HAH1 Activators consist of a range of compounds that, through indirect mechanisms, enhance the functional activity of HAH1, a protein encoded by the ATOX1 gene and critical in copper homeostasis. The primary role of HAH1 is to bind and shuttle copper ions to ATP7A and ATP7B transporters in the trans-Golgi network, a process vital for proper copper distribution and utilization in the cell. Copper(II) Sulfate is fundamental in this context as it provides the necessary copper ions for HAH1 to bind and transport. The presence of this compound is crucial in facilitating HAH1's role in maintaining copper balance within the cell. In addition to direct copper suppliers, various chelating agents play a significant role in modulating HAH1 activity. Compounds such as Bathocuproine, Tetrathiomolybdate (TTM), Penicillamine, and Neocuproine, by binding free copper ions, create a cellular environment that necessitates efficient copper mobilization, thereby increasing the demand for HAH1's activity. This scenario underscores the importance of HAH1 in adapting to changes in copper availability and maintaining homeostasis.
Similarly, compounds like Disulfiram and chelators like Clioquinol, Ammonium tetrathiomolybdate, and Triethylenetetramine enhance HAH1's activity by sequestering copper, thus elevating the cell's reliance on HAH1 for copper transport and regulation. Moreover, other agents such as Zinc sulfate solution and L-Histidine, although not directly interacting with copper, influence copper homeostasis by competing for binding sites or forming complexes with copper ions. This competition further highlights the critical function of HAH1 in navigating the cellular copper landscape. Additionally, L-Mimosine, known for its iron-chelating properties, can also impact copper homeostasis, thereby indirectly enhancing the requirement for HAH1's role in copper transport. Collectively, these HAH1 Activators, through their varied mechanisms of copper modulation, underscore the protein's essential function in regulating copper homeostasis, a key aspect of cellular health and metabolism.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper(II) Sulfate indirectly enhances HAH1 activity. HAH1 functions in copper homeostasis by binding and transferring copper ions. The availability of copper ions, provided by compounds like Copper(II) Sulfate, is crucial for HAH1's activity in binding and shuttling copper to ATP7A/B transporters in the trans-Golgi network. | ||||||
Bathocuproine | 4733-39-5 | sc-257115 | 500 mg | $51.00 | ||
Bathocuproine, a copper chelator, indirectly enhances HAH1 activity. By binding free copper ions, it creates a need for more efficient copper mobilization within the cell. This situation potentially increases the demand for HAH1's copper-binding and transfer activity, emphasizing its role in intracellular copper regulation. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc sulfate solution indirectly enhances HAH1 activity. While Zinc does not directly interact with HAH1, it can compete with copper for binding sites in cells. This competition may lead to an increased requirement for HAH1's role in copper homeostasis, as HAH1 is essential in regulating and transporting copper ions. | ||||||
L-Histidine | 71-00-1 | sc-394101 sc-394101A sc-394101B sc-394101C sc-394101D | 25 g 100 g 250 g 500 g 1 kg | $53.00 $82.00 $185.00 $200.00 $332.00 | 1 | |
L-Histidine, an amino acid that binds copper, indirectly enhances HAH1 activity. L-Histidine can form complexes with copper ions, potentially increasing the demand for HAH1-mediated copper transport within the cell to maintain copper homeostasis and supply copper to essential copper-dependent enzymes. |