ATPases

Ciliobrevin D is a AAA+ ATPase motor cytoplasmic dynein inhibitor. Ciliobrevin D inhibits Hedgehog (Hh) signaling and primary cilia formation and it also inhibits dynein-dependent microtubule gliding and ATPase activity in vitro.

Esomeprazole Magnesium (NEXIUM) is the S-isomer of omeprazole, can reduce gastric acid secretion with selective and irreversible proton pump inhibitor activity.Esomeprazole magnesium acts as an exosome inhibitor by blocking the exosome release via the inhibition of V-H+-ATPases

Esomeprazole Sodium ((S)-Omeprazole sodium) is the S-isomer of omeprazole with selective and irreversible proton pump inhibitor activity.Esomeprazole acts as an exosome inhibitor by blocking the exosome release via the inhibition of V-H+-ATPases

Esomeprazole Magnesium trihydrate ((S)-Omeprazole magnesium trihydrate) is a proton pump inhibitor indicated for the short-term treatment of gastroesophageal reflux disease in patients with a history of erosive esophagitis.Esomeprazole magnesium trihydrate acts as an exosome inhibitor by blocking the exosome release via the inhibition of V-H+-ATPases

V-ATPase-IN-1 (Compound 3b-03) is an inhibitor of Vacuolar-type H+-ATPases (V-ATPase), exhibiting an inhibition constant (IC50) of 194.80 μM and effectively targeting the V-ATPase subunit A with a dissociation constant (Kd) of 0.803 μM. This compound demonstrates insecticidal activity against M. separata (LC50 = 2.64 mM), aiding in the development of chemical insecticides.

AU-24118 is an orally bioavailable chimeric degrader (PROTAC) that targets the proteolysis of mSWI/SNF ATPases (SMARCA2 and SMARCA4) and PBRM1.

Blebbistatin ((±)-Blebbistatin) is a non-muscle myosin II (NMII)-selective and non-muscle myosin heavy chain 9 (MYH9)-specific inhibitor that promotes directional migration of corneal endothelial cells (CECs) and accelerates wound healing, while preserving the integrity of cell junctions and barrier function.

vacuolar H+-ATPases (V-ATPases) inhibitor

Rutamycin is a macrolide antibiotic of the oligomycin group obtained from Streptomyces rutgersensis. It inhibits various ATPases and uncouples oxidative phosphorylation from electron transport.

Concanamycin B is a macrolide antibiotic that selectively inhibits vacuolar type H+-ATPases (IC50 = 5 nM), thereby blocking vacuolar organelle acidification and early to late endosomal transport. It interferes with bone resorption, maturation of CD8 T lymphocytes, and prevents processing of major histocompatibility complex (MHC) class II precursors in human B cells, inhibiting MHC class II molecule expression on the cell surface.

(S)-nitro-Blebbistatin is a more stable form of (-)-blebbistatin , which is a selective cell-permeable inhibitor of non-muscle myosin II ATPases. (-)-Blebbistatin rapidly and reversibly inhibits Mg-ATPase activity and in vitro motility of non-muscle myosin IIA and IIB for several species (IC50s = 0.5-5 μM), while poorly inhibiting smooth muscle myosin (IC50 = 80 μM). Through these effects, it blocks apoptosis-related bleb formation, directed cell migration, and cytokinesis in vertebrate cells. However, prolonged exposure to blue light (450-490 nm) results in degradation of blebbistatin to an inactive product via cytotoxic intermediates, which may be problematic for its use in fluorescent live cell imaging applications. The addition of a nitro group stabilizes the molecule to circumvent its degradation by prolonged blue light exposure. (S)-nitro-Blebbistatin has the same stereochemistry as the active (-)-blebbistatin enantiomer.

para-amino-Blebbistatin is a more water-soluble form of (S)-4'-nitro-blebbistatin , which is a more stable and less phototoxic form of (-)-blebbistatin .1,2,3 (-)-Blebbistatin is a selective cell-permeable inhibitor of non-muscle myosin II ATPases that rapidly and reversibly inhibits Mg-ATPase activity and in vitro motility of non-muscle myosin IIA and IIB for several species (IC50s = 0.5-5 μM), while poorly inhibiting smooth muscle myosin (IC50 = 80 μM).2,3,4 Through these effects, it blocks apoptosis-related bleb formation, directed cell migration, and cytokinesis in vertebrate cells. However, prolonged exposure to blue light (450-490 nm) results in degradation of blebbistatin to an inactive product via cytotoxic intermediates, which may be problematic for its use in fluorescent live cell imaging applications.5,6 The addition of a 4'-amino group increases its water solubility, decreases the inherent fluorescence, stabilizes the molecule to circumvent its degradation by prolonged blue light exposure, and decreases its phototoxicity while retaining the in vitro and in vivo activity of blebbistatin.7 para-amino-Blebbistatin has the same stereochemistry as the active (-)-blebbistatin enantiomer. |1. Várkuti, B.H., Képiró, M., Horváth, I.á., et al. A highly soluble, non-phototoxic, non-fluorescent blebbistatin derivative. Sci. Rep. 6:26141, (2016).|2. Straight, A.F., Cheung, A., Limouze, J., et al. Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor. Science 299(5613), 1743-1747 (2003).|3. Kovács, M., Tóth, J., Hetényi, C., et al. Mechanism of blebbistatin inhibition of myosin II. J. Biol. Chem. 279(34), 35557-35563 (2004).|4. Limouze, J., Straight, A.F., Mitchison, T., et al. Specificity of blebbistatin, an inhibitor of myosin II. J. Muscle Res. Cell Motil. 25(4-5), 337-341 (2004).|5. Kolega, J. Phototoxicity and photoinactivation of blebbistatin in UV and visible light. Biochem. Biophys. Res. Commun. 320(3), 1020-1025 (2004).|6. Sakamoto, T., Limouze, J., Combs, C.A., et al. Blebbistatin, a myosin II inhibitor, is photoinactivated by blue light. Biochemistry 44(2), 584-588 (2005).|7. Verhasselt, S., Roman, B.I., Bracke, M.E., et al. Improved synthesis and comparative analysis of the tool properties of new and existing D-ring modified (S)-blebbistatin analogs. Eur. J. Med. Chem. 136, 85-103 (2017).

Manzamine A hydrochloride is an orally active beta-carboline alkaloid that exhibits specific inhibitory effects on GSK-3β (IC50 = 10.2 μM) and CDK-5 (IC50 = 1.5 μM). Additionally, it targets vacuolar ATPases, leading to the inhibition of autophagy in pancreatic cancer cells. Manzamine A hydrochloride possesses antimalarial and anticancer properties, and also demonstrates potent activity against HSV-1[4].

Inosine-5'-triphosphate trisodium salt (ITP) is used in studies on the impact of deamination of ATP and GTP by various enzymes and chemical processes. Inosine-5'-triphosphate trisodium salt (ITP) may be used as a substrate to study the specificity and kinetics of nucleoside-5′-triphosphatase and ATPase. Inosine-5'-triphosphate trisodium salt (ITP) is also used to study activation of various ATPases and GTPases.

(-)-Blebbistatin ((S)-(-)-Blebbistatin) is an S enantiomer of blebbistatin. It is a potent and selective myosin II inhibitor with IC50 ranging from 0.5 to 5 μM.

Naja Mossambica Venom (Mozambique Spitting Cobra Venom) is a snake venom derived from Naja Mossambica, exhibiting antifungal activity against Candida species. Extracts, including phospholipase A2, can inhibit sodium-potassium ATPase activity [1] [2].

SPAI-1, a peptide isolated from porcine duodenum, serves as a specific inhibitor to monovalent cation transporting ATPases, effectively inhibiting Na+, K+-ATPase and H+, K+-ATPase while stimulating Mg2+-ATPase in vitro [1] [2].

(S)-3'-hydroxy-Blebbistatin is a more stable and less phototoxic derivative of (–)-blebbistatin, retaining the latter's properties as a selective, cell-permeable inhibitor of non-muscle myosin II ATPases. Unlike its predecessor, (S)-3'-hydroxy-Blebbistatin exhibits reduced fluorescence, improving its utility in live cell imaging applications by diminishing degradation into cytotoxic intermediates under blue light exposure (450-490 nm). It effectively inhibits the Mg-ATPase activity and in vitro motility of non-muscle myosin IIA and IIB across various species with IC50 values ranging from 0.5-5 µM and shows minimal inhibition against smooth muscle myosin with an IC50 of 80 µM. This compound plays a critical role in preventing apoptosis-related bleb formation, directed cell migration, and cytokinesis in vertebrate cells, mirroring the active (–)-blebbistatin enantiomer in mechanism and efficacy.

(S)-3'-amino Blebbistatin, retaining the active stereochemistry of the less stable and more phototoxic (–)-blebbistatin, serves as a refined selective cell-permeable inhibitor of non-muscle myosin II ATPases. This compound efficaciously inhibits the Mg-ATPase activity and in vitro motility of non-muscle myosin IIA and IIB across several species with IC50s ranging from 0.5-5 µM, and exhibits minimal inhibition against smooth muscle myosin (IC50= 80 µM). Its primary functions include obstructing apoptosis-related bleb formation, directed cell migration, and cytokinesis in vertebrate cells. (S)-3'-amino Blebbistatin overcomes (–)-blebbistatin's limitation of rapid degradation under blue light (450-490 nm) exposure, which generates cytotoxic intermediates, thus posing a challenge for fluorescent live cell imaging applications. The introduction of a 3'-amino group to its structure notably reduces fluorescence while maintaining (–)-blebbistatin's activity, making it a superior alternative for research purposes.

Caloxin 1C2 is a specific inhibitor of PMCA (plasma membrane Ca2+-ATPases), displaying selective affinity for PMCA4 over PMCA1, 2, and 3. The Ki values for Caloxin 1C2 are 2.3 μM for PMCA4 and 21 μM for PMCA1. Notably, Caloxin 1C2 does not significantly affect overall Ca2+ transport. Additionally, it impacts the contractile force of coronary arteries.

RUVBL1/2 ATPase-IN-1 is an effective RUVBL1/2 ATPase inhibitor with IC50 values of 6.0 and 7.7 μM, respectively. RUVBL1/2 ATPase-IN-1 can be used in cancer disease studies.

Esomeprazole sodium-d6 is a deuterated compound of Esomeprazole sodium. Esomeprazole sodium has a CAS number of 161796-78-7. Esomeprazole Sodium is the S-isomer of omeprazole with selective and irreversible proton pump inhibitor activity.Esomeprazole acts as an exosome inhibitor by blocking the exosome release via the inhibition of V-H+-ATPases

Concanamycin C, a natural macrolide antibiotic, was initially isolated from Streptomyces and identified as an inhibitor of T-cell proliferation in response to concanavalin A (1,2). It exhibits cytotoxicity to fungi, including yeasts, by inhibiting vacuolar-type ATPases (3,4).