recombinant enpp1 enzyme (R&D Systems)
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recombinant enpp1 enzyme
Recombinant Enpp1 Enzyme, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+enpp1+enzyme/Recombinant+Human+ENPP-1+Protein%2C+CF/pm41687265-331-13-17
Average 94 stars, based on 15 article reviews
Recombinant Enpp1 Enzyme, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+enpp1+enzyme/Recombinant+Human+ENPP-1+Protein%2C+CF/pm41687265-331-13-17
Average 94 stars, based on 15 article reviews
recombinant enpp1 enzyme - by Bioz Stars,
2026-10
94/100 stars
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Incubation:Article Title: Discovery of novel ENPP1 inhibitors with benzotriazole core for cancer immunotherapy. Article Snippet: The cGAS-STING signaling pathway is an essential mechanism in the recruitment and activation of innate and adaptive immune cells to exert an antitumor response in cancer immunotherapy. cGAMP is a crucial immunotransmitter, which is potentially degraded by ENPP1, resulting in the deactivation of STING-mediated antitumor immune responses.. We herein describe the design, synthesis, and biological evaluation of novel ENPP1 inhibitors containing a benzotriazole core and a sulfonimidamide Zn binder.. Notably, compound 44a demonstrated potent and selective ENPP1 inhibition with an IC50 value of 13.1 nM and effectively activated the STING pathway in HCT116-DualTM cells. Recombinant:Article Title: Discovery of novel ENPP1 inhibitors with benzotriazole core for cancer immunotherapy. Article Snippet: The cGAS-STING signaling pathway is an essential mechanism in the recruitment and activation of innate and adaptive immune cells to exert an antitumor response in cancer immunotherapy. cGAMP is a crucial immunotransmitter, which is potentially degraded by ENPP1, resulting in the deactivation of STING-mediated antitumor immune responses.. We herein describe the design, synthesis, and biological evaluation of novel ENPP1 inhibitors containing a benzotriazole core and a sulfonimidamide Zn binder.. Notably, compound 44a demonstrated potent and selective ENPP1 inhibition with an IC50 value of 13.1 nM and effectively activated the STING pathway in HCT116-DualTM cells. Article Title: Identification of novel pyrrolopyrimidine and pyrrolopyridine derivatives as potent ENPP1 inhibitors. Article Snippet: .. Serially diluted ENPP1 inhibitors (usually range from 10 lM to 0.5 nM) are pre-incubated with human Article Title: Identification of novel pyrrolopyrimidine and pyrrolopyridine derivatives as potent ENPP1 inhibitors Article Snippet: .. Serially diluted ENPP1 inhibitors (usually range from 10 μM to 0.5 nM) are pre-incubated with |
![High glucose levels impair the pyrophosphate-to-phosphate ratio. Aortic smooth muscle cells were incubated for one month in medium containing 1 g/L or 4.5 g/L glucose. A Autoradiograph displaying representative products from the hydrolysis of ATP (1 µmol/L ATP, 10 µCi/mL [γ 32 Pi]ATP) incubated with or without recombinant eNPP1 (ectonucleotide pyrophosphatase/phosphodiesterase 1) or eNTPD1 (ectonucleoside triphosphate diphosphohydrolase 1) enzymes. Enzymatic hydrolysis generated radiolabeled 32 PPi (32-pyrophosphate) and 32 Pi (32-phosphate), which, alongside unreacted [γ 32 Pi]ATP, were separated by thin-layer chromatography (TLC), as detailed in the section. B Representative time course of ATP hydrolysis showing the products released over time. C Synthesis of the pyrophosphate 32 PPi via hydrolysis of [γ 32 Pi]ATP (10 µCi/mL; 1 µmol/L ATP) in the absence or presence of 100 µmol/L SBI245 (a specific TNAP inhibitor) or inorganic pyrophosphatase (PPase). D The pyrophosphate-to-phosphate ( 32 PPi/ 32 Pi) ratio was quantified following hydrolysis of [γ 32 Pi]ATP (10 µCi/mL; 1 µmol/L ATP) under various conditions: in the absence of inhibitors (Control), in the presence of an ectonucleoside triphosphate diphosphohydrolase (eNTPD) inhibitor (INH, 200 µmol/L), or with the recombinant enzymes eNPP1 and eNTPD1 (100 ng/mL). Experiments were conducted in media containing either physiological (1 g/L) or elevated (4.5 g/L) glucose concentrations. D) Synthesis of 32 PPi by hydrolysis of [γ 32 Pi]ATP (10 µCi/mL and 1 µmol/L ATP). E Hydrolysis of 32 PPi (10 µCi/mL and 5 µmol/L PPi). The results are shown as the mean ± SEM (4 independent experiments with 4 plates per experiment). Student’s t test ( E, F ) or one-way ANOVA with Tukey’s post hoc test ( C, D ) was used for statistical analysis. Asterisks indicate a statistically significant difference compared with the control group: * P < 0.05; *** P < 0.001. ### Indicates a value of P < 0.001 compared with the control group (1 g/L)](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_5999/pmc11555999/pmc11555999__12933_2024_2502_Fig3_HTML.jpg)
![STZ-treated rats exhibit impaired extracellular pyrophosphate metabolism in the aortic wall. A A representative time course of ATP hydrolysis was conducted using a 1 µmol/L ATP solution containing 10 µCi/mL [γ- 32 P]ATP as a radiotracer. The products of hydrolysis, 32 PPi (32-pyrophosphate), 32 Pi (32-phosphate), and [γ- 32 P]ATP-, were separated and quantified via thin layer chromatography, as outlined in the section. B The synthesis of pyrophosphate (PPi) was analyzed by hydrolyzing 1 µmol/L ATP containing 10 µCi/mL [γ- 32 P]ATP as a radiotracer. The reactions were carried out in the absence or presence of either a specific TNAP inhibitor (SBI-425) or inorganic pyrophosphatase (PPase). C The ratio of 32 PPi to 32 Pi generated by ATP hydrolysis was calculated to assess the efficiency and specificity of pyrophosphate synthesis. D The synthesis of 32 PPi was evaluated by hydrolyzing 1 µmol/L ATP containing 10 µCi/mL [γ- 32 P]ATP. E The release of 32 Pi was measured following the hydrolysis of 5 µmol/L pyrophosphate, which contained 10 µCi/mL 32 PPi as a radiotracer. F Quantification of protein levels via ELISA. G , H Total RNA was isolated from rat aortas to evaluate the expression levels of key enzymes involved in extracellular pyrophosphate metabolism, including eNTPD1 (ectonucleoside triphosphate diphosphohydrolase 1), eNPP1 (ectonucleotide pyrophosphatase/phosphodiesterase 1), and tissue-nonspecific alkaline phosphatase (TNAP) (panel G . Additionally, the expression of calcification-related proteins, such as matrix Gla protein (MGP) and osteopontin (OPN), was assessed (panel H). The data are shown as the mean ± SEM and represent data from 12–16 independent aortas. Statistical analyses were performed via Student’s t test. Asterisks indicate a significant difference with *** P < 0.001](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_5999/pmc11555999/pmc11555999__12933_2024_2502_Fig6_HTML.jpg)