V-ATPase D Inhibitors
V-ATPase D Inhibitors belong to a class of chemical compounds designed to selectively target and modulate the activity of the V-ATPase D subunit. The V-ATPase (Vacuolar-type ATPase) is a multi-subunit enzyme complex found in various cellular membranes, including those of endosomes, lysosomes, and the plasma membrane. It plays a pivotal role in regulating intracellular pH, ion homeostasis, and the acidification of cellular compartments. The V-ATPase D subunit is one of the essential components of this complex, contributing to its function in proton translocation across membranes.
Inhibitors of the V-ATPase D subunit are designed to interfere with the proton-pumping activity of the V-ATPase complex. These inhibitors typically target the catalytic subunits of the enzyme, including the V-ATPase D subunit, to block its role in proton transport. By inhibiting the activity of the V-ATPase D subunit, these compounds can disrupt pH regulation within intracellular compartments, leading to alterations in vesicular trafficking, protein processing, and other cellular processes that rely on proper pH maintenance. Researchers study V-ATPase D inhibitors to investigate the functional consequences of V-ATPase inhibition on cellular physiology and to gain insights into the roles of V-ATPase complexes in various cellular processes, including endocytosis, autophagy, and lysosomal function. Understanding the effects of V-ATPase D inhibition contributes to a broader understanding of the intricate mechanisms that govern cellular homeostasis and compartmentalization.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Bafilomycin A1 | 88899-55-2 | sc-201550 sc-201550A sc-201550B sc-201550C | 100 µg 1 mg 5 mg 10 mg | $96.00 $250.00 $750.00 $1428.00 | 280 | |
Bafilomycin A1 inhibits V-ATPase by binding irreversibly to the V0 domain, obstructing the proton translocation pathway. This binding prevents the rotation of the V0 subunit, essential for proton transport, ultimately leading to the inhibition of lysosomal acidification. | ||||||
Concanamycin A | 80890-47-7 | sc-202111 sc-202111A sc-202111B sc-202111C | 50 µg 200 µg 1 mg 5 mg | $65.00 $162.00 $650.00 $2550.00 | 109 | |
Similar to bafilomycin A1, concanamycin A binds to the V0 domain of V-ATPase, inhibiting proton translocation across the lysosomal membrane. By interfering with the rotation of the V0 subunit, concanamycin A effectively blocks the proton pump activity of V-ATPase, resulting in impaired lysosomal acidification. | ||||||
Omeprazole | 73590-58-6 | sc-202265 | 50 mg | $66.00 | 4 | |
Omeprazole inhibits V-ATPase by covalently binding to cysteine residues within the enzyme's catalytic subunit, blocking the proton pumping activity essential for acid secretion in the stomach. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine inhibits V-ATPase by accumulating within acidic vesicles, raising their internal pH and disrupting proton translocation across the vesicular membrane, ultimately impairing lysosomal acidification. | ||||||
Dihydro Artemisinin | 71939-50-9 | sc-211332 | 100 mg | $228.00 | 1 | |
Dihydro artemisinin inhibits V-ATPase by interfering with its proton pumping activity, possibly by affecting the conformational changes necessary for proton translocation across the lysosomal membrane, leading to inhibition of lysosomal acidification. | ||||||
U 18666A | 3039-71-2 | sc-203306 sc-203306A | 10 mg 50 mg | $140.00 $500.00 | 2 | |
U18666A inhibits V-ATPase by interfering with proton translocation across the lysosomal membrane, likely by affecting the structural integrity or function of the enzyme, ultimately leading to impaired lysosomal acidification. | ||||||