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rhsphk2  (R&D Systems)
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Fig. 4. Sphingolipidomic analysis after treatment with ARC39 in L929 cells. Cells were treated with 20 M of ARC39 for the indicated dura- tions and the endogenous levels of the following sphingolipids were determined by MS in whole-cell lysates: sphingomyelins (SMs) (A); ce- ramides (Cers) (B). Numbers indicate the chain length and saturation of the fatty acyl chain. C: dhSph, Sph, and S1P, respectively. D: Time-resolved fluorescence emission at 590 nm. Activity of rhSphK1 (left) and <t>rhSphK2</t> (right) was determined in real-time after pretreat- ment with ARC39 as indicated. The reaction mixture contained 30 M of NBD-C18-Sph, 150 nM of SphK1, or 6.9 nM of SphK2 with or without 1 mM of ATP. Data are represented as mean ± SD, n = 3 experiments. Two-way ANOVA was used followed by Bonferroni correction. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.
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Fig. 4. Sphingolipidomic analysis after treatment with ARC39 in L929 cells. Cells were treated with 20 M of ARC39 for the indicated dura- tions and the endogenous levels of the following sphingolipids were determined by MS in whole-cell lysates: sphingomyelins (SMs) (A); ce- ramides (Cers) (B). Numbers indicate the chain length and saturation of the fatty acyl chain. C: dhSph, Sph, and S1P, respectively. D: Time-resolved fluorescence emission at 590 nm. Activity of rhSphK1 (left) and rhSphK2 (right) was determined in real-time after pretreat- ment with ARC39 as indicated. The reaction mixture contained 30 M of NBD-C18-Sph, 150 nM of SphK1, or 6.9 nM of SphK2 with or without 1 mM of ATP. Data are represented as mean ± SD, n = 3 experiments. Two-way ANOVA was used followed by Bonferroni correction. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Journal: Journal of Lipid Research

Article Title: Characterization of the small molecule ARC39, a direct and specific inhibitor of acid sphingomyelinase in vitro

doi: 10.1194/jlr.ra120000682

Figure Lengend Snippet: Fig. 4. Sphingolipidomic analysis after treatment with ARC39 in L929 cells. Cells were treated with 20 M of ARC39 for the indicated dura- tions and the endogenous levels of the following sphingolipids were determined by MS in whole-cell lysates: sphingomyelins (SMs) (A); ce- ramides (Cers) (B). Numbers indicate the chain length and saturation of the fatty acyl chain. C: dhSph, Sph, and S1P, respectively. D: Time-resolved fluorescence emission at 590 nm. Activity of rhSphK1 (left) and rhSphK2 (right) was determined in real-time after pretreat- ment with ARC39 as indicated. The reaction mixture contained 30 M of NBD-C18-Sph, 150 nM of SphK1, or 6.9 nM of SphK2 with or without 1 mM of ATP. Data are represented as mean ± SD, n = 3 experiments. Two-way ANOVA was used followed by Bonferroni correction. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Article Snippet: Assays were initiated with 20× ATP [20 mM ATP, 200 mM MgCl2, 900 mM Tris-HCl (pH 7.4)] followed by shaking and mixing for 15 s. Assays were prepared as master mixes immediately before use in either SphK1 or SphK2 reaction buffer containing 30 M of NBD-Sph, 150 nM of rhSphK1 (R&D Systems, 5536-SK-010), or 6.9 nM of rhSphK2 (R&D Systems, 5298-SK-010).

Techniques: Fluorescence, Activity Assay