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Eliglustat-d15 (tartrate) Sale

(Synonyms: Genz 99067-d15 tartrate) 目录号 : GC47286

An internal standard for the quantification of eliglustat

Eliglustat-d15 (tartrate) Chemical Structure

Cas No.:1884556-84-6

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1 mg
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产品描述

Eliglustat-d15 is intended for use as an internal standard for the quantification of eliglustat by GC- or LC-MS. Eliglustat is an inhibitor of glucosylceramide synthase (IC50 = 40 nM for inhibition of glucosylceramide production in K562 cells).1 It is selective for glucosylceramide synthase over α-glucosidase I and II, α-1,6-glucosidase, lysosomal glucocerebrosidase, non-lysosomal glucosylceramidase, sucrase, and maltase (IC50s = >10 µM for all). It decreases cell surface levels of the gangliosides GM1 and GM3 in K562 and B16/F10 cells with IC50 values of 24 and 29 nM, respectively. Eliglustat (150 mg/kg per day) decreases glucosylceramide levels in the liver and lungs of D409V/null mice, a model of Gaucher disease. Formulations containing eliglustat have been used in the treatment of type 1 Gaucher disease.

1.McEachern, K.A., Fung, J., Komarnitsky, S., et al.A specific and potent inhibitor of glucosylceramide synthase for substrate inhibition therapy of Gaucher diseaseMol. Genet. Metab.91(3)259-267(2007)

Chemical Properties

Cas No. 1884556-84-6 SDF
别名 Genz 99067-d15 tartrate
Canonical SMILES O[C@@H]([C@H](NC(C([2H])([2H])C([2H])([2H])C([2H])([2H])C([2H])([2H])C([2H])([2H])C([2H])([2H])C([2H])([2H])[2H])=O)CN1CCCC1)C2=CC=C(OCCO3)C3=C2.OC([C@H](O)[C@@H](O)C(O)=O)=O
分子式 C23H21D15N2O4.C4H6O6 分子量 569.7
溶解度 DMSO: soluble,Methanol: soluble,Water: soluble 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 1.7553 mL 8.7765 mL 17.5531 mL
5 mM 0.3511 mL 1.7553 mL 3.5106 mL
10 mM 0.1755 mL 0.8777 mL 1.7553 mL
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Research Update

Calcium tartrate gel

Anal Biochem 1989 May 15;179(1):86-9.PMID:2757203DOI:10.1016/0003-2697(89)90205-4.

A method for preparation of a gel for chromatography has been developed. The adsorbent is calcium tartrate treated with potassium phosphate. By changing the temperature of synthesis (10-65 degrees C) and concentration of the salts (calcium chloride and sodium potassium tartrate) from 0.3 to 3.0 M, we have been able to prepare adsorbent crystals of definite sizes in the range 35-200 microns. In all cases, for synthesis of adsorbent, the Ca2+/K+Na+ ratio was greater than 1. After treatment of calcium tartrate crystals with 0.075-1.5 M potassium phosphate at 80-100 degrees C and pH 8.5-9.0, an appropriate chromatographic adsorbent was prepared. The chromatographic properties of calcium tartrate gel have been studied. The adsorbent permits flow rates of 25-150 ml/h, depending on the particle size. The capacity of calcium tartrate gel for binding BSA, RNA, and DNA was similar to that of Tiselius' hydroxyapatite (A. Tiselius, S. Hjerten, O. Levin (1956) Arch. Biochem. Biophys. 65, 132-155). The spheric shape of gel particles permits uniform and compact packing of adsorbent under the conditions of column chromatography.

Investigation of radiation sensitivity of some tartrate compounds

Radiat Prot Dosimetry 2014 Jun;159(1-4):199-202.PMID:24736299DOI:10.1093/rpd/ncu119.

Potential electron spin resonance (ESR) dosimetric application of different compounds of sodium tartrate, such as sodium tartrate dihydrate, sodium bitartrate monohydrate and potassium sodium tartrate tetrahydrate, was investigated in the range of 0.74-25 Gy. While the radiation-induced intermediates produced in these compounds are similar, their radiation yields are different. It is found that the radiation yield of sodium tartrate dihydrate is higher than other compounds of sodium tartrates. Comparison of the radiation yields were also made between well-known samples of ammonium tartrate, alanine and lithium formate. It is found that the radiation yields of sodium tartrate dihydrate, sodium bitartrate monohydrate and potassium sodium tartrate tetrahydrate have the values of 1.22, 0.18 and 0.13, respectively.

Inhibitory effect of tartrate against phosphate-induced DJ-1 aggregation

Int J Biol Macromol 2018 Feb;107(Pt B):1650-1658.PMID:29030185DOI:10.1016/j.ijbiomac.2017.10.022.

The DJ-1 protein engages in diverse cellular and pathological processes, including tumorigenesis, apoptosis, sperm fertilization, and the progression of Parkinson's disease (PD). The functional dimeric form of DJ-1 transforms into non-functional filamentous aggregates in an inorganic phosphate (Pi)-dependent manner in vitro. Here, we demonstrated that Pi and reactive oxygen species (ROS) induce DJ-1 aggregation in Neuro2A and SH-SY5Y cells. Remarkably, tartrate treatment significantly reduced Pi- and ROS-induced DJ-1 aggregation and restored Pi- and ROS-provoked cell death using quantitative data as mean±standard deviation, and statistics. Mechanistically, tartrate prevented DJ-1 aggregation via occupying the Pi-binding site. These findings revealed an unexpected physiological role of tartrate in the maintenance of DJ-1 function, and thus, a potential use as an inhibitor of DJ-1 aggregation.

The L-tartrate/succinate antiporter TtdT (YgjE) of L-tartrate fermentation in Escherichia coli

J Bacteriol 2007 Mar;189(5):1597-603.PMID:17172328DOI:10.1128/JB.01402-06.

Escherichia coli ferments L-tartrate under anaerobic conditions in the presence of an additional electron donor to succinate. The carrier for L-tartrate uptake and succinate export and its relation to the general C(4)-dicarboxylate carriers DcuA, DcuB, and DcuC were studied. The secondary carrier TtdT, encoded by the ttdT (previously called ygjE) gene, is required for the uptake of L-tartrate. The ttdT gene is located downstream of the ttdA and ttdB genes, encoding the L-tartrate dehydratase TtdAB. Analysis of mRNA by reverse transcription-PCR showed that ttdA, ttdB, and ttdT are cotranscribed. Deletion of ttdT abolished growth by L-tartrate and degradation of L-tartrate completely. Bacteria containing TtdT catalyze L-tartrate or succinate uptake and specific heterologous L-tartrate/succinate antiporting. D-Tartrate is not a substrate for TtdT. TtdT operates preferentially in the direction of tartrate uptake and succinate excretion. The Dcu carriers do not support anaerobic growth on L-tartrate or L-tartrate transport. TtdT is related in sequence and function to CitT, which catalyzes heterologous citrate/succinate antiporting in citrate fermentation.

Tuning the shell structure of peptide nanotubes with sodium tartrate: From monolayer to bilayer

J Colloid Interface Sci 2022 Feb 15;608(Pt 2):1685-1695.PMID:34742083DOI:10.1016/j.jcis.2021.10.023.

Though the function of peptide based nanotubes are well correlated with its shape and size, controlling the dimensions of nanotubes still remains a great challenge in the field of peptide self-assembly. Here, we demonstrated that the shell structure of nanotubes formed by a bola peptide Ac-KI3VK-NH2 (KI3VK, in which K, I, and V are abbreviations of lysine, isoleucine, and valine) can be regulated by mixing it with the salt sodium tartrate (STA). The ratio of KI3VK and STA had a great impact on shell structure of the nanotubes. Bilayer nanotubes can be constructed when the molar ratio of KI3VK and STA was less than 1:2. Both the two hydroxyls and the negative charges carried by STA were proved to play important roles in the bilayer nanotubes formation. Observations of different intermediates provided obvious evidence for the varied pathway of the bilayer nanotubes formation. Based on these experimental results, the possible mechanism for bilayer nanotubes formation was proposed. Such a study provides a simple and effective way for regulating the shell structure of the nanotubes and may expand their applications in different fields.