10 0 10 0 ps (Avanti Polar)
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Structured Review
Avanti Polar
10 0 10 0 ps
10 0 10 0 Ps, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/10 0 10 0 ps/product/Avanti Polar
Average 90 stars, based on 10 article reviews
10 0 10 0 Ps, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/10 0 10 0 ps/product/Avanti Polar
Average 90 stars, based on 10 article reviews
10 0 10 0 ps - by Bioz Stars,
2026-02
90/100 stars
Images
1) Product Images from "Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis"
Article Title: Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis
Journal: Scientific Reports
doi: 10.1038/s41598-021-85195-5
Figure Legend Snippet: Phospholipid-bound structures. ( A ) A scheme of NaCNBH 3 -dependent reduction of Schiff base. Ptd, phosphatidyl moiety ( B ) MALDI-ToF analysis of phospholipid conjugation on α-chain. The MS peaks of apo and modified α-chains are marked as gray dashed lines and black arrows for comparison of the m/z values. Observed and calculated m/z values of conjugates are 4925.6, 4926.6 (8:0/8:0 PE-conjugated), 4981.8, 4980.7 (10:0/10:0 PE-conjugated), and 5093.8, 5092.8 (14:0/14:0 PE-conjugated), respectively. ( C ) A zoomed-in view of linked phospholipid from 8PE-PSD (Left) and 10PE-PSD (Right). A Fo–Fc omit map of the phospholipid is illustrated as mesh contoured at 2.5 σ. Carbon atoms of the lipid are displayed in yellow, oxygen in red, nitrogen in blue, and phosphorous in purple. ( D ) Overlay of the acyl-chains of bound lipid in the hydrophobic pocket from all four subunits of 10PE-PSD structure. Hydrophobic residues surrounding the acyl-chains are labeled and highlighted as light blue stick.
Techniques Used: Conjugation Assay, Modification, Labeling
Figure Legend Snippet: Active site of PS decarboxylation. ( A ) Close-up views of the active site of 8PE-PSD (Left) and 10PE-PSD (Right). Hydrogen bonds and distances between amine group of reduced Schiff base and His-144 are shown in dashed lines with an averaged distance from all protomers in the asymmetric unit. ( B ) LC–MS analysis of the PS decarboxylation activity by the wild type and mutant proteins. Conversion rate was calculated by measuring the relative peak areas of 16:0/18:1 PS and 16:0/18:1 PE. Mean and standard deviation are plotted. Experiments were performed in triplicates. ( C ) Ligand conjugation assay of His-144 mutants. Ligand conjugation by NaCNBH 3 -dependent reduction was performed in H144A (A) or H144N (B) mutants. The conjugated α-chains were analyzed by MALDI-ToF. Theoretical m/z values of α-chains are 8261 Da (control), 8712 Da (8PE-conjugated), 8813 Da (10PS-conjugated), and 8925 Da (14PS-conjugated). The MS peaks of control and 8PE-conjugated α-chains are marked as gray dashed lines for comparison of m/z values. Theoretical mass difference of control and 8PE-conjugated α-chains is 450 Da.
Techniques Used: Liquid Chromatography with Mass Spectroscopy, Activity Assay, Mutagenesis, Standard Deviation, Conjugation Assay
Figure Legend Snippet: Proposed mechanism of PS decarboxylation and membrane association. ( A ) A scheme of decarboxylation after the formation of a Schiff base intermediate. A 10:0/10:0 acyl-chain of PS is depicted as a representative. Protein residues surrounding the substrate are colored in light blue and carboxylate of PS in red. ( B ) A model of membrane association of E. coli PSD, where core domains of PSD αβ-heterodimer are colored in cyan, and N-terminal helices in magenta. Pyruvoyl residues of the active site on each molecule are denoted as black stick. Inner membrane (IM) is shown in orange and brown.
Techniques Used:
