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Bio-Rad biotinylated marker proteins
Biotinylated Marker Proteins, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/biotinylated marker proteins/product/Bio-Rad
Average 91 stars, based on 2 article reviews
Price from $9.99 to $1999.99
biotinylated marker proteins - by Bioz Stars, 2020-07
91/100 stars

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Article Title: Torilin Inhibits Inflammation by Limiting TAK1-Mediated MAP Kinase and NF-κB Activation
Article Snippet: .. All materials, equipment, and biotinylated marker proteins for gel electrophoresis were from Bio-Rad. ..

Article Title: The Mitochondrial Message-specific mRNA Protectors Cbp1 and Pet309 Are Associated in a High-Molecular Weight Complex
Article Snippet: .. Biotinylated marker proteins (Bio-Rad) were used to estimate protein molecular weights. .. Isolated mitochondria were sonicated in buffer containing 1 M KCl.

Nucleic Acid Electrophoresis:

Article Title: Torilin Inhibits Inflammation by Limiting TAK1-Mediated MAP Kinase and NF-κB Activation
Article Snippet: .. All materials, equipment, and biotinylated marker proteins for gel electrophoresis were from Bio-Rad. ..

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  • 92
    Bio-Rad pgp9 5
    a - b X axis: time points. Y axis: nerve fiber score, 0–3 scale a) Trend of nerve <t>fibers–PGP9.5</t> in submucosa (panel a ): median and range values, T0 vs. T1 p = 0.002, T0 vs. T2 p = 0.003, T0 vs T12 p = 0.008 and T2 vs T12 p = 0.59 b ) Trend of nerve fibers–PGP9.5 in the smooth muscle (panel b ): median and range values, T0 vs. T1 p = 0.004, T0 vs. T2 p = 0.003, T0 vs T12 p = 0.025, and T2 vs T12 p = 0.024
    Pgp9 5, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pgp9 5/product/Bio-Rad
    Average 92 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    pgp9 5 - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    88
    Bio-Rad biotinylated protein marker
    Expression of SIRPα on monocytes. Detection of SIRPα by WB in freshly isolated human PBMC and PMN using anti-SIRPα.ex (SIRPα.ex) and anti-SIRPα.ct (SIRPα.ct) antibodies. B) Immunofluorescence staining of PBMC. Cell surface SIRPα was labeled with anti-SIRPα.ex under non-permeable conditions. Monocytes (arrow heads) were defined by anti-human CD14 antibody, and T and B lymphocytes were defined with anti-Lck and anti-B220 antibodies, respectively. C) Determination of the distribution of SIRPα in PMN and monocytes by cell biotinylation. Cells were <t>biotinylated</t> with either NHS-biotin (cell permeable) or sulfo-NHS-biotin (non-cell permeable), followed by the IP of SIRPα from the lysates. Biotinylated and total SIRPα were blotted by streptavidin-HRP and anti-SIRPα.ct, respectively. The same amount of protein was used for IP as confirmed by the actin blots. D) FACS analysis to determine SIRPα in monocytes labeled under cell permeable and non-permeable conditions.
    Biotinylated Protein Marker, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated protein marker/product/Bio-Rad
    Average 88 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    biotinylated protein marker - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

    Image Search Results


    a - b X axis: time points. Y axis: nerve fiber score, 0–3 scale a) Trend of nerve fibers–PGP9.5 in submucosa (panel a ): median and range values, T0 vs. T1 p = 0.002, T0 vs. T2 p = 0.003, T0 vs T12 p = 0.008 and T2 vs T12 p = 0.59 b ) Trend of nerve fibers–PGP9.5 in the smooth muscle (panel b ): median and range values, T0 vs. T1 p = 0.004, T0 vs. T2 p = 0.003, T0 vs T12 p = 0.025, and T2 vs T12 p = 0.024

    Journal: BMC Pulmonary Medicine

    Article Title: Nerve ablation after bronchial thermoplasty and sustained improvement in severe asthma

    doi: 10.1186/s12890-017-0554-8

    Figure Lengend Snippet: a - b X axis: time points. Y axis: nerve fiber score, 0–3 scale a) Trend of nerve fibers–PGP9.5 in submucosa (panel a ): median and range values, T0 vs. T1 p = 0.002, T0 vs. T2 p = 0.003, T0 vs T12 p = 0.008 and T2 vs T12 p = 0.59 b ) Trend of nerve fibers–PGP9.5 in the smooth muscle (panel b ): median and range values, T0 vs. T1 p = 0.004, T0 vs. T2 p = 0.003, T0 vs T12 p = 0.025, and T2 vs T12 p = 0.024

    Article Snippet: Free-floating sections were stained using primary antibodies raised in rabbit against the pan-axonal marker protein gene product 9.5 (PGP9.5; Bio-Rad Laboratories, Hercules, CA, USA; dilution 1:1200) species-specific biotinylated secondary antibody (Vector Lab Inc., Burlingame, CA, USA), Peroxidase Avidin Biotin Complex (ABC, Vector Labs, Burlingame, CA, USA), and peroxidase substrate Vector SG (Vector Labs).

    Techniques:

    a ) Overall picture of the nerve endings/fibers (arrows) immunodetected with PGP9.5 at time T0 in bronchial biopsies of a patient with asthma. e : Bronchial Epithelium (green); S: Bronchial Submucosa (blue); M: Bronchial Muscle (red). b ) Bronchial biopsy at T1. c ) Bronchial biopsy at T2. d ) Bronchial biopsy at T12. Note the scarcity of nerve fibers in the submucosa and muscle bundles at T1 to T12

    Journal: BMC Pulmonary Medicine

    Article Title: Nerve ablation after bronchial thermoplasty and sustained improvement in severe asthma

    doi: 10.1186/s12890-017-0554-8

    Figure Lengend Snippet: a ) Overall picture of the nerve endings/fibers (arrows) immunodetected with PGP9.5 at time T0 in bronchial biopsies of a patient with asthma. e : Bronchial Epithelium (green); S: Bronchial Submucosa (blue); M: Bronchial Muscle (red). b ) Bronchial biopsy at T1. c ) Bronchial biopsy at T2. d ) Bronchial biopsy at T12. Note the scarcity of nerve fibers in the submucosa and muscle bundles at T1 to T12

    Article Snippet: Free-floating sections were stained using primary antibodies raised in rabbit against the pan-axonal marker protein gene product 9.5 (PGP9.5; Bio-Rad Laboratories, Hercules, CA, USA; dilution 1:1200) species-specific biotinylated secondary antibody (Vector Lab Inc., Burlingame, CA, USA), Peroxidase Avidin Biotin Complex (ABC, Vector Labs, Burlingame, CA, USA), and peroxidase substrate Vector SG (Vector Labs).

    Techniques:

    Expression of SIRPα on monocytes. Detection of SIRPα by WB in freshly isolated human PBMC and PMN using anti-SIRPα.ex (SIRPα.ex) and anti-SIRPα.ct (SIRPα.ct) antibodies. B) Immunofluorescence staining of PBMC. Cell surface SIRPα was labeled with anti-SIRPα.ex under non-permeable conditions. Monocytes (arrow heads) were defined by anti-human CD14 antibody, and T and B lymphocytes were defined with anti-Lck and anti-B220 antibodies, respectively. C) Determination of the distribution of SIRPα in PMN and monocytes by cell biotinylation. Cells were biotinylated with either NHS-biotin (cell permeable) or sulfo-NHS-biotin (non-cell permeable), followed by the IP of SIRPα from the lysates. Biotinylated and total SIRPα were blotted by streptavidin-HRP and anti-SIRPα.ct, respectively. The same amount of protein was used for IP as confirmed by the actin blots. D) FACS analysis to determine SIRPα in monocytes labeled under cell permeable and non-permeable conditions.

    Journal: PLoS ONE

    Article Title: 'Clustering' SIRP? into the Plasma Membrane Lipid Microdomains Is Required for Activated Monocytes and Macrophages to Mediate Effective Cell Surface Interactions with CD47

    doi: 10.1371/journal.pone.0077615

    Figure Lengend Snippet: Expression of SIRPα on monocytes. Detection of SIRPα by WB in freshly isolated human PBMC and PMN using anti-SIRPα.ex (SIRPα.ex) and anti-SIRPα.ct (SIRPα.ct) antibodies. B) Immunofluorescence staining of PBMC. Cell surface SIRPα was labeled with anti-SIRPα.ex under non-permeable conditions. Monocytes (arrow heads) were defined by anti-human CD14 antibody, and T and B lymphocytes were defined with anti-Lck and anti-B220 antibodies, respectively. C) Determination of the distribution of SIRPα in PMN and monocytes by cell biotinylation. Cells were biotinylated with either NHS-biotin (cell permeable) or sulfo-NHS-biotin (non-cell permeable), followed by the IP of SIRPα from the lysates. Biotinylated and total SIRPα were blotted by streptavidin-HRP and anti-SIRPα.ct, respectively. The same amount of protein was used for IP as confirmed by the actin blots. D) FACS analysis to determine SIRPα in monocytes labeled under cell permeable and non-permeable conditions.

    Article Snippet: A biotinylated protein marker ranging from 40-250 kD (BioRad) was ultracentrifugated along with the cell lysates to serve as the MW reference.

    Techniques: Expressing, Western Blot, Isolation, Immunofluorescence, Staining, Labeling, FACS

    (a) Molecular mass estimation of the capsid protein of NA1 particles purified by CsCl density gradient centrifugation. M, molecular masses of biotinylated standard proteins (kDa). Track 1: bovine IgG as a control for blotting and staining with the anti‐bovine conjugate; track 2: biotinylated standard proteins; track 3: biotinylated standard proteins plus the NA1 capsid protein; track 4: the NA1 capsid protein; arrow indicates the NA1 protein. (b) Molecular mass estimation of the capsid protein of FCV grown in CRFK cells using the same electrophoresis conditions as those used for NA1. Arrow indicates the FCV capsid protein. M, molecular masses of biotinylated standard proteins (kDa). Track 1: preparation from uninfected CRFK cells; track 2: biotinylated standard proteins plus the preparation from FCV‐infected cells; track 3: FCV‐infected cells; track 4: rabbit IgG (the FCV NADC rabbit antiserum) used as a control for blotting and immunostaining with the anti‐rabbit conjugate.

    Journal: FEMS Microbiology Letters

    Article Title: Characterisation of the bovine enteric calici‐like virus, Newbury agent 1

    doi: 10.1111/j.1574-6968.2000.tb09370.x

    Figure Lengend Snippet: (a) Molecular mass estimation of the capsid protein of NA1 particles purified by CsCl density gradient centrifugation. M, molecular masses of biotinylated standard proteins (kDa). Track 1: bovine IgG as a control for blotting and staining with the anti‐bovine conjugate; track 2: biotinylated standard proteins; track 3: biotinylated standard proteins plus the NA1 capsid protein; track 4: the NA1 capsid protein; arrow indicates the NA1 protein. (b) Molecular mass estimation of the capsid protein of FCV grown in CRFK cells using the same electrophoresis conditions as those used for NA1. Arrow indicates the FCV capsid protein. M, molecular masses of biotinylated standard proteins (kDa). Track 1: preparation from uninfected CRFK cells; track 2: biotinylated standard proteins plus the preparation from FCV‐infected cells; track 3: FCV‐infected cells; track 4: rabbit IgG (the FCV NADC rabbit antiserum) used as a control for blotting and immunostaining with the anti‐rabbit conjugate.

    Article Snippet: A mixture of biotinylated protein markers (from 200 to 6.5 kDa; Bio‐Rad) was co‐run with the disrupted virus proteins for accurate molecular mass determinations.

    Techniques: Purification, Gradient Centrifugation, Staining, Electrophoresis, Infection, Immunostaining

    (a) Molecular mass estimation of the capsid protein of NA1 particles purified by CsCl density gradient centrifugation. M, molecular masses of biotinylated standard proteins (kDa). Track 1: bovine IgG as a control for blotting and staining with the anti-bovine conjugate; track 2: biotinylated standard proteins; track 3: biotinylated standard proteins plus the NA1 capsid protein; track 4: the NA1 capsid protein; arrow indicates the NA1 protein. (b) Molecular mass estimation of the capsid protein of FCV grown in CRFK cells using the same electrophoresis conditions as those used for NA1. Arrow indicates the FCV capsid protein. M, molecular masses of biotinylated standard proteins (kDa). Track 1: preparation from uninfected CRFK cells; track 2: biotinylated standard proteins plus the preparation from FCV-infected cells; track 3: FCV-infected cells; track 4: rabbit IgG (the FCV NADC rabbit antiserum) used as a control for blotting and immunostaining with the anti-rabbit conjugate.

    Journal: FEMS Microbiology Letters

    Article Title: Characterisation of the bovine enteric calici-like virus, Newbury agent 1

    doi: 10.1016/S0378-1097(00)00422-5

    Figure Lengend Snippet: (a) Molecular mass estimation of the capsid protein of NA1 particles purified by CsCl density gradient centrifugation. M, molecular masses of biotinylated standard proteins (kDa). Track 1: bovine IgG as a control for blotting and staining with the anti-bovine conjugate; track 2: biotinylated standard proteins; track 3: biotinylated standard proteins plus the NA1 capsid protein; track 4: the NA1 capsid protein; arrow indicates the NA1 protein. (b) Molecular mass estimation of the capsid protein of FCV grown in CRFK cells using the same electrophoresis conditions as those used for NA1. Arrow indicates the FCV capsid protein. M, molecular masses of biotinylated standard proteins (kDa). Track 1: preparation from uninfected CRFK cells; track 2: biotinylated standard proteins plus the preparation from FCV-infected cells; track 3: FCV-infected cells; track 4: rabbit IgG (the FCV NADC rabbit antiserum) used as a control for blotting and immunostaining with the anti-rabbit conjugate.

    Article Snippet: A mixture of biotinylated protein markers (from 200 to 6.5 kDa; Bio-Rad) was co-run with the disrupted virus proteins for accurate molecular mass determinations.

    Techniques: Purification, Gradient Centrifugation, Staining, Electrophoresis, Infection, Immunostaining