The inhibitors targeting KRTAP10-7 function predominantly manipulate the cytoskeletal framework and signaling pathways that are crucial for the protein's role in hair follicle keratin structure and function. Some inhibitors exert their effects by altering the phosphorylation state of proteins within the cell, which is a key regulatory mechanism for protein function and interaction. For instance, compounds that modulate kinase activity can lead to apoptosis or impact cytoskeletal dynamics essential for keratin filament assembly. The disruption of kinase signaling indirectly affects KRTAP10-7, as its function is contingent upon phosphorylation events. Similarly, phosphatase inhibitors can alter the phosphorylation landscape and thereby influence KRTAP10-7's role in keratin filament organization and stability.
Other inhibitors intervene directly with the cytoskeletal components such as microtubules and actin filaments, which provide structural support for KRTAP10-7's activity. Agents that destabilize microtubules or interfere with their polymerization can indirectly inhibit KRTAP10-7 by disrupting the cellular architecture. This destabilization can affect the proper localization and function of KRTAP10-7, as the integrity of hair follicle structures is closely tied to the cytoskeletal framework. Similarly, compounds that inhibit actin polymerization or promote its disassembly result in cytoskeleton disruption, which can indirectly impact KRTAP10-7's interaction with keratin filaments. Additionally, inhibitors of muscle contractile elements can also affect cellular tension and, consequently, the stability of keratin structures associated with KRTAP10-7.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Staurosporine | 62996-74-1 | sc-3510 sc-3510A sc-3510B | 100 µg 1 mg 5 mg | $82.00 $150.00 $388.00 | 113 | |
A potent kinase inhibitor that acts on various kinases involved in signal transduction pathways, leading to apoptosis. Since KRTAP10-7 is involved in keratin intermediate filament assembly, its function could be indirectly inhibited as kinase activity is essential for phosphorylation events that regulate cytoskeletal dynamics. | ||||||
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 | $98.00 $315.00 $2244.00 $4396.00 $17850.00 $34068.00 | 3 | |
By binding to tubulin and preventing its polymerization into microtubules, colchicine disrupts the cytoskeletal structure and mitotic spindle formation. As KRTAP10-7 is associated with hair follicle keratin, the disruption of microtubules may indirectly affect the structural integrity and function of KRTAP10-7 by altering the cellular framework that supports its proper localization and function. | ||||||
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 | $40.00 $73.00 $217.00 $242.00 $724.00 $1196.00 | 39 | |
A microtubule stabilizer that hyperpolymerizes tubulin, affecting cell division and cytoskeletal dynamics. The altered dynamics and mechanical stress within the cell could indirectly inhibit KRTAP10-7 function by disrupting the physical context in which it operates, affecting keratin filament assembly. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Acts by inhibiting actin polymerization, leading to cytoskeleton disruption. KRTAP10-7's role in hair follicle keratin structures may be inhibited indirectly as actin cytoskeleton is crucial for maintaining cell shape and providing a scaffold for protein localization, potentially affecting KRTAP10-7's interaction with keratin filaments. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $127.00 $572.00 $4090.00 $20104.00 | 20 | |
A steroidal lactone that can bind to annexin II and vimentin, causing cytoskeletal disorganization. By disrupting vimentin, an intermediate filament protein, it may indirectly inhibit KRTAP10-7 function in maintaining structural integrity of hair follicles as both are involved in filament assembly and stability. | ||||||
Trichostatin A | 58880-19-6 | sc-3511 sc-3511A sc-3511B sc-3511C sc-3511D | 1 mg 5 mg 10 mg 25 mg 50 mg | $149.00 $470.00 $620.00 $1199.00 $2090.00 | 33 | |
A histone deacetylase inhibitor that leads to hyperacetylation of histone proteins, affecting gene expression. By altering the expression of genes encoding cytoskeletal proteins, trichostatin A could indirectly inhibit KRTAP10-7 function by affecting the availability or properties of keratin proteins with which KRTAP10-7 interacts. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A sc-24000C | 10 µg 100 µg 1 mg | $160.00 $750.00 $3000.00 | 59 | |
A phosphatase inhibitor that can alter the phosphorylation state of various proteins, including those involved in cytoskeletal dynamics. By impacting the phosphorylation-dependent regulatory mechanisms, calyculin A may indirectly inhibit KRTAP10-7's function related to keratin filament organization and stability. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
A cyclic peptide that stabilizes actin filaments and promotes actin polymerization. By altering the actin cytoskeleton, jasplakinolide may indirectly impact KRTAP10-7 function by modifying the cellular structure that supports the interaction of keratin associated proteins with intermediate filaments. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $182.00 $693.00 | 88 | |
A selective inhibitor of the Rho-associated protein kinase (ROCK), which is involved in actin cytoskeleton organization. Inhibition of ROCK could lead to cytoskeletal rearrangements that indirectly inhibit KRTAP10-7's role in keratin filament assembly within hair follicles. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $71.00 $260.00 $485.00 $949.00 | ||
An inhibitor of myosin II ATPase activity, leading to muscle relaxation. By altering the cellular contractile machinery, this compound may indirectly influence KRTAP10-7 function as changes in cellular tension could affect the cytoskeletal elements and thus the keratin structures associated with KRTAP10-7. | ||||||