AHSA2 Activators
Chemical activators of AHSA2 can play a crucial role in modulating its function as a co-chaperone in the heat shock protein 90 (Hsp90) complex. For instance, Adenosine triphosphate (ATP) is a direct energy source that can facilitate the proper folding and stabilization of AHSA2, which is necessary for its activity. The provision of energy by ATP is fundamental for the chaperone cycle, allowing AHSA2 to assist in the folding of nascent polypeptide chains and the stabilization of unfolded proteins. Similarly, divalent cations such as magnesium from Magnesium chloride (MgCl2), zinc from Zinc sulfate (ZnSO4), calcium from Calcium chloride (CaCl2), and copper from Copper(II) sulfate (CuSO4) can bind to AHSA2. This binding can lead to conformational changes that enhance AHSA2's ability to interact with client proteins, thereby improving its chaperone function.
Other chemicals such as Sodium orthovanadate (Na3VO4) can inhibit phosphatases that would otherwise dephosphorylate proteins within the Hsp90 complex, thereby preserving the phosphorylation state that is conducive to AHSA2 activity. Nicotinamide adenine dinucleotide (NADH) provides reducing power that can be crucial for maintaining the redox state of the chaperone complex, which in turn can influence AHSA2 activity. Potassium from Potassium chloride (KCl) and ammonium from Ammonium chloride (NH4Cl) can affect the ionic environment and pH around AHSA2, which can lead to enhanced interaction with its client proteins. Sodium sulfide (Na2S) can contribute to the formation of hydrogen sulfide, a signaling molecule that can lead to post-translational modifications of AHSA2, thereby enhancing its chaperone activity. Arginine can be metabolized into nitric oxide, which can post-translationally modify AHSA2 and similar proteins through S-nitrosylation, a modification that can enhance chaperone activity. Lastly, selenium, provided by Sodium selenite (Na2SeO3), is a critical component for selenoproteins that are involved in the redox regulation within cells, which can indirectly enhance the chaperone activity of AHSA2 by maintaining a reducing environment conducive to its activity.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Adenosine 5′-Triphosphate, disodium salt | 987-65-5 | sc-202040 sc-202040A | 1 g 5 g | $39.00 $75.00 | 9 | |
ATP can activate AHSA2 by providing the energy required for its proper folding and stabilization, which is necessary for its chaperone activity. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $28.00 $35.00 $48.00 $125.00 | 2 | |
Mg2+ ions from MgCl2 can bind to AHSA2 and promote its proper conformation, enhancing its ability to facilitate the folding of target proteins. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zn2+ ions from ZnSO4 can interact with AHSA2, potentially stabilizing its structure and promoting its chaperone function. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $66.00 $262.00 | 1 | |
Ca2+ ions from CaCl2 can bind to AHSA2, inducing a conformational change that increases its chaperone activity. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $49.00 $57.00 $187.00 | 142 | |
As a phosphatase inhibitor, Na3VO4 can prevent dephosphorylation of proteins within the Hsp90 chaperone complex, including AHSA2, thus enhancing its activity. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $46.00 $122.00 $189.00 | 3 | |
Cu2+ ions from CuSO4 can bind to AHSA2, which may lead to a conformational change that increases its activity in assisting protein folding. | ||||||
NAD+, Free Acid | 53-84-9 | sc-208084B sc-208084 sc-208084A sc-208084C sc-208084D sc-208084E sc-208084F | 1 g 5 g 10 g 25 g 100 g 1 kg 5 kg | $57.00 $191.00 $302.00 $450.00 $1800.00 $3570.00 $10710.00 | 4 | |
NADH can provide reducing power that may be required for the regeneration of other cofactors critical for the chaperone function of AHSA2. | ||||||
L-Arginine | 74-79-3 | sc-391657B sc-391657 sc-391657A sc-391657C sc-391657D | 5 g 25 g 100 g 500 g 1 kg | $20.00 $31.00 $61.00 $219.00 $352.00 | 2 | |
Arginine can be converted into nitric oxide, which may modulate the function of molecular chaperones including AHSA2 by S-nitrosylation. | ||||||
Ammonium Chloride | 12125-02-9 | sc-202936 sc-202936A sc-202936B | 25 g 500 g 2.5 kg | $39.00 $55.00 $150.00 | 4 | |
NH4+ from NH4Cl can affect the pH and ionic strength around AHSA2, which can alter its conformation and potentially enhance its chaperone activity. | ||||||
Sodium selenite | 10102-18-8 | sc-253595 sc-253595B sc-253595C sc-253595A | 5 g 500 g 1 kg 100 g | $49.00 $183.00 $316.00 $98.00 | 3 | |
Selenium from Na2SeO3 can be incorporated into selenoproteins, which may be involved in the redox regulation of chaperone proteins including AHSA2. | ||||||