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methylumbelliferyl 2 acetamido 2 deoxy α d galactopyranoside galnacα 4 mu  (Biosynth Carbosynth)


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    Structured Review

    Biosynth Carbosynth methylumbelliferyl 2 acetamido 2 deoxy α d galactopyranoside galnacα 4 mu
    a POGase screening strategy: Only POGases cleave the α2,3sialylCore 1 from α2,3sialylCore <t>1-(4-MU)</t> to release fluorescence 4-MU while all O-glycanases can cleave Core 1 from Core 1-(4-MU) to release fluorescence 4-MU. b Representative screening results: after incubating with substrate α2,3sialylCore 1-(4-MU), four of 13 candidates in a library of 30 uncharacterized and putative O-glycanases (#1–30, Supplementary Table ) were identified to release 4-MU which is fluorescent under UV light. c The candidates’ activities towards α2,3sialylCore 1-(4-MU) (left) and Core 1-(4-MU) (right) were measured respectively. Data are presented as mean values ± SD ( n = 2). d Representative screening results of 16 more putative O-glycanases: an expression library of 16 more putative POGases (#31–46, Supplementary Table ) with significant sequence similarity to the candidate #22 (termed POGase TB) was screened. Five more candidates, #31 (N01), #34 (N04), #37 (N07), #38 (N08), and #39 (N09) were identified to have significant fluorescence or activity and were shown. Activity comparison of POGase candidates: Enzymatic Reactions of 5 POGase candidates with significant activity to α2,3sialylCore 1-(4-MU) were compared. Data are presented as mean values ± SD ( n = 2). Source data are provided as a Source Data file.
    Methylumbelliferyl 2 Acetamido 2 Deoxy α D Galactopyranoside Galnacα 4 Mu, supplied by Biosynth Carbosynth, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/methylumbelliferyl 2 acetamido 2 deoxy α d galactopyranoside galnacα 4 mu/product/Biosynth Carbosynth
    Average 92 stars, based on 6 article reviews
    methylumbelliferyl 2 acetamido 2 deoxy α d galactopyranoside galnacα 4 mu - by Bioz Stars, 2026-02
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    1) Product Images from "Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities"

    Article Title: Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities

    Journal: Nature Communications

    doi: 10.1038/s41467-025-57143-8

    a POGase screening strategy: Only POGases cleave the α2,3sialylCore 1 from α2,3sialylCore 1-(4-MU) to release fluorescence 4-MU while all O-glycanases can cleave Core 1 from Core 1-(4-MU) to release fluorescence 4-MU. b Representative screening results: after incubating with substrate α2,3sialylCore 1-(4-MU), four of 13 candidates in a library of 30 uncharacterized and putative O-glycanases (#1–30, Supplementary Table ) were identified to release 4-MU which is fluorescent under UV light. c The candidates’ activities towards α2,3sialylCore 1-(4-MU) (left) and Core 1-(4-MU) (right) were measured respectively. Data are presented as mean values ± SD ( n = 2). d Representative screening results of 16 more putative O-glycanases: an expression library of 16 more putative POGases (#31–46, Supplementary Table ) with significant sequence similarity to the candidate #22 (termed POGase TB) was screened. Five more candidates, #31 (N01), #34 (N04), #37 (N07), #38 (N08), and #39 (N09) were identified to have significant fluorescence or activity and were shown. Activity comparison of POGase candidates: Enzymatic Reactions of 5 POGase candidates with significant activity to α2,3sialylCore 1-(4-MU) were compared. Data are presented as mean values ± SD ( n = 2). Source data are provided as a Source Data file.
    Figure Legend Snippet: a POGase screening strategy: Only POGases cleave the α2,3sialylCore 1 from α2,3sialylCore 1-(4-MU) to release fluorescence 4-MU while all O-glycanases can cleave Core 1 from Core 1-(4-MU) to release fluorescence 4-MU. b Representative screening results: after incubating with substrate α2,3sialylCore 1-(4-MU), four of 13 candidates in a library of 30 uncharacterized and putative O-glycanases (#1–30, Supplementary Table ) were identified to release 4-MU which is fluorescent under UV light. c The candidates’ activities towards α2,3sialylCore 1-(4-MU) (left) and Core 1-(4-MU) (right) were measured respectively. Data are presented as mean values ± SD ( n = 2). d Representative screening results of 16 more putative O-glycanases: an expression library of 16 more putative POGases (#31–46, Supplementary Table ) with significant sequence similarity to the candidate #22 (termed POGase TB) was screened. Five more candidates, #31 (N01), #34 (N04), #37 (N07), #38 (N08), and #39 (N09) were identified to have significant fluorescence or activity and were shown. Activity comparison of POGase candidates: Enzymatic Reactions of 5 POGase candidates with significant activity to α2,3sialylCore 1-(4-MU) were compared. Data are presented as mean values ± SD ( n = 2). Source data are provided as a Source Data file.

    Techniques Used: Fluorescence, Expressing, Sequencing, Activity Assay, Comparison

    a Expression and purification of recombinant POGase AS: The POGase AS with 6xHis tag at its C-terminus was recombinantly expressed in E. coli (BL21(DE3)) cells and purified with a Ni-NTA-column. SDS-PAGE with CBB staining and Western blot analysis of purified POGase AS were shown. The experiment was repeated three times independently with similar results. b Optimum pH: Activity of recombinant POGase AS toward α2,3sialylCore 1-(4-MU) was measured in enzymatic reactions under different pH conditions. Data are presented as mean values ± SD ( n = 2) in two independent experiments. c Kinetic parameters of recombinant POGase AS: kinetics of cleavage of Core 1-(4-MU), α2,3sialylCore 1-(4-MU), Core 2-(4-MU), and Core 3-(4-MU) by recombinant POGase AS were determined. Source data are provided as a Source Data file.
    Figure Legend Snippet: a Expression and purification of recombinant POGase AS: The POGase AS with 6xHis tag at its C-terminus was recombinantly expressed in E. coli (BL21(DE3)) cells and purified with a Ni-NTA-column. SDS-PAGE with CBB staining and Western blot analysis of purified POGase AS were shown. The experiment was repeated three times independently with similar results. b Optimum pH: Activity of recombinant POGase AS toward α2,3sialylCore 1-(4-MU) was measured in enzymatic reactions under different pH conditions. Data are presented as mean values ± SD ( n = 2) in two independent experiments. c Kinetic parameters of recombinant POGase AS: kinetics of cleavage of Core 1-(4-MU), α2,3sialylCore 1-(4-MU), Core 2-(4-MU), and Core 3-(4-MU) by recombinant POGase AS were determined. Source data are provided as a Source Data file.

    Techniques Used: Expressing, Purification, Recombinant, SDS Page, Staining, Western Blot, Activity Assay



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    Image Search Results


    a POGase screening strategy: Only POGases cleave the α2,3sialylCore 1 from α2,3sialylCore 1-(4-MU) to release fluorescence 4-MU while all O-glycanases can cleave Core 1 from Core 1-(4-MU) to release fluorescence 4-MU. b Representative screening results: after incubating with substrate α2,3sialylCore 1-(4-MU), four of 13 candidates in a library of 30 uncharacterized and putative O-glycanases (#1–30, Supplementary Table ) were identified to release 4-MU which is fluorescent under UV light. c The candidates’ activities towards α2,3sialylCore 1-(4-MU) (left) and Core 1-(4-MU) (right) were measured respectively. Data are presented as mean values ± SD ( n = 2). d Representative screening results of 16 more putative O-glycanases: an expression library of 16 more putative POGases (#31–46, Supplementary Table ) with significant sequence similarity to the candidate #22 (termed POGase TB) was screened. Five more candidates, #31 (N01), #34 (N04), #37 (N07), #38 (N08), and #39 (N09) were identified to have significant fluorescence or activity and were shown. Activity comparison of POGase candidates: Enzymatic Reactions of 5 POGase candidates with significant activity to α2,3sialylCore 1-(4-MU) were compared. Data are presented as mean values ± SD ( n = 2). Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities

    doi: 10.1038/s41467-025-57143-8

    Figure Lengend Snippet: a POGase screening strategy: Only POGases cleave the α2,3sialylCore 1 from α2,3sialylCore 1-(4-MU) to release fluorescence 4-MU while all O-glycanases can cleave Core 1 from Core 1-(4-MU) to release fluorescence 4-MU. b Representative screening results: after incubating with substrate α2,3sialylCore 1-(4-MU), four of 13 candidates in a library of 30 uncharacterized and putative O-glycanases (#1–30, Supplementary Table ) were identified to release 4-MU which is fluorescent under UV light. c The candidates’ activities towards α2,3sialylCore 1-(4-MU) (left) and Core 1-(4-MU) (right) were measured respectively. Data are presented as mean values ± SD ( n = 2). d Representative screening results of 16 more putative O-glycanases: an expression library of 16 more putative POGases (#31–46, Supplementary Table ) with significant sequence similarity to the candidate #22 (termed POGase TB) was screened. Five more candidates, #31 (N01), #34 (N04), #37 (N07), #38 (N08), and #39 (N09) were identified to have significant fluorescence or activity and were shown. Activity comparison of POGase candidates: Enzymatic Reactions of 5 POGase candidates with significant activity to α2,3sialylCore 1-(4-MU) were compared. Data are presented as mean values ± SD ( n = 2). Source data are provided as a Source Data file.

    Article Snippet: 4-Methylumbelliferyl 2-acetamido-2-deoxy-α-D-galactopyranoside [GalNAcα-(4-MU)] (Cat# EM04782) and CMP-Neu5Ac (sialic acid) (Cat# MC04391) were purchased from Biosynth Carbosynth (Berkshire, UK).

    Techniques: Fluorescence, Expressing, Sequencing, Activity Assay, Comparison

    a Expression and purification of recombinant POGase AS: The POGase AS with 6xHis tag at its C-terminus was recombinantly expressed in E. coli (BL21(DE3)) cells and purified with a Ni-NTA-column. SDS-PAGE with CBB staining and Western blot analysis of purified POGase AS were shown. The experiment was repeated three times independently with similar results. b Optimum pH: Activity of recombinant POGase AS toward α2,3sialylCore 1-(4-MU) was measured in enzymatic reactions under different pH conditions. Data are presented as mean values ± SD ( n = 2) in two independent experiments. c Kinetic parameters of recombinant POGase AS: kinetics of cleavage of Core 1-(4-MU), α2,3sialylCore 1-(4-MU), Core 2-(4-MU), and Core 3-(4-MU) by recombinant POGase AS were determined. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities

    doi: 10.1038/s41467-025-57143-8

    Figure Lengend Snippet: a Expression and purification of recombinant POGase AS: The POGase AS with 6xHis tag at its C-terminus was recombinantly expressed in E. coli (BL21(DE3)) cells and purified with a Ni-NTA-column. SDS-PAGE with CBB staining and Western blot analysis of purified POGase AS were shown. The experiment was repeated three times independently with similar results. b Optimum pH: Activity of recombinant POGase AS toward α2,3sialylCore 1-(4-MU) was measured in enzymatic reactions under different pH conditions. Data are presented as mean values ± SD ( n = 2) in two independent experiments. c Kinetic parameters of recombinant POGase AS: kinetics of cleavage of Core 1-(4-MU), α2,3sialylCore 1-(4-MU), Core 2-(4-MU), and Core 3-(4-MU) by recombinant POGase AS were determined. Source data are provided as a Source Data file.

    Article Snippet: 4-Methylumbelliferyl 2-acetamido-2-deoxy-α-D-galactopyranoside [GalNAcα-(4-MU)] (Cat# EM04782) and CMP-Neu5Ac (sialic acid) (Cat# MC04391) were purchased from Biosynth Carbosynth (Berkshire, UK).

    Techniques: Expressing, Purification, Recombinant, SDS Page, Staining, Western Blot, Activity Assay