Chemical inhibitors of PYROXD1 can act through various mechanisms to hinder the protein's function, primarily by altering the oxidative state within the cell, which PYROXD1 is presumed to require for its enzymatic activity. Allopurinol, a well-known inhibitor of xanthine oxidase, can contribute to a reduction in oxidative stress, thereby creating an environment less suitable for the oxidative functions of PYROXD1. Similarly, Apocynin, which impedes the activity of NADPH oxidase, curtails the production of reactive oxygen species (ROS), subsequently reducing the oxidative conditions that are necessary for the proper functioning of PYROXD1 within its role in oxidative protein folding. Ascorbic acid, with its reducing properties, can maintain a cellular redox state that is unfavorable for the oxidative activity associated with PYROXD1. The presence of reduced glutathione further maintains the reductive environment, potentially disrupting the oxidative milieu that PYROXD1 requires.
Furthermore, chemicals like L-Mimosine and Methimazole, which chelate iron and act as radical scavengers respectively, can suppress the formation of radicals that contribute to the oxidative stress implicated in the regulation of PYROXD1 function. Inhibition of signaling pathways that respond to oxidative stress, such as the MAPK pathway by PD98059 or the JNK pathway by SP600125, can alter cellular responses that indirectly affect the activity of PYROXD1. Phenylarsine oxide's ability to inhibit thiol-reactive processes can impede enzymes that depend on thiol groups for their activity, including PYROXD1. Stattic's inhibition of STAT3 signaling can modulate the cell's response to oxidative stress, consequently influencing the function of PYROXD1. Radical-scavenging antioxidants like Tempol and Tiron can also play a role in diminishing the oxidative stress within the cell, indirectly inhibiting the functional environment for PYROXD1 by mitigating the oxidative conditions under which it operates.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Allopurinol | 315-30-0 | sc-207272 | 25 g | $131.00 | ||
Allopurinol inhibits xanthine oxidase, an enzyme involved in the production of uric acid. Inhibition of this enzyme can reduce oxidative stress, which may impair the function of PYROXD1 as it is sensitive to redox changes. | ||||||
Apocynin | 498-02-2 | sc-203321 sc-203321A sc-203321B sc-203321C | 1 g 10 g 100 g 500 g | $27.00 $68.00 $116.00 $360.00 | 74 | |
Apocynin inhibits NADPH oxidase, reducing the production of reactive oxygen species (ROS). Lowered ROS levels can decrease oxidative stress, potentially inhibiting PYROXD1 function as it pertains to handling oxidative protein folding. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $46.00 | 5 | |
Ascorbic acid can act as a reducing agent, potentially maintaining the redox state that is less conducive to the oxidative environment PYROXD1 requires for proper function. | ||||||
Glutathione, reduced | 70-18-8 | sc-29094 sc-29094A | 10 g 1 kg | $82.00 $2091.00 | 8 | |
Glutathione in its reduced form maintains a reductive environment in the cell. This state can inhibit the oxidative environment needed for PYROXD1 to function optimally in oxidative protein folding. | ||||||
L-Mimosine | 500-44-7 | sc-201536A sc-201536B sc-201536 sc-201536C | 25 mg 100 mg 500 mg 1 g | $36.00 $88.00 $220.00 $436.00 | 8 | |
L-Mimosine chelates iron, potentially inhibiting the formation of hydroxyl radicals through the Fenton reaction. This inhibition of radical formation can indirectly inhibit PYROXD1 by reducing oxidative stress that may interfere with its function. | ||||||
Methimazole | 60-56-0 | sc-205747 sc-205747A | 10 g 25 g | $70.00 $112.00 | 4 | |
Methimazole acts as an antioxidant and can scavenge free radicals, thereby potentially inhibiting the oxidative environment required for PYROXD1's enzymatic activity. | ||||||
PD 98059 | 167869-21-8 | sc-3532 sc-3532A | 1 mg 5 mg | $40.00 $92.00 | 212 | |
PD98059 is an inhibitor of MEK, which is upstream of ERK1/2 in the MAPK pathway. Inhibition of this pathway can affect cellular responses to oxidative stress, which may indirectly inhibit PYROXD1's function in redox-sensitive pathways. | ||||||
Phenylarsine oxide | 637-03-6 | sc-3521 | 250 mg | $41.00 | 4 | |
Phenylarsine oxide is an inhibitor of thiol-reactive processes, which can inhibit enzymes like PYROXD1 that may rely on thiol groups for catalytic activity. | ||||||
SP600125 | 129-56-6 | sc-200635 sc-200635A | 10 mg 50 mg | $40.00 $150.00 | 257 | |
SP600125 inhibits JNK, which can affect response to oxidative stress and inflammation, potentially inhibiting the function of PYROXD1 as it is involved in oxidative protein folding. | ||||||
Stat3 inhibitor V, stattic | 19983-44-9 | sc-202818 sc-202818A sc-202818B sc-202818C sc-202818D sc-202818E sc-202818F | 25 mg 100 mg 250 mg 500 mg 1 g 2.5 g 5 g | $130.00 $196.00 $274.00 $512.00 $731.00 $1408.00 $2091.00 | 114 | |
Stattic inhibits STAT3, which is involved in response to oxidative stress. Inhibition of STAT3 signaling can indirectly inhibit PYROXD1 by altering the cellular response to the oxidative stress that affects PYROXD1's function. | ||||||