830071P Search Results


substrates  (Croda International Plc)
94
Croda International Plc substrates
Enzymatic activity of recombinant PLDs upon SM and LysoPC measured by Amplex Red TM assay. ( A ) Enzymatic activity of LiRecDT1, LlRecDT1, and LgRecDT1 upon SM depicted in a time-dependent analysis. ( B ) Enzymatic activity of LiRecDT1, LlRecDT1, and LgRecDT1 on LysoPC depicted in a time-dependent analysis. For both <t>substrates,</t> the product of reaction (choline) was fluorometrically measured by excitation at 540 nm and emission at 570 nm. Negative control was performed by incubation of Amplex Red reagent mixture without PLDs. The values represent average ± SEM of five independent experiments carried out in triplicate (*** p < 0.001). Statistical analyses compared the values corresponding to LgRecDT1 with those from LiRecDT1 and LlRecDT1.
Substrates, supplied by Croda International Plc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/substrates/product/Croda International Plc
Average 94 stars, based on 1 article reviews
substrates - by Bioz Stars, 2026-04
94/100 stars
  Buy from Supplier

Image Search Results


Enzymatic activity of recombinant PLDs upon SM and LysoPC measured by Amplex Red TM assay. ( A ) Enzymatic activity of LiRecDT1, LlRecDT1, and LgRecDT1 upon SM depicted in a time-dependent analysis. ( B ) Enzymatic activity of LiRecDT1, LlRecDT1, and LgRecDT1 on LysoPC depicted in a time-dependent analysis. For both substrates, the product of reaction (choline) was fluorometrically measured by excitation at 540 nm and emission at 570 nm. Negative control was performed by incubation of Amplex Red reagent mixture without PLDs. The values represent average ± SEM of five independent experiments carried out in triplicate (*** p < 0.001). Statistical analyses compared the values corresponding to LgRecDT1 with those from LiRecDT1 and LlRecDT1.

Journal: International Journal of Molecular Sciences

Article Title: Comparative Biochemical, Structural, and Functional Analysis of Recombinant Phospholipases D from Three Loxosceles Spider Venoms

doi: 10.3390/ijms241512006

Figure Lengend Snippet: Enzymatic activity of recombinant PLDs upon SM and LysoPC measured by Amplex Red TM assay. ( A ) Enzymatic activity of LiRecDT1, LlRecDT1, and LgRecDT1 upon SM depicted in a time-dependent analysis. ( B ) Enzymatic activity of LiRecDT1, LlRecDT1, and LgRecDT1 on LysoPC depicted in a time-dependent analysis. For both substrates, the product of reaction (choline) was fluorometrically measured by excitation at 540 nm and emission at 570 nm. Negative control was performed by incubation of Amplex Red reagent mixture without PLDs. The values represent average ± SEM of five independent experiments carried out in triplicate (*** p < 0.001). Statistical analyses compared the values corresponding to LgRecDT1 with those from LiRecDT1 and LlRecDT1.

Article Snippet: LiRecDT1, LlRecDT1, and LgRecDT1 (2.5 μg each, in five trials) were added to the Amplex Red reagent mixture containing 250 μM (in 0.01% Triton X-100) of the substrates (egg sphingomyelin and l-α-lysophosphatidylcholine (egg lyso PC) from Avanti Polar Lipids, Inc. Alabaster, AL, USA).

Techniques: Activity Assay, Recombinant, Negative Control, Incubation

Enzymatic activity of recombinant PLDs upon SM and LysoPC analyzed by HPTLC. ( A ) The bands of substrates and products formed after incubation with LiRecDT1 (letter I), LlRecDT1 (letter L), and LgRecDT1 (letter G) and analyzed in silica gel plates are depicted after reaction with molybdenum blue. ( B ) Band intensities for substrates and generated products were estimated densitometrically and the percentages of degradation were normalized on the basis of the intensity of the bands from untreated substrates (considered 100%).

Journal: International Journal of Molecular Sciences

Article Title: Comparative Biochemical, Structural, and Functional Analysis of Recombinant Phospholipases D from Three Loxosceles Spider Venoms

doi: 10.3390/ijms241512006

Figure Lengend Snippet: Enzymatic activity of recombinant PLDs upon SM and LysoPC analyzed by HPTLC. ( A ) The bands of substrates and products formed after incubation with LiRecDT1 (letter I), LlRecDT1 (letter L), and LgRecDT1 (letter G) and analyzed in silica gel plates are depicted after reaction with molybdenum blue. ( B ) Band intensities for substrates and generated products were estimated densitometrically and the percentages of degradation were normalized on the basis of the intensity of the bands from untreated substrates (considered 100%).

Article Snippet: LiRecDT1, LlRecDT1, and LgRecDT1 (2.5 μg each, in five trials) were added to the Amplex Red reagent mixture containing 250 μM (in 0.01% Triton X-100) of the substrates (egg sphingomyelin and l-α-lysophosphatidylcholine (egg lyso PC) from Avanti Polar Lipids, Inc. Alabaster, AL, USA).

Techniques: Activity Assay, Recombinant, High Performance Thin Layer Chromatography, Incubation, Generated