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sypro ruby protein gel stain  (Thermo Fisher)


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    Structured Review

    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+stain/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

    Staining:

    Article Title: Identification of candidate vaccine antigens using 2-D gel electrophoresis and immunoproteomics for cross protection against Glaesserella parasuis.
    Article Snippet: The large gels were run in an Ettan DALTsix electrophoresis unit (GE Healthcare, USA) overnight. .. Total protein was detected in 2-D gels with SYPRO Ruby protein gel stain (Thermo Fisher Scientific, USA). .. The protein gels were bound to a glass plate with BindSilane (GE Healthcare, USA).

    Article Title: Iron triggers Tv PI4P5K proteostasis and Arf-mediated cell membrane trafficking to regulate PIP 2 signaling crucial for multiple pathogenic activities of the parasitic protozoan Trichomonas vaginalis .
    Article Snippet: .. The protein sample denatured in 1× SDS sample buffer was separated by SDS PAGE in a 10% gel, and the protein bands were visualized by SYPRO Ruby Protein Gel Stain (ThermoFisher Scientific). ..

    Article Title: Scale-up of a low-temperature spray-drying process for a tuberculosis vaccine candidate using lab-scale equipment.
    Article Snippet: Diluted samples were then heated to 85 ◦C for 15 min, cooled to room temperature, centrifuged at 2000 RPM in a benchtop centrifuge (Thermo Fisher Scientific, Waltham, MA, USA) for 2 min to collect the sample, and loaded on a precast, 4–20 % TrisGlycine SDS-PAGE gel (Thermo Fisher Scientific, Waltham, MA, USA). .. The gel was run at 180 V for 65 min. SYPRO Ruby protein gel stain was used to visualize ID93 in the gel according to the manufacturer’s instructions for overnight staining (Thermo Fisher Scientific, Waltham, MA, USA). .. The gel imaging system (ChemiDoc; Bio-Rad, Mississauga, ON, Canada) utilized the installed SYPRO Ruby protocol for visualization.

    Article Title: Immunomodulatory antibodies and methods of use thereof
    Article Snippet: .. Sample loading buffer+10% 2-mercaptoethanol was added and the samples were heated for 5 min at 90° C. Five microliters of each sample was reserved for SYPRO Ruby Protein Gel Stain (ThermoFisher Scientific, No. S12000) analysis. ..

    Article Title: Iron triggers Tv PI4P5K proteostasis and Arf-mediated cell membrane trafficking to regulate PIP 2 signaling crucial for multiple pathogenic activities of the parasitic protozoan Trichomonas vaginalis
    Article Snippet: .. The protein sample denatured in 1× SDS sample buffer was separated by SDS PAGE in a 10% gel, and the protein bands were visualized by SYPRO Ruby Protein Gel Stain (ThermoFisher Scientific). ..

    Article Title: Secreted PD-L1 alleviates inflammatory arthritis in mice through local and systemic AAV gene therapy
    Article Snippet: .. SYPRO Ruby protein gel stain (Thermo Fisher, Waltham, Massachusetts, US) was used to verify the capsids contained all three VP1, VP2 and VP3 proteins. ..

    Article Title: Expression of Resuscitation-Promoting Factor C Stimulates the Growth of Mycobacterium bovis BCG and Delays DevR Regulon Activation in Hypoxia
    Article Snippet: .. Then, proteins were separated on 12.5% SDS-PAGE gels and visualized by staining with Sypro Ruby Protein Gel Stain (Thermo Fisher Scientific, Waltham, MA, USA) following the manufacturer's recommendations. .. The gels were analyzed using the PDQuest 8.0 software (Bio-Rad, Hercules, CA, USA).

    Article Title: Marfan syndrome cardiomyocytes show excess of titin isoform N2BA and extended sarcomeric M-band.
    Article Snippet: Marfan syndrome (MFS) is an autosomal dominant disease caused by mutations in the gene (FBN1) of fibrillin-1, a major determinant of the extracellular matrix (ECM).. Functional impairment in the cardiac left ventricle (LV) of these patients is usually a consequence of aortic valve disease.. However, LV passive stiffness may also be affected by chronic changes in mechanical load and ECM dysfunction.

    SDS Page:

    Article Title: Iron triggers Tv PI4P5K proteostasis and Arf-mediated cell membrane trafficking to regulate PIP 2 signaling crucial for multiple pathogenic activities of the parasitic protozoan Trichomonas vaginalis .
    Article Snippet: .. The protein sample denatured in 1× SDS sample buffer was separated by SDS PAGE in a 10% gel, and the protein bands were visualized by SYPRO Ruby Protein Gel Stain (ThermoFisher Scientific). ..

    Article Title: Iron triggers Tv PI4P5K proteostasis and Arf-mediated cell membrane trafficking to regulate PIP 2 signaling crucial for multiple pathogenic activities of the parasitic protozoan Trichomonas vaginalis
    Article Snippet: .. The protein sample denatured in 1× SDS sample buffer was separated by SDS PAGE in a 10% gel, and the protein bands were visualized by SYPRO Ruby Protein Gel Stain (ThermoFisher Scientific). ..

    Article Title: Expression of Resuscitation-Promoting Factor C Stimulates the Growth of Mycobacterium bovis BCG and Delays DevR Regulon Activation in Hypoxia
    Article Snippet: .. Then, proteins were separated on 12.5% SDS-PAGE gels and visualized by staining with Sypro Ruby Protein Gel Stain (Thermo Fisher Scientific, Waltham, MA, USA) following the manufacturer's recommendations. .. The gels were analyzed using the PDQuest 8.0 software (Bio-Rad, Hercules, CA, USA).

    Expressing:

    Article Title: Marfan syndrome cardiomyocytes show excess of titin isoform N2BA and extended sarcomeric M-band.
    Article Snippet: Marfan syndrome (MFS) is an autosomal dominant disease caused by mutations in the gene (FBN1) of fibrillin-1, a major determinant of the extracellular matrix (ECM).. Functional impairment in the cardiac left ventricle (LV) of these patients is usually a consequence of aortic valve disease.. However, LV passive stiffness may also be affected by chronic changes in mechanical load and ECM dysfunction.

    Nucleic Acid Electrophoresis:

    Article Title: Marfan syndrome cardiomyocytes show excess of titin isoform N2BA and extended sarcomeric M-band.
    Article Snippet: Marfan syndrome (MFS) is an autosomal dominant disease caused by mutations in the gene (FBN1) of fibrillin-1, a major determinant of the extracellular matrix (ECM).. Functional impairment in the cardiac left ventricle (LV) of these patients is usually a consequence of aortic valve disease.. However, LV passive stiffness may also be affected by chronic changes in mechanical load and ECM dysfunction.



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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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    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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    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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    (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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    Bio-Rad protein gel stain
    (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.
    Protein Gel Stain, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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