3518B
sc-3518
sc-3518C
sc-3518A
5 mg
10 mg
25 mg
50 mg
$59.00
$85.00
$143.00
$247.00
38
(2)

Nocodazole is a synthetic compound that disrupts microtubule dynamics by binding to tubulin and inhibiting its polymerization. RINT-1 is associated with microtubule-dependent vesicle transport; thus, the disruption of microtubules by Nocodazole would inhibit RINT-1's ability to mediate vesicle trafficking effectively.

Taxol

33069-62-4sc-201439D
sc-201439
sc-201439A
sc-201439E
sc-201439B
sc-201439C
1 mg
5 mg
25 mg
100 mg
250 mg
1 g
$41.00
$74.00
$221.00
$247.00
$738.00
$1220.00
39
(2)

Paclitaxel is a chemotherapeutic agent that stabilizes microtubules and prevents their depolymerization. By hyper-stabilizing microtubules, Paclitaxel can inhibit the dynamic rearrangement of microtubules required for RINT-1's role in vesicle trafficking.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$165.00
$486.00
64
(4)

Cytochalasin D is known to inhibit actin polymerization. Since RINT-1 is involved in vesicular trafficking, which relies on the actin cytoskeleton, inhibition of actin polymerization by Cytochalasin D would impair RINT-1-mediated vesicular movement and fusion.

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$265.00
$815.00
36
(2)

Latrunculin A binds to actin monomers, preventing their polymerization. This actin disruption would inhibit RINT-1 function because RINT-1 requires the actin cytoskeleton for the trafficking and sorting of vesicles.

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$31.00
$53.00
$124.00
$374.00
25
(3)

Brefeldin A inhibits ADP-ribosylation factor (ARF), a small GTPase involved in vesicle formation from the Golgi. By inhibiting ARF, Brefeldin A would disrupt vesicular transport from the ER to the Golgi and thereby inhibit RINT-1's role in this process.

Golgicide A

1005036-73-6sc-215103
sc-215103A
5 mg
25 mg
$191.00
$683.00
11
(1)

Golgicide A specifically inhibits the Golgi BFA resistance factor 1 (GBF1), a guanine nucleotide exchange factor for ARF. Inhibition of GBF1 by Golgicide A will disrupt the function of the Golgi apparatus, which is necessary for RINT-1's role in vesicle trafficking.

Dynamin Inhibitor I, Dynasore

304448-55-3sc-202592
10 mg
$89.00
44
(2)

Dynasore is a non-competitive inhibitor of the GTPase activity of dynamin, which is required for vesicle scission during endocytosis. By inhibiting dynamin, Dynasore would directly inhibit endocytic vesicle formation, thus indirectly inhibiting RINT-1's function in this process.

Pitstop 2

1419320-73-2sc-507418
10 mg
$360.00
(0)

Pitstop 2 is an inhibitor of clathrin-mediated endocytosis. It would inhibit RINT-1's function by blocking vesicle formation and trafficking, processes in which RINT-1 is involved.

ML 141

71203-35-5sc-362768
sc-362768A
5 mg
25 mg
$137.00
$512.00
7
(1)

ML141 is a selective inhibitor of Cdc42 GTPase. By inhibiting Cdc42, ML141 would disrupt actin cytoskeleton organization, which is essential for RINT-1's function in vesicular trafficking.