sialidase  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97
    Name:
    O Glycosidase and Neuraminidase Bundle
    Description:
    O Glycosidase and Neuraminidase Bundle
    Catalog Number:
    e0540s
    Price:
    191
    Category:
    Glycosidases
    Buy from Supplier


    Structured Review

    New England Biolabs sialidase
    O Glycosidase and Neuraminidase Bundle
    O Glycosidase and Neuraminidase Bundle
    https://www.bioz.com/result/sialidase/product/New England Biolabs
    Average 97 stars, based on 22 article reviews
    Price from $9.99 to $1999.99
    sialidase - by Bioz Stars, 2020-08
    97/100 stars

    Images

    1) Product Images from "Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure"

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0150210

    Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from sialidase-treated LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p
    Figure Legend Snippet: Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from sialidase-treated LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p

    Techniques Used: Staining, Polyacrylamide Gel Electrophoresis, Western Blot, Recombinant, Negative Control, Expressing, Real-time Polymerase Chain Reaction, Immunoprecipitation, SDS Page

    Altered mucin-type O -glycosylation in the LV of DS hypertensive rats. (A) T-synthase activity in LV extracts. Data were normalized to protein content. (B) Correlation of T-synthase activity with ANP gene expression. ANP gene expression level was quantified by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (C) Correlation of T-synthase activity with ejection fraction. (D) Relative expression levels of glycogenes involved in the early stage of mucin-type O -glycosylation in the LV tissues of DS rats were analyzed by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (E) Schematic summary of gene expression analysis data shown in (D). Examined glycosyltransferases in the mucin-type O -glycosylation pathway are shown in red (upregulated), blue (downregulated), or black (no change) letters. Relatively rare core structures (core 5, 6, 7, and 8) synthesized from Tn are omitted. The biosynthetic pathway of disialyl-T is upregulated, as indicated with bold arrows. GalNAc, N -acetylgalactosamine; GlcNAc, N -acetylglucosamine; Gal, galactose; NeuAc, N -acetylneuraminic acid. (F) Lectin blot analysis of sialidase-treated LV extracts using ACA. Representative images demonstrate ACA-reactive glycoproteins and SYPRO Ruby-stained total proteins of three individual rats in each group. Lower panel shows densitometry analysis; intensity of each band was normalized to total protein amount. Data are presented as the fold change (n = 6) compared with sialidase-untreated LV extracts of HS rats at 12 weeks. (A,D) The numbers of examined rats were n = 12 and n = 15 for the HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (A,D,F) *, p
    Figure Legend Snippet: Altered mucin-type O -glycosylation in the LV of DS hypertensive rats. (A) T-synthase activity in LV extracts. Data were normalized to protein content. (B) Correlation of T-synthase activity with ANP gene expression. ANP gene expression level was quantified by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (C) Correlation of T-synthase activity with ejection fraction. (D) Relative expression levels of glycogenes involved in the early stage of mucin-type O -glycosylation in the LV tissues of DS rats were analyzed by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (E) Schematic summary of gene expression analysis data shown in (D). Examined glycosyltransferases in the mucin-type O -glycosylation pathway are shown in red (upregulated), blue (downregulated), or black (no change) letters. Relatively rare core structures (core 5, 6, 7, and 8) synthesized from Tn are omitted. The biosynthetic pathway of disialyl-T is upregulated, as indicated with bold arrows. GalNAc, N -acetylgalactosamine; GlcNAc, N -acetylglucosamine; Gal, galactose; NeuAc, N -acetylneuraminic acid. (F) Lectin blot analysis of sialidase-treated LV extracts using ACA. Representative images demonstrate ACA-reactive glycoproteins and SYPRO Ruby-stained total proteins of three individual rats in each group. Lower panel shows densitometry analysis; intensity of each band was normalized to total protein amount. Data are presented as the fold change (n = 6) compared with sialidase-untreated LV extracts of HS rats at 12 weeks. (A,D) The numbers of examined rats were n = 12 and n = 15 for the HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (A,D,F) *, p

    Techniques Used: Activity Assay, Aqueous Normal-phase Chromatography, Expressing, Real-time Polymerase Chain Reaction, Synthesized, Staining

    Related Articles

    Western Blot:

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits
    Article Snippet: .. Where indicated, the streptavidin bead-adherent proteins were treated with O- glycosidase & Neuraminidase Bundle (New England BioLabs) as described by the manufacturer and analyzed by western blotting. .. A549 cells were transfected with 120 pmol of human FXYD5 siRNA duplex (final concentration 100 µM) (Santa Cruz Biotechnology) using Lipofectamine RNAiMAX (Invitrogen).

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure
    Article Snippet: .. Protein deglycosylation LV extracts prepared for western blot and lectin blot analyses and recombinant proteins were treated with glycosidases, including sialidase, O -glycosidase, and PNGase F, which were all obtained from New England Biolabs (Beverly, MA). ..

    Incubation:

    Article Title: Proteomic analysis of skeletal organic matrix from the stony coral Stylophora pistillata
    Article Snippet: .. Both fractions were incubated at 4 °C overnight, centrifuged at 10,000 × g at 4 °C for 30 min, washed twice with ice-cold 90% (vol/vol) acetone at 4 °C for 15 min, and centrifuged at 10,000 × g at 4 °C for 30 min. Additionally, SOM proteins were enzymatically deglycosylated with O-glycosidase, N -glycosidase F, sialidase, B1-4 galactosidase, and B- N -acetylglucosaminidase in a deglycosylation mix per manufacturer instructions (New England BioLabs). .. SOM proteins were separated by SDS/PAGE and bands were visualized by silver staining (Pierce silver stain for mass spectrometry) and Periodic acid-Schiff staining (Pierce glycoprotein staining kit).

    Article Title: Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains
    Article Snippet: .. Deglycosylation of chimeric MC-IgYs Chimeric MC-IgY proteins (5 μg) were incubated with a deglycosylation enzyme mixture (New England Biolabs) containing O-glycosidase, PNGase F, neuraminidase (sialidase), β1–4 galactosidase, and β-N-acetylglucosaminidase for 4 h at 37 °C according to the manufacturer’s guidelines (New England Biolabs; cat# P6039S). .. Periodic acid-Schiff (PAS) staining of chimeric MC-IgYs Chimeric MC-IgY proteins (5 μg), before and after reaction with a deglycosylation enzyme cocktail, were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and PAS staining was performed to detect protein-bound carbohydrates using a glycoprotein staining kit according to the manufacturer’s instructions (ThermoFisher Scientific; cat# 24562).

    other:

    Article Title: Analysis of N- and O-Glycosylation of Lysosomal Glycoproteins
    Article Snippet: Enzymes: Peptide- N -Glycosidase F (PNGase F) from Flavobacterium meningosepticum (New England BioLabs), endoglycosidase H (Endo H) from Streptomyces plicatus (Glyco-Prozyme Inc.), Jack bean α-Mannosidase (Sigma-Aldrich) and O -glycosidase & Neuraminidase Bundle (New England BioLabs).

    Recombinant:

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure
    Article Snippet: .. Protein deglycosylation LV extracts prepared for western blot and lectin blot analyses and recombinant proteins were treated with glycosidases, including sialidase, O -glycosidase, and PNGase F, which were all obtained from New England Biolabs (Beverly, MA). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97
    New England Biolabs sialidase
    Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from <t>sialidase-treated</t> LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p
    Sialidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sialidase/product/New England Biolabs
    Average 97 stars, based on 21 article reviews
    Price from $9.99 to $1999.99
    sialidase - by Bioz Stars, 2020-08
    97/100 stars
      Buy from Supplier

    Image Search Results


    Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from sialidase-treated LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p

    Journal: PLoS ONE

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure

    doi: 10.1371/journal.pone.0150210

    Figure Lengend Snippet: Altered O -glycosylation on CSRP3 in the LV of DS hypertensive rats. (A) ACA lectin blot analysis and SYPRO Ruby staining of fractions from sialidase-treated LV extracts. Arrow indicates the ACA-positive band, which is observed strongly in fraction 3 of HS ( H ) but weakly in that of the LS ( L ) group. (B) Two-dimensional PAGE images of sialidase-treated LV fraction 3. Proteins transferred to membranes were subjected to SYPRO Ruby staining, and then to ACA lectin blotting. Insets show magnified images of two spots used for protein identification. (C) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of recombinant human CSRP3. Recombinant proteins expressed in E . coli (unglycosylated negative control) and in HEK293 cells (potentially glycosylated reference) were analyzed after treatment with sialidase and O -glycosidase. (D) Relative expression levels of Csrp3 in the LV tissues. qPCR data were normalized to Tbp expression levels. The numbers of examined rats were n = 12 and n = 15 for HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (E) Protein levels of CSRP3 in LV extracts. Densitometry analysis data of western blotting are shown (n = 6). (D,E) The data are presented as the fold change compared with LS rats at 12 weeks. (F) Western blot ( WB ) and ACA lectin blot ( LB ) analyses of CSRP3 from LV extracts of DS rats. CSRP3 in LV extracts was immunoprecipitated, denatured, separated by SDS-PAGE, and analyzed. Recombinant human CSRP3 was used as an experimental control of immunoprecipitation with anti-CSRP3 antibody (+) or normal IgG (-). Lower panel shows densitometry analysis data; the intensity of each band in LB was normalized to that in WB (n = 6). (G) Effects of glycosidases on CSRP3 dimerization. LV extracts from three HS ( H ) or LS ( L ) rats at 16 weeks were treated with three glycosidases as indicated and then analyzed by western blotting for CSRP3. Arrows indicate the bands corresponding to monomers and dimers. Lower panels show densitometry analysis from five experiments; dimer/monomer ratios are presented as the fold change compared with LS rats without glycosidase treatment. (D-G) *, p

    Article Snippet: Protein deglycosylation LV extracts prepared for western blot and lectin blot analyses and recombinant proteins were treated with glycosidases, including sialidase, O -glycosidase, and PNGase F, which were all obtained from New England Biolabs (Beverly, MA).

    Techniques: Staining, Polyacrylamide Gel Electrophoresis, Western Blot, Recombinant, Negative Control, Expressing, Real-time Polymerase Chain Reaction, Immunoprecipitation, SDS Page

    Altered mucin-type O -glycosylation in the LV of DS hypertensive rats. (A) T-synthase activity in LV extracts. Data were normalized to protein content. (B) Correlation of T-synthase activity with ANP gene expression. ANP gene expression level was quantified by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (C) Correlation of T-synthase activity with ejection fraction. (D) Relative expression levels of glycogenes involved in the early stage of mucin-type O -glycosylation in the LV tissues of DS rats were analyzed by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (E) Schematic summary of gene expression analysis data shown in (D). Examined glycosyltransferases in the mucin-type O -glycosylation pathway are shown in red (upregulated), blue (downregulated), or black (no change) letters. Relatively rare core structures (core 5, 6, 7, and 8) synthesized from Tn are omitted. The biosynthetic pathway of disialyl-T is upregulated, as indicated with bold arrows. GalNAc, N -acetylgalactosamine; GlcNAc, N -acetylglucosamine; Gal, galactose; NeuAc, N -acetylneuraminic acid. (F) Lectin blot analysis of sialidase-treated LV extracts using ACA. Representative images demonstrate ACA-reactive glycoproteins and SYPRO Ruby-stained total proteins of three individual rats in each group. Lower panel shows densitometry analysis; intensity of each band was normalized to total protein amount. Data are presented as the fold change (n = 6) compared with sialidase-untreated LV extracts of HS rats at 12 weeks. (A,D) The numbers of examined rats were n = 12 and n = 15 for the HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (A,D,F) *, p

    Journal: PLoS ONE

    Article Title: Aberrant Glycosylation in the Left Ventricle and Plasma of Rats with Cardiac Hypertrophy and Heart Failure

    doi: 10.1371/journal.pone.0150210

    Figure Lengend Snippet: Altered mucin-type O -glycosylation in the LV of DS hypertensive rats. (A) T-synthase activity in LV extracts. Data were normalized to protein content. (B) Correlation of T-synthase activity with ANP gene expression. ANP gene expression level was quantified by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (C) Correlation of T-synthase activity with ejection fraction. (D) Relative expression levels of glycogenes involved in the early stage of mucin-type O -glycosylation in the LV tissues of DS rats were analyzed by qPCR and normalized to that of Tbp . Data are presented as the fold change compared with LS rats at 12 weeks. (E) Schematic summary of gene expression analysis data shown in (D). Examined glycosyltransferases in the mucin-type O -glycosylation pathway are shown in red (upregulated), blue (downregulated), or black (no change) letters. Relatively rare core structures (core 5, 6, 7, and 8) synthesized from Tn are omitted. The biosynthetic pathway of disialyl-T is upregulated, as indicated with bold arrows. GalNAc, N -acetylgalactosamine; GlcNAc, N -acetylglucosamine; Gal, galactose; NeuAc, N -acetylneuraminic acid. (F) Lectin blot analysis of sialidase-treated LV extracts using ACA. Representative images demonstrate ACA-reactive glycoproteins and SYPRO Ruby-stained total proteins of three individual rats in each group. Lower panel shows densitometry analysis; intensity of each band was normalized to total protein amount. Data are presented as the fold change (n = 6) compared with sialidase-untreated LV extracts of HS rats at 12 weeks. (A,D) The numbers of examined rats were n = 12 and n = 15 for the HS groups at 12 and 16 weeks, respectively; n = 6 for LS groups at each period. (A,D,F) *, p

    Article Snippet: Protein deglycosylation LV extracts prepared for western blot and lectin blot analyses and recombinant proteins were treated with glycosidases, including sialidase, O -glycosidase, and PNGase F, which were all obtained from New England Biolabs (Beverly, MA).

    Techniques: Activity Assay, Aqueous Normal-phase Chromatography, Expressing, Real-time Polymerase Chain Reaction, Synthesized, Staining