spectinomycin resistance cassette  (Millipore)


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  • 99
    Name:
    Spectinomycin
    Description:
    Chemical structure aminoglycoside
    Catalog Number:
    s0692
    Price:
    None
    Applications:
    Spectinomycin is an aminocyclitol antibiotic derived from Streptomyces spectabilis. It has been shown to have a wide variety of uses, including treating acute gonorrheal urethritis and cervictis, to mark cell layers to monitor cell fate during leaf development, as a selection marker in plant related transformation systems for plant cells containing the marker gene Spcr, to study respiratory tract infections of cattle caused by Pasteurella multocida and Mannheimia haemolytica, and to generate plants deficient for the plastid-encoded RNA polymerase on MS-agar media. Spectinomycin also has use in amplification of low copy number plasmid carrying replicons. It is recommended for use in cell culture applications at 7.5-20 mg/L.
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    Structured Review

    Millipore spectinomycin resistance cassette
    (A) Schematic representation of the insertion of transcriptional luxAB fusions into the cmp locus of the Synechococcus chromosome. The recombinational plasmid pYK5, which cannot replicate in the cyanobacterium, contains a promoterless luxAB gene cluster, a <t>spectinomycin</t> resistance cassette ( spe r ), and a PlacI q :: ntcA transcriptional fusion, which are flanked by Synechococcus cmpB and cmpC genes. Various fragments of the nirA-nirB intergenic region were cloned between the Spe I (Sp) and Bgl II (Bg) sites preceding the luxAB gene cluster. Transformation of Synechococcus with the plasmid resulted in spectinomycin-resistant strains in which homologous recombination had transferred the reporter construct to the cyanobacterial chromosome. (B) The nirA-nirB intergenic region of Synechococcus sp. strain PCC 7942, showing the nucleotide sequences of both DNA strands. Numbers above the sequences indicate positions of the nucleotides with respect to the translation start site of nirA . The transcription start sites of the nirA and nirB operons are indicated by filled triangles. The putative −10 elements of the promoters of the nirA and nirB operons are underlined. The three NtcA-binding sites ( nir I, nir II, and nir III) and the two potential binding sites for LysR-type DNA-binding proteins (L1 and L2) are boxed. The letters above and below the sequences represent the base replacements created in strains YKA4, YKA5, YKA6, YKA7, YKA9, and YKB4. Sites of the luxAB fusion are also indicated.
    Chemical structure aminoglycoside
    https://www.bioz.com/result/spectinomycin resistance cassette/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    spectinomycin resistance cassette - by Bioz Stars, 2020-07
    99/100 stars

    Images

    1) Product Images from "cis-Acting Sequences Required for NtcB-Dependent, Nitrite-Responsive Positive Regulation of the Nitrate Assimilation Operon in the Cyanobacterium Synechococcus sp. Strain PCC 7942"

    Article Title: cis-Acting Sequences Required for NtcB-Dependent, Nitrite-Responsive Positive Regulation of the Nitrate Assimilation Operon in the Cyanobacterium Synechococcus sp. Strain PCC 7942

    Journal: Journal of Bacteriology

    doi:

    (A) Schematic representation of the insertion of transcriptional luxAB fusions into the cmp locus of the Synechococcus chromosome. The recombinational plasmid pYK5, which cannot replicate in the cyanobacterium, contains a promoterless luxAB gene cluster, a spectinomycin resistance cassette ( spe r ), and a PlacI q :: ntcA transcriptional fusion, which are flanked by Synechococcus cmpB and cmpC genes. Various fragments of the nirA-nirB intergenic region were cloned between the Spe I (Sp) and Bgl II (Bg) sites preceding the luxAB gene cluster. Transformation of Synechococcus with the plasmid resulted in spectinomycin-resistant strains in which homologous recombination had transferred the reporter construct to the cyanobacterial chromosome. (B) The nirA-nirB intergenic region of Synechococcus sp. strain PCC 7942, showing the nucleotide sequences of both DNA strands. Numbers above the sequences indicate positions of the nucleotides with respect to the translation start site of nirA . The transcription start sites of the nirA and nirB operons are indicated by filled triangles. The putative −10 elements of the promoters of the nirA and nirB operons are underlined. The three NtcA-binding sites ( nir I, nir II, and nir III) and the two potential binding sites for LysR-type DNA-binding proteins (L1 and L2) are boxed. The letters above and below the sequences represent the base replacements created in strains YKA4, YKA5, YKA6, YKA7, YKA9, and YKB4. Sites of the luxAB fusion are also indicated.
    Figure Legend Snippet: (A) Schematic representation of the insertion of transcriptional luxAB fusions into the cmp locus of the Synechococcus chromosome. The recombinational plasmid pYK5, which cannot replicate in the cyanobacterium, contains a promoterless luxAB gene cluster, a spectinomycin resistance cassette ( spe r ), and a PlacI q :: ntcA transcriptional fusion, which are flanked by Synechococcus cmpB and cmpC genes. Various fragments of the nirA-nirB intergenic region were cloned between the Spe I (Sp) and Bgl II (Bg) sites preceding the luxAB gene cluster. Transformation of Synechococcus with the plasmid resulted in spectinomycin-resistant strains in which homologous recombination had transferred the reporter construct to the cyanobacterial chromosome. (B) The nirA-nirB intergenic region of Synechococcus sp. strain PCC 7942, showing the nucleotide sequences of both DNA strands. Numbers above the sequences indicate positions of the nucleotides with respect to the translation start site of nirA . The transcription start sites of the nirA and nirB operons are indicated by filled triangles. The putative −10 elements of the promoters of the nirA and nirB operons are underlined. The three NtcA-binding sites ( nir I, nir II, and nir III) and the two potential binding sites for LysR-type DNA-binding proteins (L1 and L2) are boxed. The letters above and below the sequences represent the base replacements created in strains YKA4, YKA5, YKA6, YKA7, YKA9, and YKB4. Sites of the luxAB fusion are also indicated.

    Techniques Used: Plasmid Preparation, Clone Assay, Transformation Assay, Homologous Recombination, Construct, Periodic Counter-current Chromatography, Binding Assay, DNA Binding Assay

    Related Articles

    Sample Prep:

    Article Title: mRNA Translocation Occurs During the Second Step of Ribosomal Intersubunit Rotation
    Article Snippet: .. Materials and sample preparation tRNAfMet was purchased from MP Biomedicals; GTP, GDPNP, fusidic acid, spectinomycin, hygromycin B, tRNAPhe and tRNAMet were purchased from Sigma. .. GDP was further purified from contaminating GMP and GTP using ion-exchange chromatography as previously described .

    Expressing:

    Article Title: Transforming growth factor beta (TGF-β) is activated by the CtBP2-p300-AP1 transcriptional complex in chronic renal failure
    Article Snippet: .. Immunoprecipitation and mass spectrometry Cells expressing pCDNA3-2×Flag-c-FOS or pCDNA3-2×Flag-c-Jun were lysed using 1× RIPA buffer containing 1×protease inhibitor (Sigma-Aldrich, #S8830), followed by centrifuging at 13,000 rpm for 15 min. .. The supernatant was immunoprecipitated with anti-Flag agarose (Sigma-Aldrich, #A2220).

    Article Title: Characterization of the ERG-regulated Kinome in Prostate Cancer Identifies TNIK as a Potential Therapeutic Target
    Article Snippet: .. Kinome Enrichment and Profiling by Mass Spectrometry DU145 cells containing the empty vector or stably expressing ERG were SILAC labeled in RPMI 1640 (RPMI R1780–500 ML, Sigma) supplemented with 382 μM L -leucine and either 219 μM L -lysine and 287 μM L -arginine (light labeled) or equal concentrations of L -[13C6 15N2 ]-lysine and L -[13C6 15N4 ]-arginine (heavy labeled) (Silantes), 10% (v/v) dialysed FBS (Hyclone) and 1% (v/v) penicillin/streptomycin (Gibco). .. The SILAC labels for DU145 empty vector and ERG expressing cells were switched in the second biological replicate.

    Stable Transfection:

    Article Title: Characterization of the ERG-regulated Kinome in Prostate Cancer Identifies TNIK as a Potential Therapeutic Target
    Article Snippet: .. Kinome Enrichment and Profiling by Mass Spectrometry DU145 cells containing the empty vector or stably expressing ERG were SILAC labeled in RPMI 1640 (RPMI R1780–500 ML, Sigma) supplemented with 382 μM L -leucine and either 219 μM L -lysine and 287 μM L -arginine (light labeled) or equal concentrations of L -[13C6 15N2 ]-lysine and L -[13C6 15N4 ]-arginine (heavy labeled) (Silantes), 10% (v/v) dialysed FBS (Hyclone) and 1% (v/v) penicillin/streptomycin (Gibco). .. The SILAC labels for DU145 empty vector and ERG expressing cells were switched in the second biological replicate.

    Isolation:

    Article Title: Heat stress transcripts, differential expression, and profiling of heat stress tolerant gene TaHsp90 in Indian wheat (Triticum aestivum L.) cv C306
    Article Snippet: .. C306 was isolated from leaf samples using Spectrum Plant RNA isolation kit (Sigma, USA). ..

    Labeling:

    Article Title: Characterization of the ERG-regulated Kinome in Prostate Cancer Identifies TNIK as a Potential Therapeutic Target
    Article Snippet: .. Kinome Enrichment and Profiling by Mass Spectrometry DU145 cells containing the empty vector or stably expressing ERG were SILAC labeled in RPMI 1640 (RPMI R1780–500 ML, Sigma) supplemented with 382 μM L -leucine and either 219 μM L -lysine and 287 μM L -arginine (light labeled) or equal concentrations of L -[13C6 15N2 ]-lysine and L -[13C6 15N4 ]-arginine (heavy labeled) (Silantes), 10% (v/v) dialysed FBS (Hyclone) and 1% (v/v) penicillin/streptomycin (Gibco). .. The SILAC labels for DU145 empty vector and ERG expressing cells were switched in the second biological replicate.

    Immunoprecipitation:

    Article Title: Transforming growth factor beta (TGF-β) is activated by the CtBP2-p300-AP1 transcriptional complex in chronic renal failure
    Article Snippet: .. Immunoprecipitation and mass spectrometry Cells expressing pCDNA3-2×Flag-c-FOS or pCDNA3-2×Flag-c-Jun were lysed using 1× RIPA buffer containing 1×protease inhibitor (Sigma-Aldrich, #S8830), followed by centrifuging at 13,000 rpm for 15 min. .. The supernatant was immunoprecipitated with anti-Flag agarose (Sigma-Aldrich, #A2220).

    Mass Spectrometry:

    Article Title: Transforming growth factor beta (TGF-β) is activated by the CtBP2-p300-AP1 transcriptional complex in chronic renal failure
    Article Snippet: .. Immunoprecipitation and mass spectrometry Cells expressing pCDNA3-2×Flag-c-FOS or pCDNA3-2×Flag-c-Jun were lysed using 1× RIPA buffer containing 1×protease inhibitor (Sigma-Aldrich, #S8830), followed by centrifuging at 13,000 rpm for 15 min. .. The supernatant was immunoprecipitated with anti-Flag agarose (Sigma-Aldrich, #A2220).

    Article Title: Characterization of the ERG-regulated Kinome in Prostate Cancer Identifies TNIK as a Potential Therapeutic Target
    Article Snippet: .. Kinome Enrichment and Profiling by Mass Spectrometry DU145 cells containing the empty vector or stably expressing ERG were SILAC labeled in RPMI 1640 (RPMI R1780–500 ML, Sigma) supplemented with 382 μM L -leucine and either 219 μM L -lysine and 287 μM L -arginine (light labeled) or equal concentrations of L -[13C6 15N2 ]-lysine and L -[13C6 15N4 ]-arginine (heavy labeled) (Silantes), 10% (v/v) dialysed FBS (Hyclone) and 1% (v/v) penicillin/streptomycin (Gibco). .. The SILAC labels for DU145 empty vector and ERG expressing cells were switched in the second biological replicate.

    Plasmid Preparation:

    Article Title: Characterization of the ERG-regulated Kinome in Prostate Cancer Identifies TNIK as a Potential Therapeutic Target
    Article Snippet: .. Kinome Enrichment and Profiling by Mass Spectrometry DU145 cells containing the empty vector or stably expressing ERG were SILAC labeled in RPMI 1640 (RPMI R1780–500 ML, Sigma) supplemented with 382 μM L -leucine and either 219 μM L -lysine and 287 μM L -arginine (light labeled) or equal concentrations of L -[13C6 15N2 ]-lysine and L -[13C6 15N4 ]-arginine (heavy labeled) (Silantes), 10% (v/v) dialysed FBS (Hyclone) and 1% (v/v) penicillin/streptomycin (Gibco). .. The SILAC labels for DU145 empty vector and ERG expressing cells were switched in the second biological replicate.

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  • 98
    Millipore anti meprin α
    Meprins are important for epithelial monolayer integrity. ( a ) Addition of 40 nM activated human recombinant <t>meprin</t> α and meprin β increased TRITC-dextran permeability of A549 cells (*p
    Anti Meprin α, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti meprin α/product/Millipore
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti meprin α - by Bioz Stars, 2020-07
    98/100 stars
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    99
    Millipore active glp 1
    Glucose (A), insulin (B), glucagon (C), active glucagon-like peptide-1 <t>(GLP-1)</t> (D), oxyntomodulin (E), glicentin (F) and GIP (G) levels during mixed-meal test (MMT). Mean and 95% CI plotted. Inset graphs show area under the curve (AUC) values over 0–180 min. Black, before surgery (Pre); red, 1 month after surgery; green, 3 months; blue, 12 months. Mixed-effects model analysis, Dunnett’s multiple comparisons test for repeated measures used to compare AUC values for Pre versus indicated times after surgery. *P
    Active Glp 1, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 102 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Price from $9.99 to $1999.99
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    Image Search Results


    Meprins are important for epithelial monolayer integrity. ( a ) Addition of 40 nM activated human recombinant meprin α and meprin β increased TRITC-dextran permeability of A549 cells (*p

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Meprins are important for epithelial monolayer integrity. ( a ) Addition of 40 nM activated human recombinant meprin α and meprin β increased TRITC-dextran permeability of A549 cells (*p

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Recombinant, Permeability

    Meprins do not influence inflammatory infiltrate after 14 days bleomycin treatment. ( a ) Representation of the cell counts from broncho-alveolar lavage fluid (BALF) from meprin α, meprin β meprin αβ and wt littermates mice after 14 days saline or bleomycin treatment (*p

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Meprins do not influence inflammatory infiltrate after 14 days bleomycin treatment. ( a ) Representation of the cell counts from broncho-alveolar lavage fluid (BALF) from meprin α, meprin β meprin αβ and wt littermates mice after 14 days saline or bleomycin treatment (*p

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Mouse Assay

    Meprin β KO mice have less collagen deposition in comparison to wt littermates and meprin β localize in region rich with immature collagen. Quantification of ( a ) fibrosis and ( b ) tissue density from masson’s trichrome staining slides of meprin α, meprin β meprin αβ KO and wt littermates mice after 14 days saline or bleomycin treatment (*p

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Meprin β KO mice have less collagen deposition in comparison to wt littermates and meprin β localize in region rich with immature collagen. Quantification of ( a ) fibrosis and ( b ) tissue density from masson’s trichrome staining slides of meprin α, meprin β meprin αβ KO and wt littermates mice after 14 days saline or bleomycin treatment (*p

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Mouse Assay, Staining

    Meprin β is regulated by TGF-β1 in epithelial cells. mRNA expression level of meprin β and meprin α upon TGF-β1 (10 ng/ml) ( a , c respectively) and TNF-α (1 ng/ml) ( b,d respectively) stimulation on A549 cells for the indicated time points (*p

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Meprin β is regulated by TGF-β1 in epithelial cells. mRNA expression level of meprin β and meprin α upon TGF-β1 (10 ng/ml) ( a , c respectively) and TNF-α (1 ng/ml) ( b,d respectively) stimulation on A549 cells for the indicated time points (*p

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Expressing

    Lack of meprins do not influence bleomycin induced phenotype. ( a ) H E and ( b ) Masson’s Trichrome staining of lung section from wt littermates, meprin α, meprin β, meprin αβ KO mice after 14 days saline or bleomycin treatment. Scale bars show 200 μm.

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Lack of meprins do not influence bleomycin induced phenotype. ( a ) H E and ( b ) Masson’s Trichrome staining of lung section from wt littermates, meprin α, meprin β, meprin αβ KO mice after 14 days saline or bleomycin treatment. Scale bars show 200 μm.

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Staining, Mouse Assay

    The localisation of Meprin β but not Meprin α changes upon bleomycin treatment. Representative pictures of immunohistochemical staining for ( a ) meprin α and ( b ) meprin β in mouse saline (n = 4) and bleomycin treated lungs (n = 5), after 14 days bleomycin injection. Arrows point at meprin staining in epithelial cells, while arrowheads point at meprin staining in inflammatory cells. Scale bars show 50 μm. ( c ) Representative pictures of immunohistochemical staining in serial slides for pro-surfactant protein C (pro-SPC), α-smooth muscle actin (α-SMA), von willebrand factor (vWF), meprin α and meprin β. Arrows point at positive staining for meprin β and pro-SPC. Scale bars show 50 μm in the overview picture and 10 μm in the zoomed area.

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: The localisation of Meprin β but not Meprin α changes upon bleomycin treatment. Representative pictures of immunohistochemical staining for ( a ) meprin α and ( b ) meprin β in mouse saline (n = 4) and bleomycin treated lungs (n = 5), after 14 days bleomycin injection. Arrows point at meprin staining in epithelial cells, while arrowheads point at meprin staining in inflammatory cells. Scale bars show 50 μm. ( c ) Representative pictures of immunohistochemical staining in serial slides for pro-surfactant protein C (pro-SPC), α-smooth muscle actin (α-SMA), von willebrand factor (vWF), meprin α and meprin β. Arrows point at positive staining for meprin β and pro-SPC. Scale bars show 50 μm in the overview picture and 10 μm in the zoomed area.

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Immunohistochemistry, Staining, Injection

    Lung function is not preserved in meprins KO mice upon bleomycin treatment. Assessment by flexivent of ( a ) static compliance (Cst) and ( b ) total lung capacity (A) in wt littermates, meprin α, meprin β meprin αβ KO mice after 14 days saline or bleomycin treatment (*p

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Lung function is not preserved in meprins KO mice upon bleomycin treatment. Assessment by flexivent of ( a ) static compliance (Cst) and ( b ) total lung capacity (A) in wt littermates, meprin α, meprin β meprin αβ KO mice after 14 days saline or bleomycin treatment (*p

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Mouse Assay

    Meprins are expressed in inflammatory and epithelial cells of human lungs. ( a ) Serial slides staining for pro-surfactant protein-C (pro-SPC), alpha-smooth muscle actin (α-SMA), meprin α, and meprin β in lungs from donor (n = 4) and IPF (n = 4). Arrows and arrowheads indicate staining of meprins in epithelial cells and inflammatory cells respectively. Scale bars show 50 μm. ( b ) mRNA expression level of meprin α and meprin β in lung homogenate from donor (n = 10) and IPF (n = 12). Every dot correspond to a single donor or IPF patient, fewer n number than 10 (donor) and 12 (IPF) indicate non detectable samples.

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Meprins are expressed in inflammatory and epithelial cells of human lungs. ( a ) Serial slides staining for pro-surfactant protein-C (pro-SPC), alpha-smooth muscle actin (α-SMA), meprin α, and meprin β in lungs from donor (n = 4) and IPF (n = 4). Arrows and arrowheads indicate staining of meprins in epithelial cells and inflammatory cells respectively. Scale bars show 50 μm. ( b ) mRNA expression level of meprin α and meprin β in lung homogenate from donor (n = 10) and IPF (n = 12). Every dot correspond to a single donor or IPF patient, fewer n number than 10 (donor) and 12 (IPF) indicate non detectable samples.

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Staining, Expressing

    Absence of meprins does not prevent E-cadherin loss in bleomycin treatment mice. ( a ) mRNA and ( b ) protein level of E-cadherin in lung homogenate from meprin α, meprin β meprin αβ KO and wt littermates mice after 14 days saline or bleomycin treatment (*p

    Journal: Scientific Reports

    Article Title: Meprin β contributes to collagen deposition in lung fibrosis

    doi: 10.1038/srep39969

    Figure Lengend Snippet: Absence of meprins does not prevent E-cadherin loss in bleomycin treatment mice. ( a ) mRNA and ( b ) protein level of E-cadherin in lung homogenate from meprin α, meprin β meprin αβ KO and wt littermates mice after 14 days saline or bleomycin treatment (*p

    Article Snippet: The following dilutions of primary antibodies were used: for human samples anti-meprin β (1:100; AF2895 R & D), anti-meprin α (1:500, AF3220, R & D) anti-proSPC (1:1000; AB3786 Millipore, Vienna, Austria), anti-SMA (1:100; PA5–19465 Thermo Scientific).

    Techniques: Mouse Assay

    Glucose (A), insulin (B), glucagon (C), active glucagon-like peptide-1 (GLP-1) (D), oxyntomodulin (E), glicentin (F) and GIP (G) levels during mixed-meal test (MMT). Mean and 95% CI plotted. Inset graphs show area under the curve (AUC) values over 0–180 min. Black, before surgery (Pre); red, 1 month after surgery; green, 3 months; blue, 12 months. Mixed-effects model analysis, Dunnett’s multiple comparisons test for repeated measures used to compare AUC values for Pre versus indicated times after surgery. *P

    Journal: BMJ Open Diabetes Research & Care

    Article Title: Proglucagon peptide secretion profiles in type 2 diabetes before and after bariatric surgery: 1-year prospective study

    doi: 10.1136/bmjdrc-2019-001076

    Figure Lengend Snippet: Glucose (A), insulin (B), glucagon (C), active glucagon-like peptide-1 (GLP-1) (D), oxyntomodulin (E), glicentin (F) and GIP (G) levels during mixed-meal test (MMT). Mean and 95% CI plotted. Inset graphs show area under the curve (AUC) values over 0–180 min. Black, before surgery (Pre); red, 1 month after surgery; green, 3 months; blue, 12 months. Mixed-effects model analysis, Dunnett’s multiple comparisons test for repeated measures used to compare AUC values for Pre versus indicated times after surgery. *P

    Article Snippet: For the prospective study, active GLP-1 and GIP were measured by a customized Milliplex magnetic bead-based multianalyte human metabolic panel (Millipore HMHEMAG-34K).

    Techniques: