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sypro ruby protein gel stain  (Thermo Fisher)


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    Thermo Fisher sypro ruby protein gel stain
    Sypro Ruby Protein Gel Stain, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sypro+ruby+protein+gel+staining/sypro+orange+protein+gel+stain/pm40516376-67-8-13
    Average 90 stars, based on 1 article reviews
    sypro ruby protein gel stain - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    SDS Page:

    Article Title: Passive Transfer of Animal-Derived Polyclonal Hyperimmune Antibodies Provides Protection of Mice from Lethal Lassa Virus Infection
    Article Snippet: The antibody concentration was determined using Pierce BCA Protein Assay Kit (Thermo Fisher Scientific). .. The purity of IgG preparations was assessed by 12% SDS-PAGE and SYPRO Ruby protein gel staining (Thermo Fisher Scientific) ( ). ..

    Article Title: Passive Transfer of Animal-Derived Polyclonal Hyperimmune Antibodies Provides Protection of Mice from Lethal Lassa Virus Infection.
    Article Snippet: The antibody concentration was determined using Pierce BCA Protein Assay Kit (Thermo Fisher Scientific). .. The purity of IgG preparations was assessed by 12% SDS-PAGE and SYPRO Ruby protein gel staining (Thermo Fisher Scientific) (Supplementary Figure S1A,B). ..

    Article Title: Adjuvant formulated virus-like particles expressing native-like forms of the Lassa virus envelope surface glycoprotein are immunogenic and induce antibodies with broadly neutralizing activity
    Article Snippet: The antibody concentration was determined using a Pierce BCA Protein Assay kit with a BSA standard (Thermo Scientific) and measured in a NanoPhotometer NP80 (Implen). .. The purity of IgG preparations was assessed by 12% SDS-PAGE and SYPRO Ruby protein gel staining (Invitrogen). ..

    Article Title: Adjuvant formulated virus-like particles expressing native-like forms of the Lassa virus envelope surface glycoprotein are immunogenic and induce antibodies with broadly neutralizing activity
    Article Snippet: .. For verification of sample quality and purity, 0.4 μg recombinant LASV GP1 and GP2 proteins and IgG purified from rabbit blood (3 μg of total protein) were separated by SDS-PAGE using 12% polyacrylamide gels and stained with SYPRO Ruby protein gel staining (Invitrogen) according to the manufacturer’s instructions. .. Samples were analyzed using the ChemiDoc Imaging System (Bio-Rad).

    Staining:

    Article Title: Passive Transfer of Animal-Derived Polyclonal Hyperimmune Antibodies Provides Protection of Mice from Lethal Lassa Virus Infection
    Article Snippet: The antibody concentration was determined using Pierce BCA Protein Assay Kit (Thermo Fisher Scientific). .. The purity of IgG preparations was assessed by 12% SDS-PAGE and SYPRO Ruby protein gel staining (Thermo Fisher Scientific) ( ). ..

    Article Title: Biophysical and functional study of CRL5 Ozz , a muscle specific ubiquitin ligase complex
    Article Snippet: .. Bound proteins were released by boiling the beads with sample buffer and separated on SDS–polyacrylamide gels under denaturing conditions, followed by SYPRO Ruby Protein Gel Staining (ThermoFisher Scientific). .. Purified insect cells expressed Ozz E3 sub complexes and reconstituted Ozz-E3 ubiquitin ligase were subjected to sedimentation velocity in a ProteomeLab XL-I analytical ultracentrifuge with a four-hole rotor (Beckman An-60Ti) following standard protocols .

    Article Title: Passive Transfer of Animal-Derived Polyclonal Hyperimmune Antibodies Provides Protection of Mice from Lethal Lassa Virus Infection.
    Article Snippet: The antibody concentration was determined using Pierce BCA Protein Assay Kit (Thermo Fisher Scientific). .. The purity of IgG preparations was assessed by 12% SDS-PAGE and SYPRO Ruby protein gel staining (Thermo Fisher Scientific) (Supplementary Figure S1A,B). ..

    Article Title: Adjuvant formulated virus-like particles expressing native-like forms of the Lassa virus envelope surface glycoprotein are immunogenic and induce antibodies with broadly neutralizing activity
    Article Snippet: The antibody concentration was determined using a Pierce BCA Protein Assay kit with a BSA standard (Thermo Scientific) and measured in a NanoPhotometer NP80 (Implen). .. The purity of IgG preparations was assessed by 12% SDS-PAGE and SYPRO Ruby protein gel staining (Invitrogen). ..

    Article Title: Adjuvant formulated virus-like particles expressing native-like forms of the Lassa virus envelope surface glycoprotein are immunogenic and induce antibodies with broadly neutralizing activity
    Article Snippet: .. For verification of sample quality and purity, 0.4 μg recombinant LASV GP1 and GP2 proteins and IgG purified from rabbit blood (3 μg of total protein) were separated by SDS-PAGE using 12% polyacrylamide gels and stained with SYPRO Ruby protein gel staining (Invitrogen) according to the manufacturer’s instructions. .. Samples were analyzed using the ChemiDoc Imaging System (Bio-Rad).

    Article Title: iTRAQ-based proteomics reveals novel biomarkers of osteoarthritis
    Article Snippet: An XL-SAP Kit (APRO Science) was used for secondary antibody reactions. .. As internal controls, 35 μg protein samples (control: n = 5; OA: n = 16) were separated by SDS-PAGE, and then, SYPRO ruby protein gel staining (Invitrogen, Carlsbad, CA) was performed according to the manufacturer’s instructions. .. Gel images were taken by a Typhoon scanner (GE Healthcare, Tyrone, PA).

    Article Title: Functional genomic profiling of O-GlcNAc reveals its context-specific interplay with RNA polymerase II.
    Article Snippet: .. Immunoprecipitated protein samples were analyzed by total protein staining using SYPRO Ruby Protein Gel Staining (Thermo Fisher Scientific #S12000) and by Western Blot analysis. ..

    Article Title: A new proteinaceous pathogen-associated molecular pattern (PAMP) identified in Ascomycete fungi induces cell death in Solanaceae.
    Article Snippet: .. The presence of RcCDI1 homologues in supernatant was confirmed via SYPRO Ruby Protein Gel staining (Invitrogen) and immunoblotting using anti-V5 antibody before plant infiltration. .. Pichia pastoris culture supernatants (CSs) containing RcCDI1 homologues from Z. tritici and M. oryzae were concentrated 20- fold using Vivaspin 10-kDa MWCO columns (GE Healthcare Life Sciences, Little Chalfont, UK).

    Recombinant:

    Article Title: Adjuvant formulated virus-like particles expressing native-like forms of the Lassa virus envelope surface glycoprotein are immunogenic and induce antibodies with broadly neutralizing activity
    Article Snippet: .. For verification of sample quality and purity, 0.4 μg recombinant LASV GP1 and GP2 proteins and IgG purified from rabbit blood (3 μg of total protein) were separated by SDS-PAGE using 12% polyacrylamide gels and stained with SYPRO Ruby protein gel staining (Invitrogen) according to the manufacturer’s instructions. .. Samples were analyzed using the ChemiDoc Imaging System (Bio-Rad).

    Purification:

    Article Title: Adjuvant formulated virus-like particles expressing native-like forms of the Lassa virus envelope surface glycoprotein are immunogenic and induce antibodies with broadly neutralizing activity
    Article Snippet: .. For verification of sample quality and purity, 0.4 μg recombinant LASV GP1 and GP2 proteins and IgG purified from rabbit blood (3 μg of total protein) were separated by SDS-PAGE using 12% polyacrylamide gels and stained with SYPRO Ruby protein gel staining (Invitrogen) according to the manufacturer’s instructions. .. Samples were analyzed using the ChemiDoc Imaging System (Bio-Rad).

    Control:

    Article Title: iTRAQ-based proteomics reveals novel biomarkers of osteoarthritis
    Article Snippet: An XL-SAP Kit (APRO Science) was used for secondary antibody reactions. .. As internal controls, 35 μg protein samples (control: n = 5; OA: n = 16) were separated by SDS-PAGE, and then, SYPRO ruby protein gel staining (Invitrogen, Carlsbad, CA) was performed according to the manufacturer’s instructions. .. Gel images were taken by a Typhoon scanner (GE Healthcare, Tyrone, PA).

    Immunoprecipitation:

    Article Title: Functional genomic profiling of O-GlcNAc reveals its context-specific interplay with RNA polymerase II.
    Article Snippet: .. Immunoprecipitated protein samples were analyzed by total protein staining using SYPRO Ruby Protein Gel Staining (Thermo Fisher Scientific #S12000) and by Western Blot analysis. ..

    Western Blot:

    Article Title: Functional genomic profiling of O-GlcNAc reveals its context-specific interplay with RNA polymerase II.
    Article Snippet: .. Immunoprecipitated protein samples were analyzed by total protein staining using SYPRO Ruby Protein Gel Staining (Thermo Fisher Scientific #S12000) and by Western Blot analysis. ..

    Article Title: A new proteinaceous pathogen-associated molecular pattern (PAMP) identified in Ascomycete fungi induces cell death in Solanaceae.
    Article Snippet: .. The presence of RcCDI1 homologues in supernatant was confirmed via SYPRO Ruby Protein Gel staining (Invitrogen) and immunoblotting using anti-V5 antibody before plant infiltration. .. Pichia pastoris culture supernatants (CSs) containing RcCDI1 homologues from Z. tritici and M. oryzae were concentrated 20- fold using Vivaspin 10-kDa MWCO columns (GE Healthcare Life Sciences, Little Chalfont, UK).



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    Representative 2D IEF-SDS-PAGE protein profiles of J. curcas somatic embryos. The analysis was carried out using ImageMaster TM 2D Platinum software version 7. Molecular masses (kDa) are indicated on the left, and isoelectric points (pI 4–7) are provided above the gel image. ( a ) Protein profile of pre-globular somatic embryos with an average of 654 ± 41 detected spots, and ( b ) protein profile of globular-stage somatic embryos with 552 ± 30 detected spots as indicated by a red cross. The blue and red circles on the gel indicate the protein spots identified through mass spectrometry; the data obtained are presented in . Red circles correspond to unique protein spots detected exclusively at the globular stage, while blue circles indicate protein spots that were at least 1.5-fold more abundant in the embryogenic stage than in the other stages. Numbers correspond to spots identified with ImageMaster TM 2D Platinum version 7. First-dimensional isoelectric focusing was performed using 11 cm IPG strips loaded with 200 µg of total protein. Second-dimension separation was carried out using 12.5% SDS-PAGE polyacrylamide gels (CRITERION Cell, Bio-Rad Laboratories, Hercules, CA, USA). Gels were stained with <t>Sypro</t> <t>Ruby</t> (Bio-Rad Laboratories, Hercules, CA, USA).
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    Thermo Fisher sypro ruby protein gel stain s12001
    (A) Schematics of constructs for APEX2 fusion protein expression. (B) Immunofluorescence analysis of the indicated proteins (detected by EGFP) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). DAPI (4’,6-diamidino-2-phenylindole) was used to stain the DNA. The scale bar represents 10 μm. (C) Western blotting and RNA dot blotting for proteins and RNAs under the indicated conditions. Desthiobiotinylated proteins and RNAs were detected using infrared dye-conjugated streptavidin. As a loading control, RPS17 protein was subjected to Western blotting, and total RNA was stained with methylene blue. (D) Polysome profiling under the indicated conditions. (E) Western blotting and RNA dot blotting for proteins and RNAs along the fractions of polysome profiling (see D for the corresponding fraction numbers). Desthiobiotinylated proteins and RNAs were detected by infrared dye-conjugated streptavidin. Total RNA was stained with methylene blue. (F) Scatter plot of the ribosome footprints from each mRNA in standard Ribo-Seq. The results in the presence and absence of H 2 O 2 were compared. (G) <t>SYPRO</t> <t>Ruby</t> staining of proteins purified after streptavidin pulldown and elution under the indicated conditions. (H) Fractions of usable reads (reads after deduplication and removal of noncoding RNA-mapped reads) in standard Ribo-Seq and cytosol APEX-Ribo-Seq under the indicated conditions. (I) Distribution of ribosome footprint length under the indicated conditions. (J) Metagene plots of ribosome footprints (the 5′-end positions) around the start codon under the indicated conditions. The data for the 29-nt footprints are shown. (K) Fraction of the frame position for the 5′ end of the footprint (29 nt) under the indicated conditions. (L) Scatter plot of the ribosome footprints from each mRNA in cytosol APEX-Ribo-Seq replicates. (M) Immunofluorescence analysis of the indicated proteins (detected by V5) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). TOM20 was detected as a mitochondrial marker. The scale bar represents 10 μm. (N) Fraction of the frame position for the 5′ end of the mitoribosome footprint (32 nt) in matrix APEX-Ribo-Seq. TPM, transcripts per million; r , Pearson’s correlation coefficient; RPM, reads per million reads. For H, K, and N, the means (bars), s.d.s (errors), and individual replicates (n = 2, points) are shown.
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    (A) Schematics of constructs for APEX2 fusion protein expression. (B) Immunofluorescence analysis of the indicated proteins (detected by EGFP) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). DAPI (4’,6-diamidino-2-phenylindole) was used to stain the DNA. The scale bar represents 10 μm. (C) Western blotting and RNA dot blotting for proteins and RNAs under the indicated conditions. Desthiobiotinylated proteins and RNAs were detected using infrared dye-conjugated streptavidin. As a loading control, RPS17 protein was subjected to Western blotting, and total RNA was stained with methylene blue. (D) Polysome profiling under the indicated conditions. (E) Western blotting and RNA dot blotting for proteins and RNAs along the fractions of polysome profiling (see D for the corresponding fraction numbers). Desthiobiotinylated proteins and RNAs were detected by infrared dye-conjugated streptavidin. Total RNA was stained with methylene blue. (F) Scatter plot of the ribosome footprints from each mRNA in standard Ribo-Seq. The results in the presence and absence of H 2 O 2 were compared. (G) <t>SYPRO</t> <t>Ruby</t> staining of proteins purified after streptavidin pulldown and elution under the indicated conditions. (H) Fractions of usable reads (reads after deduplication and removal of noncoding RNA-mapped reads) in standard Ribo-Seq and cytosol APEX-Ribo-Seq under the indicated conditions. (I) Distribution of ribosome footprint length under the indicated conditions. (J) Metagene plots of ribosome footprints (the 5′-end positions) around the start codon under the indicated conditions. The data for the 29-nt footprints are shown. (K) Fraction of the frame position for the 5′ end of the footprint (29 nt) under the indicated conditions. (L) Scatter plot of the ribosome footprints from each mRNA in cytosol APEX-Ribo-Seq replicates. (M) Immunofluorescence analysis of the indicated proteins (detected by V5) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). TOM20 was detected as a mitochondrial marker. The scale bar represents 10 μm. (N) Fraction of the frame position for the 5′ end of the mitoribosome footprint (32 nt) in matrix APEX-Ribo-Seq. TPM, transcripts per million; r , Pearson’s correlation coefficient; RPM, reads per million reads. For H, K, and N, the means (bars), s.d.s (errors), and individual replicates (n = 2, points) are shown.
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    Image Search Results


    Representative 2D IEF-SDS-PAGE protein profiles of J. curcas somatic embryos. The analysis was carried out using ImageMaster TM 2D Platinum software version 7. Molecular masses (kDa) are indicated on the left, and isoelectric points (pI 4–7) are provided above the gel image. ( a ) Protein profile of pre-globular somatic embryos with an average of 654 ± 41 detected spots, and ( b ) protein profile of globular-stage somatic embryos with 552 ± 30 detected spots as indicated by a red cross. The blue and red circles on the gel indicate the protein spots identified through mass spectrometry; the data obtained are presented in . Red circles correspond to unique protein spots detected exclusively at the globular stage, while blue circles indicate protein spots that were at least 1.5-fold more abundant in the embryogenic stage than in the other stages. Numbers correspond to spots identified with ImageMaster TM 2D Platinum version 7. First-dimensional isoelectric focusing was performed using 11 cm IPG strips loaded with 200 µg of total protein. Second-dimension separation was carried out using 12.5% SDS-PAGE polyacrylamide gels (CRITERION Cell, Bio-Rad Laboratories, Hercules, CA, USA). Gels were stained with Sypro Ruby (Bio-Rad Laboratories, Hercules, CA, USA).

    Journal: International Journal of Molecular Sciences

    Article Title: Proteomic Analysis and Expression of Selected Genes During the Early Somatic Embryogenesis of Jatropha curcas L.

    doi: 10.3390/ijms26136384

    Figure Lengend Snippet: Representative 2D IEF-SDS-PAGE protein profiles of J. curcas somatic embryos. The analysis was carried out using ImageMaster TM 2D Platinum software version 7. Molecular masses (kDa) are indicated on the left, and isoelectric points (pI 4–7) are provided above the gel image. ( a ) Protein profile of pre-globular somatic embryos with an average of 654 ± 41 detected spots, and ( b ) protein profile of globular-stage somatic embryos with 552 ± 30 detected spots as indicated by a red cross. The blue and red circles on the gel indicate the protein spots identified through mass spectrometry; the data obtained are presented in . Red circles correspond to unique protein spots detected exclusively at the globular stage, while blue circles indicate protein spots that were at least 1.5-fold more abundant in the embryogenic stage than in the other stages. Numbers correspond to spots identified with ImageMaster TM 2D Platinum version 7. First-dimensional isoelectric focusing was performed using 11 cm IPG strips loaded with 200 µg of total protein. Second-dimension separation was carried out using 12.5% SDS-PAGE polyacrylamide gels (CRITERION Cell, Bio-Rad Laboratories, Hercules, CA, USA). Gels were stained with Sypro Ruby (Bio-Rad Laboratories, Hercules, CA, USA).

    Article Snippet: Following electrophoresis, the gels were fixed in 10% ( v / v ) ethanol and 7% ( v / v ) acetic acid for 30 min and subsequently stained with Sypro Ruby protein stain (Bio-Rad Laboratories, Hercules, CA, USA) for 20 h. Destaining was performed by incubating the gels in the same fixing solution for 1 h with gentle agitation.

    Techniques: SDS Page, Software, Mass Spectrometry, Staining

    (A) Schematics of constructs for APEX2 fusion protein expression. (B) Immunofluorescence analysis of the indicated proteins (detected by EGFP) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). DAPI (4’,6-diamidino-2-phenylindole) was used to stain the DNA. The scale bar represents 10 μm. (C) Western blotting and RNA dot blotting for proteins and RNAs under the indicated conditions. Desthiobiotinylated proteins and RNAs were detected using infrared dye-conjugated streptavidin. As a loading control, RPS17 protein was subjected to Western blotting, and total RNA was stained with methylene blue. (D) Polysome profiling under the indicated conditions. (E) Western blotting and RNA dot blotting for proteins and RNAs along the fractions of polysome profiling (see D for the corresponding fraction numbers). Desthiobiotinylated proteins and RNAs were detected by infrared dye-conjugated streptavidin. Total RNA was stained with methylene blue. (F) Scatter plot of the ribosome footprints from each mRNA in standard Ribo-Seq. The results in the presence and absence of H 2 O 2 were compared. (G) SYPRO Ruby staining of proteins purified after streptavidin pulldown and elution under the indicated conditions. (H) Fractions of usable reads (reads after deduplication and removal of noncoding RNA-mapped reads) in standard Ribo-Seq and cytosol APEX-Ribo-Seq under the indicated conditions. (I) Distribution of ribosome footprint length under the indicated conditions. (J) Metagene plots of ribosome footprints (the 5′-end positions) around the start codon under the indicated conditions. The data for the 29-nt footprints are shown. (K) Fraction of the frame position for the 5′ end of the footprint (29 nt) under the indicated conditions. (L) Scatter plot of the ribosome footprints from each mRNA in cytosol APEX-Ribo-Seq replicates. (M) Immunofluorescence analysis of the indicated proteins (detected by V5) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). TOM20 was detected as a mitochondrial marker. The scale bar represents 10 μm. (N) Fraction of the frame position for the 5′ end of the mitoribosome footprint (32 nt) in matrix APEX-Ribo-Seq. TPM, transcripts per million; r , Pearson’s correlation coefficient; RPM, reads per million reads. For H, K, and N, the means (bars), s.d.s (errors), and individual replicates (n = 2, points) are shown.

    Journal: bioRxiv

    Article Title: Sequence grammar and dynamics of subcellular translation revealed by APEX-Ribo-Seq

    doi: 10.1101/2025.05.26.656194

    Figure Lengend Snippet: (A) Schematics of constructs for APEX2 fusion protein expression. (B) Immunofluorescence analysis of the indicated proteins (detected by EGFP) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). DAPI (4’,6-diamidino-2-phenylindole) was used to stain the DNA. The scale bar represents 10 μm. (C) Western blotting and RNA dot blotting for proteins and RNAs under the indicated conditions. Desthiobiotinylated proteins and RNAs were detected using infrared dye-conjugated streptavidin. As a loading control, RPS17 protein was subjected to Western blotting, and total RNA was stained with methylene blue. (D) Polysome profiling under the indicated conditions. (E) Western blotting and RNA dot blotting for proteins and RNAs along the fractions of polysome profiling (see D for the corresponding fraction numbers). Desthiobiotinylated proteins and RNAs were detected by infrared dye-conjugated streptavidin. Total RNA was stained with methylene blue. (F) Scatter plot of the ribosome footprints from each mRNA in standard Ribo-Seq. The results in the presence and absence of H 2 O 2 were compared. (G) SYPRO Ruby staining of proteins purified after streptavidin pulldown and elution under the indicated conditions. (H) Fractions of usable reads (reads after deduplication and removal of noncoding RNA-mapped reads) in standard Ribo-Seq and cytosol APEX-Ribo-Seq under the indicated conditions. (I) Distribution of ribosome footprint length under the indicated conditions. (J) Metagene plots of ribosome footprints (the 5′-end positions) around the start codon under the indicated conditions. The data for the 29-nt footprints are shown. (K) Fraction of the frame position for the 5′ end of the footprint (29 nt) under the indicated conditions. (L) Scatter plot of the ribosome footprints from each mRNA in cytosol APEX-Ribo-Seq replicates. (M) Immunofluorescence analysis of the indicated proteins (detected by V5) and desthiobiotinylated proteins/RNAs (detected with Alexa Fluor 555-conjugated streptavidin). TOM20 was detected as a mitochondrial marker. The scale bar represents 10 μm. (N) Fraction of the frame position for the 5′ end of the mitoribosome footprint (32 nt) in matrix APEX-Ribo-Seq. TPM, transcripts per million; r , Pearson’s correlation coefficient; RPM, reads per million reads. For H, K, and N, the means (bars), s.d.s (errors), and individual replicates (n = 2, points) are shown.

    Article Snippet: The gels were stained with SYPRO Ruby Protein Gel Stain (Thermo Fisher Scientific, S12001) and imaged using a Pharos FX imaging system (Bio-Rad).

    Techniques: Construct, Expressing, Immunofluorescence, Staining, Western Blot, Control, Purification, Marker