Chemical inhibitors of KRTAP13 utilize various modes of action to impede the protein's function. Alizarin, for instance, inhibits KRTAP13 by chelating divalent metal ions such as calcium, which are integral to the hair keratin complex's structural stability. This chelation process disrupts the ionic interactions that are essential for KRTAP13's role in hair shaft reinforcement. Another compound, Dihydrotanshinone I, interferes with cellular redox states, thus impacting oxidation-sensitive pathways that could affect the formation of disulfide bonds, which are critical for the structural integrity of KRTAP13. Ellagic acid can destabilize KRTAP13 by disrupting the hydrogen bonding network within the keratin-associated protein complexes, a key factor in maintaining the protein's structural conformation.
Furthermore, Epigallocatechin gallate (EGCG) binds to protein aggregates, potentially preventing the proper assembly of KRTAP13 with other hair keratin proteins. Genistein, a tyrosine kinase inhibitor, alters phosphorylation patterns of proteins associated with keratin, potentially affecting the function and interaction of KRTAP13 with other hair shaft proteins. Indirubin's action on blocking cyclin-dependent kinases could impede the phosphorylation state of KRTAP13, thereby affecting its role in hair structure stabilization. Kaempferol and Quercetin target different aspects; Kaempferol may affect KRTAP13's ability to bind to DNA, which is crucial for the regulation of gene expression in hair follicle development, while Quercetin, acting as a zinc ionophore, chelates zinc ions that are cofactors for proteins in hair follicles, including KRTAP13. Resveratrol influences KRTAP13 by impacting sirtuin activity, which in turn could alter protein acetylation affecting KRTAP13 structure and function in the hair follicle. Lastly, Silibinin's inhibition of STAT3 signaling can have an effect on the activities that are necessary for the optimal expression of KRTAP13 within the hair follicle.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Alizarin | 72-48-0 | sc-214519 sc-214519A | 1.5 g 100 g | $21.00 $51.00 | ||
Alizarin can inhibit KRTAP13 by chelating divalent metal ions such as calcium, which are essential for the structural stability of hair keratin complexes. By binding to these ions, Alizarin may disrupt the ionic interactions crucial for KRTAP13's function in hair shaft reinforcement. | ||||||
Ellagic Acid, Dihydrate | 476-66-4 | sc-202598 sc-202598A sc-202598B sc-202598C | 500 mg 5 g 25 g 100 g | $58.00 $95.00 $245.00 $727.00 | 8 | |
Ellagic acid has the potential to inhibit KRTAP13 by disrupting the hydrogen bonding network within keratin associated protein complexes, as it is known to form strong hydrogen bonds with protein residues, thereby destabilizing the protein's structural conformation. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
Epigallocatechin gallate (EGCG) can inhibit KRTAP13 by binding to protein aggregates, potentially preventing the proper assembly of KRTAP13 with other hair keratin proteins, which is necessary for their collective structural function in hair fiber. | ||||||
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $45.00 $164.00 $200.00 $402.00 $575.00 $981.00 $2031.00 | 46 | |
Genistein can inhibit KRTAP13 by acting as a tyrosine kinase inhibitor, potentially altering phosphorylation patterns of proteins associated with keratin, including KRTAP13, which may rely on specific phosphorylation for its function and interaction with other hair shaft proteins. | ||||||
Indirubin | 479-41-4 | sc-201531 sc-201531A | 5 mg 25 mg | $114.00 $525.00 | 4 | |
Indirubin can inhibit KRTAP13 by blocking cyclin-dependent kinases, which may be involved in the phosphorylation state of hair follicle proteins. The alteration of this state can prevent KRTAP13 from assuming its role in hair structure stabilization. | ||||||
Kaempferol | 520-18-3 | sc-202679 sc-202679A sc-202679B | 25 mg 100 mg 1 g | $99.00 $216.00 $510.00 | 11 | |
Kaempferol can inhibit KRTAP13 by affecting the protein's ability to bind to DNA in the regulation of gene expression relevant to hair follicle development. This flavonoid has been shown to influence DNA-binding proteins, which could include those interacting with KRTAP13. | ||||||
Luteolin | 491-70-3 | sc-203119 sc-203119A sc-203119B sc-203119C sc-203119D | 5 mg 50 mg 500 mg 5 g 500 g | $27.00 $51.00 $101.00 $153.00 $1925.00 | 40 | |
Luteolin can inhibit KRTAP13 activity by modulating signal transduction pathways involved in keratinocyte differentiation. As keratinocytes differentiate, they produce keratins and associated proteins like KRTAP13, and luteolin's influence could inhibit this differentiation process. | ||||||
Myricetin | 529-44-2 | sc-203147 sc-203147A sc-203147B sc-203147C sc-203147D | 25 mg 100 mg 1 g 25 g 100 g | $97.00 $188.00 $260.00 $510.00 $1022.00 | 3 | |
Myricetin can inhibit KRTAP13 by acting as an antioxidant, thereby potentially altering the oxidative environment necessary for the proper formation and stabilization of keratin-associated protein complexes, including those involving KRTAP13. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $110.00 $250.00 $936.00 $50.00 | 33 | |
Quercetin can inhibit KRTAP13 through its role as a zinc ionophore. By chelating zinc, it may interfere with zinc-dependent protein interactions and the proper functioning of KRTAP13 in hair shaft reinforcement, as zinc is a cofactor for many proteins in hair follicles. | ||||||
Resveratrol | 501-36-0 | sc-200808 sc-200808A sc-200808B | 100 mg 500 mg 5 g | $80.00 $220.00 $460.00 | 64 | |
Resveratrol can inhibit KRTAP13 by affecting the activity of sirtuins, which could lead to alterations in protein acetylation and affect the structure and function of keratin-associated proteins, including KRTAP13, in the hair follicle. | ||||||