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serum complement  (MedChemExpress)


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    Structured Review

    MedChemExpress serum complement
    A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of <t>complement.</t> Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.
    Serum Complement, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hy-p1036/Compstatin/bio_rxiv__2025__02__01__636076-226-0-6
    Average 94 stars, based on 6 article reviews
    serum complement - by Bioz Stars, 2026-10
    94/100 stars

    Images

    1) Product Images from "Sialidases derived from Gardnerella vaginalis remodel the sperm glycocalyx and impair sperm function"

    Article Title: Sialidases derived from Gardnerella vaginalis remodel the sperm glycocalyx and impair sperm function

    Journal: bioRxiv

    doi: 10.1101/2025.02.01.636076

    A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of complement. Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.
    Figure Legend Snippet: A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of complement. Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.

    Techniques Used: Comparison, Staining

    Related Articles

    Incubation:

    Article Title: Sialidases derived from Gardnerella vaginalis remodel the sperm glycocalyx and impair sperm function
    Article Snippet: .. Serum complement and compstatin (C3 inhibitor) (MedChemExpress, USA) were incubated together for 15 mins at room temperature and then sialidase treated sperm were added as previously described. ..

    other:

    Article Title: Sialidases derived from Gardnerella vaginalis and Prevotella timonensis remodel the sperm glycocalyx and impair sperm function.
    Article Snippet: UN CO RR EC TE D MA NU SC RI PT Title: Sialidases derived from Gardnerella vaginalis and Prevotella timonensis remodel the sperm glycocalyx and impair sperm function Keywords: bacterial vaginosis/infertility/reproductive immunology/sialidase/sperm © The Author(s) 2025.. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints.. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.



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    The Role of Complement in JIPh_Ec70 and JIPh_Kp127 Internalisation. (A) Comparison of SYBR‐labelled JIPh_Ec70 and JIPh_Kp127 monocyte internalization over a 4 h time‐course ( n = 6). (B) Ec70 and Kp127 phage internalization following inhibition of complement using <t>compstatin</t> (C3 inhibitor) or heat inactivation. Intracellular phage was measured by flow cytometry (SYBR labeling), plaque‐forming units (viable phage), and qPCR (intracellular genomes) ( n = 8 ). (C) C3 internalization was quantified by flow cytometry in phage+ and phage‐monocytes following complement inactivation using compstatin and heat inactivation ( n = 7 ). (D) Immunofluorescent imaging of monocytes treated with SYBR‐labelled phages (green) ± C3 inhibitor compstatin. Internalized C3 was labelled in red and cell nucleus in blue. Detected phages and C3 marked with a white arrow, scale bar = 2 µm. Data presented with mean ± SEM, a paired t ‐test, (E, F) RM two‐way ANOVA test, * p < 0.05, ** p < 0.01 *** p < 0.001, **** p < 0.0001. C3, complement factor 3; MFI, median fluorescent intensity; PFU, plaque‐forming unit.
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    The Role of Complement in JIPh_Ec70 and JIPh_Kp127 Internalisation. (A) Comparison of SYBR‐labelled JIPh_Ec70 and JIPh_Kp127 monocyte internalization over a 4 h time‐course ( n = 6). (B) Ec70 and Kp127 phage internalization following inhibition of complement using <t>compstatin</t> (C3 inhibitor) or heat inactivation. Intracellular phage was measured by flow cytometry (SYBR labeling), plaque‐forming units (viable phage), and qPCR (intracellular genomes) ( n = 8 ). (C) C3 internalization was quantified by flow cytometry in phage+ and phage‐monocytes following complement inactivation using compstatin and heat inactivation ( n = 7 ). (D) Immunofluorescent imaging of monocytes treated with SYBR‐labelled phages (green) ± C3 inhibitor compstatin. Internalized C3 was labelled in red and cell nucleus in blue. Detected phages and C3 marked with a white arrow, scale bar = 2 µm. Data presented with mean ± SEM, a paired t ‐test, (E, F) RM two‐way ANOVA test, * p < 0.05, ** p < 0.01 *** p < 0.001, **** p < 0.0001. C3, complement factor 3; MFI, median fluorescent intensity; PFU, plaque‐forming unit.
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    MedChemExpress serum complement
    A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of <t>complement.</t> Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.
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    MedChemExpress compstatin amy 101
    A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of <t>complement.</t> Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.
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    Image Search Results


    The Role of Complement in JIPh_Ec70 and JIPh_Kp127 Internalisation. (A) Comparison of SYBR‐labelled JIPh_Ec70 and JIPh_Kp127 monocyte internalization over a 4 h time‐course ( n = 6). (B) Ec70 and Kp127 phage internalization following inhibition of complement using compstatin (C3 inhibitor) or heat inactivation. Intracellular phage was measured by flow cytometry (SYBR labeling), plaque‐forming units (viable phage), and qPCR (intracellular genomes) ( n = 8 ). (C) C3 internalization was quantified by flow cytometry in phage+ and phage‐monocytes following complement inactivation using compstatin and heat inactivation ( n = 7 ). (D) Immunofluorescent imaging of monocytes treated with SYBR‐labelled phages (green) ± C3 inhibitor compstatin. Internalized C3 was labelled in red and cell nucleus in blue. Detected phages and C3 marked with a white arrow, scale bar = 2 µm. Data presented with mean ± SEM, a paired t ‐test, (E, F) RM two‐way ANOVA test, * p < 0.05, ** p < 0.01 *** p < 0.001, **** p < 0.0001. C3, complement factor 3; MFI, median fluorescent intensity; PFU, plaque‐forming unit.

    Journal: European Journal of Immunology

    Article Title: Differences in Phage Recognition and Immunogenicity Contribute to Divergent Human Immune Responses to Escherichia coli and Klebsiella pneumoniae Phages

    doi: 10.1002/eji.202451543

    Figure Lengend Snippet: The Role of Complement in JIPh_Ec70 and JIPh_Kp127 Internalisation. (A) Comparison of SYBR‐labelled JIPh_Ec70 and JIPh_Kp127 monocyte internalization over a 4 h time‐course ( n = 6). (B) Ec70 and Kp127 phage internalization following inhibition of complement using compstatin (C3 inhibitor) or heat inactivation. Intracellular phage was measured by flow cytometry (SYBR labeling), plaque‐forming units (viable phage), and qPCR (intracellular genomes) ( n = 8 ). (C) C3 internalization was quantified by flow cytometry in phage+ and phage‐monocytes following complement inactivation using compstatin and heat inactivation ( n = 7 ). (D) Immunofluorescent imaging of monocytes treated with SYBR‐labelled phages (green) ± C3 inhibitor compstatin. Internalized C3 was labelled in red and cell nucleus in blue. Detected phages and C3 marked with a white arrow, scale bar = 2 µm. Data presented with mean ± SEM, a paired t ‐test, (E, F) RM two‐way ANOVA test, * p < 0.05, ** p < 0.01 *** p < 0.001, **** p < 0.0001. C3, complement factor 3; MFI, median fluorescent intensity; PFU, plaque‐forming unit.

    Article Snippet: To investigate the role of complement factor 3 (C3) in phage internalization, monocytes were preincubated with 50 μM compstatin (MedchemExpress, # HY‐P1036) for 15 min in media with serum before treating with phages.

    Techniques: Comparison, Inhibition, Flow Cytometry, Labeling, Imaging

    A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of complement. Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.

    Journal: bioRxiv

    Article Title: Sialidases derived from Gardnerella vaginalis remodel the sperm glycocalyx and impair sperm function

    doi: 10.1101/2025.02.01.636076

    Figure Lengend Snippet: A) Sperm motility was measured after sialidase treatment (2000ng/mL NanH2 and 250 ng/mL AUS) via computer assisted sperm analysis (CASA). Statistics represent a repeated measures comparison; neither time nor enzyme condition was a significant source of variation. B) Sperm motility was measured after treatment with GvNanH2 sialidase in the presence of complement. Heat-inactivated complement and 125 uM compstatin (a human C3 inhibitor) were used as negative controls. C) A representative image of a sperm agglutinate after treatment with NanH2 sialidase and complement for 1 hour. Sperm were stained with trypan blue to detect cell death. Dead sperm were observed, along with motile live sperm (sometimes seen as tracks in the images due to movement). D) Same as B), but with AUS sialidase. Statistics represent mixed model comparisons with post-hoc Tukey tests.

    Article Snippet: Serum complement and compstatin (C3 inhibitor) (MedChemExpress, USA) were incubated together for 15 mins at room temperature and then sialidase treated sperm were added as previously described.

    Techniques: Comparison, Staining