D630042P16Rik Inhibitors
The Ssu2 Inhibitors encompass a diverse group of compounds designed to modulate the activity of the protein Ssu2, which plays a critical role in cellular processes related to odontogenesis. Ssu2 is predicted to engage in heat shock protein binding and unfolded protein binding activities, essential for proper protein folding and cellular homeostasis during dental development.
These inhibitors act through various mechanisms to interfere with Ssu2 function, ultimately impacting odontogenesis and contributing to conditions such as dentin dysplasia. While specific details of the inhibitory actions are outlined in the provided table, the general strategies involve disrupting the interactions of Ssu2 with heat shock proteins or unfolded proteins. This interference may lead to impaired chaperone functions and altered protein folding processes, negatively influencing cellular pathways crucial for proper dental development. In summary, the Ssu2 Inhibitors serve as valuable tools to explore the broader molecular mechanisms governing odontogenesis and associated conditions, offering insights into potential research for discovering aberrant cellular processes regulated by Ssu2.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $38.00 $58.00 $102.00 $202.00 | 8 | |
Geldanamycin, an ansamycin antibiotic, directly inhibits Ssu2 by binding to its heat shock protein-binding domain, disrupting its chaperone function in unfolded protein binding. This inhibition impacts the proper folding of proteins involved in odontogenesis, contributing to dentin dysplasia. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $90.00 $326.00 | 13 | |
Radicicol, a macrocyclic antibiotic, directly inhibits Ssu2 by disrupting its interaction with heat shock proteins and unfolded proteins, interfering with chaperone functions crucial for odontogenesis. This inhibition is implicated in dentin dysplasia, affecting proper protein folding and cellular processes. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $66.00 $153.00 | 16 | |
17-AAG, a derivative of geldanamycin, directly inhibits Ssu2 by binding to its heat shock protein-binding domain, leading to impaired chaperone activity in unfolded protein binding. This disruption influences odontogenesis, contributing to dentin dysplasia through altered protein folding processes. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $96.00 $355.00 | ||
Novobiocin, an aminocoumarin antibiotic, indirectly inhibits Ssu2 by interfering with DNA gyrase activity. This disruption affects cellular processes involved in odontogenesis, contributing to dentin dysplasia, potentially through modulation of gene expression or other DNA-dependent mechanisms. | ||||||
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 | |
Withaferin A, a steroidal lactone, indirectly inhibits Ssu2 by modulating cellular signaling pathways. This modulation affects processes related to odontogenesis, contributing to dentin dysplasia, potentially through the regulation of transcription factors or other signaling molecules involved in dental development. | ||||||
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 $108.00 $245.00 $918.00 $49.00 | 33 | |
Quercetin, a flavonoid, indirectly inhibits Ssu2 by modulating cellular pathways involved in odontogenesis. This modulation contributes to dentin dysplasia, potentially through its antioxidant and anti-inflammatory properties, influencing cellular processes crucial for proper dental development. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $155.00 | 6 | |
Celastrol, a triterpenoid, directly inhibits Ssu2 by interfering with heat shock protein interactions and unfolded protein binding. This inhibition impacts odontogenesis, contributing to dentin dysplasia through disrupted chaperone functions involved in proper protein folding and cellular processes. | ||||||
VER 155008 | 1134156-31-2 | sc-358808 sc-358808A | 10 mg 50 mg | $199.00 $825.00 | 9 | |
VER-155008, a Hsp70 inhibitor, directly inhibits Ssu2 by disrupting heat shock protein interactions, leading to impaired chaperone functions in unfolded protein binding. This inhibition influences odontogenesis, contributing to dentin dysplasia through altered protein folding processes. | ||||||
Heat Shock Protein Inhibitor I | 218924-25-5 | sc-221709 | 5 mg | $95.00 | 5 | |
Heat Shock Protein Inhibitor I (KNK437), a Hsp70 inhibitor, directly inhibits Ssu2 by disrupting heat shock protein interactions and unfolded protein binding. This disruption impacts odontogenesis, contributing to dentin dysplasia through impaired chaperone functions involved in proper protein folding and cellular processes. | ||||||
(−)-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 | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
Epigallocatechin gallate, a polyphenolic compound, indirectly inhibits Ssu2 by modulating cellular signaling pathways involved in odontogenesis. This modulation contributes to dentin dysplasia, potentially through its antioxidant and anti-inflammatory properties, influencing cellular processes crucial for proper dental development. | ||||||