TTLL7 Inhibitors
TTLL7 Inhibitors encompass a diverse array of chemical compounds that attenuate the functional activity of TTLL7 by affecting the microtubule dynamics and availability of tubulin substrates, with which TTLL7 interacts to carry out tubulin polyglutamylation. Colchicine, Vincristine, Nocodazole, Podophyllotoxin, ARQ 197, Combretastatin A4, and 2-Methoxyestradiol, all function by binding to tubulin and either inhibiting polymerization or promoting depolymerization of microtubules. These actions result in a decreased availability of polyglutamylatable substrates for TTLL7, thereby leading to a diminished activity of this protein through reduced substrate accessibility. Similarly, Taxol and Peloruside A stabilize microtubules, and while this may seem counterintuitive, the resultant decrease in microtubule turnover can indirectly diminish TTLL7 activity by preventing the normal dynamics required for TTLL7 to modify the microtubules effectively.
In addition to these compounds, Eribulin mesylate, Griseofulvin, and Vinflunine contribute to the inhibition of TTLL7 activity by their respective interactions with tubulin which influence microtubule assembly and stability. Eribulin mesylate inhibits the growth phase of microtubules, Vinflunine prevents assembly, and Griseofulvin disrupts microtubule function by affecting the mitotic spindle. These pharmacological actions collectively contribute to a reduction in the functional activity of TTLL7 by diminishing the pool of polyglutamylatable microtubules. By altering the microtubule landscape within the cell, these TTLL7 inhibitors indirectly ensure that TTLL7's role in tubulin polyglutamylation is attenuated due to a lack of proper substrate or altered substrate dynamics, reinforcing the specificity of these compounds in influencing the activity of TTLL7 without affecting its expression.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $100.00 $321.00 $2289.00 $4484.00 $18207.00 $34749.00 | 3 | |
Colchicine binds to tubulin, one of the main constituents of microtubules, preventing its polymerization. As TTLL7 is involved in the post-translational modification of tubulin, specifically polyglutamylation, the inhibition of microtubule polymerization by Colchicine would lead to a reduced substrate availability for TTLL7, thereby diminishing its functional activity. | ||||||
Taxol | 33069-62-4 | sc-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 | |
Taxol stabilizes microtubules and prevents their disassembly. This stabilization can lead to aberrant microtubule dynamics where TTLL7 may not effectively access or modify the microtubules, thus indirectly diminishing the activity of TTLL7. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $59.00 $85.00 $143.00 $247.00 | 38 | |
Nocodazole disrupts microtubule polymerization. The decrease in polymerized microtubules would logically lead to diminished activity of TTLL7, as there would be fewer microtubule substrates to polyglutamylate. | ||||||
Podophyllotoxin | 518-28-5 | sc-204853 | 100 mg | $84.00 | 1 | |
Podophyllotoxin inhibits the polymerization of tubulin into microtubules. This inhibition results in fewer polyglutamylation targets for TTLL7, indirectly diminishing its activity. | ||||||
Eribulin | 253128-41-5 | sc-507547 | 5 mg | $865.00 | ||
Eribulin mesylate inhibits the growth phase of microtubule dynamics, potentially reducing the available targets for TTLL7-mediated polyglutamylation, thereby indirectly diminishing TTLL7 activity. | ||||||
Griseofulvin | 126-07-8 | sc-202171A sc-202171 sc-202171B | 5 mg 25 mg 100 mg | $85.00 $220.00 $598.00 | 4 | |
Griseofulvin disrupts microtubule function by binding to tubulin and affects mitotic spindle formation. This interference with microtubule dynamics indirectly diminishes the activity of TTLL7. | ||||||
ARQ 197 | 905854-02-6 | sc-364408 sc-364408A | 50 mg 200 mg | $712.00 $1920.00 | ||
ARQ 197 disrupts microtubule function by inhibiting tubulin polymerization. Reduced microtubule polymerization diminishes the substrate pool for TTLL7, thus indirectly diminishing its activity. | ||||||
Vinflunine | 162652-95-1 | sc-507411 | 10 mg | $390.00 | ||
Vinflunine interacts with tubulin and inhibits microtubule assembly. Inhibition of microtubule assembly indirectly reduces the functional activity of TTLL7 by decreasing the number of polyglutamylation sites. | ||||||
Combrestatin A4 | 117048-59-6 | sc-204697 sc-204697A | 1 mg 5 mg | $46.00 $81.00 | ||
Combretastatin A4 binds to tubulin at the colchicine binding site, leading to microtubule disassembly. This disruption of microtubules would logically diminish the activity of TTLL7 due to reduced substrate availability. | ||||||
2-Methoxyestradiol | 362-07-2 | sc-201371 sc-201371A | 10 mg 50 mg | $71.00 $288.00 | 6 | |
2-Methoxyestradiol binds to the colchicine site on tubulin, disrupting microtubule networks. This disruption reduces the potential for TTLL7 to polyglutamylate microtubules, thereby diminishing its activity. | ||||||