| 包装 | 价格(元) |
| 10mM (in 1mL DMSO) | 电议 |
| 10mg | 电议 |
| 50mg | 电议 |
Kinase assays | Dehydrogenase activity was measured as conversion of NAD (1 mM) to NADH in the presence of formaldehyde, acetaldehyde, or propionaldehyde (1 mM each) by monitoring the change in absorbance at 340 nm at 25 ℃. The reactions were performed in 50 mM sodium pyrophosphate buffer (pH 9.0) containing 10 mM MgCl2 and 10 μM Alda-1 or 0.5% (v/v) DMSO as a vehicle control. |
Animal models | Mouse xenograft SCC VII tumor model |
Dosage form | Alda-1 (3 mM in 95% ethanol solution in a volume of 0.25 ml) was applied locally on the skin. |
Application | Concomitant topical application of the ALDH2 activator, Alda-1, effectively reduced the severity and delayed the onset of radiation-induced dermatitis in mice. Therefore, Alda-1, may be used as an adjunct to radiation therapy for the treatment of solid tumors in which radiation-induced dermatitis is an important clinical problem. |
Other notes | Please test the solubility of all compounds indoor, and the actual solubility may slightly differ with the theoretical value. This is caused by an experimental system error and it is normal. |
| 产品描述 | IC50: N/A Alda 1 is an activator of aldehyde dehydrogenase 2 (ALDH2). Alda 1 increases activity of wild-type ALDH2*1 and variant ALDH2*2 (by ~2-fold and 11-fold respectively), Capable of partly restoring mutant ALDH2*2 activity, and protective against cardiac ischemia. In vitro: In the present study , Alda-1 increased acetaldehyde oxidation by ALDH2*1 and ALDH2*2 approximately 1.5- and 6-fold, respectively, regarding GTN bioactivation and the effects of Alda-1. To similar extent, Alda-1 induced the esterase activities of both enzymes as the coenzyme NAD. NAD pronounced inhibition occurring at >5mM, its the effect was biphasic. In the presence of 1 mM NAD, Alda-1 induced ALDH2*2-catalyzed ester hydrolysis 73-fold, whereas the NAD-induced activity of ALDH2*1 was inhibited on account of 20-fold increased inhibitory potency of NAD in the presence of the drug. ALDH2*2 displayed 7-fold lower GTN denitrating activity and GTN affinity than ALDH2*1, but the rate of nitric oxide formation was only reduced 2-fold. Soluble guanylate cyclase (sGC) activation was more pronounced than with wild type ALDH2 at saturating GTN. Alda-1 caused slight inhibition of GTN denitration, and in the presence of either variant, GTN-induced sGC activation was increased. The present results imply that established ALDH2 activities stimulated by Alda-1, which improved NAD binding but does not improve the GTN binding affinity of the Asian variant. In addition, an unexpected discrepancy between GTN reductase activity and sGC activation was revealed, which suggested that GTN denitration and bioactivation may display independent pathways of ALDH2-catalyzed GTN biotransformation [1]. In vivo: Alda-1 (a high-throughput screen yielded a small-molecule activator of ALDH2, administered to rats before an ischemic event) reduced infarct size by 60%, most likely through the inhibition of the formation of cytotoxic aldehydes. Thus, pharmacologic enhancement of ALDH2 activity may be benefit to patients with wild-type or mutant ALDH2 who are subjected to cardiac ischemia, such as during coronary bypass surgery [2]. Clinical trial: Clinical study has been conducted. References: |
m.cnreagent.com