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pyriine and 4-dimethylaminopyridine (4-dmap)  (Merck KGaA)

 
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    Merck KGaA pyriine and 4-dimethylaminopyridine (4-dmap)
    Pyriine And 4 Dimethylaminopyridine (4 Dmap), supplied by Merck KGaA, 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/apo-e2/human+recombinant+apoe2++3++and+4+produced+in+s++frugiperda/pm23121936-49-2-7
    Average 90 stars, based on 1 article reviews
    pyriine and 4-dimethylaminopyridine (4-dmap) - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Metal(loid) exposure assessment and biomarker responses in captive and free-ranging European brown bear (Ursus arctos).
    Article Snippet: The malondialdehyde (MDA) as an index of lipid peroxidation was measured using a highperformance liquid chromatography based (HPLC; Shimadzu Corporation, Kyoto, Japan) thiobarbituric acid (TBA) assay (Drury et al. 1997). .. Within the HPLC apparatus, degasser, isocratic pump, column oven, Shimadzu UV detector set at 532 nm, C-18 reverse-phase (LiChrospher, Merck, Darmstadt, Germany) guard column and analytical column with 5 μm particles (4.0x4.0 and 4.0x125.0 mm, respectively) were used. ..

    Purification:

    Article Title: Coupling of soft-modeling methods with multivariate pattern recognition technique for the identification of nitroaniline isomers
    Article Snippet: A new approach that takes advantage of both soft-modeling and pattern recognition methods is proposed to analyze kinetic data monitored spectrometrically to classify structurally similar nitroaniline isomers.. The colorimetric condensation reaction of 1,2-naphthoquinone-4-sulfonate (NQS) with amines has been used to classify 2-, 3-, and 4-nitroaniline on the basis of their different kinetic properties.. These nitroanilines react differentially with NQS at pH 7 to produce a colored product.

    Article Title: Tissue transglutaminase-catalysed cross-linking induces Apolipoprotein E multimers inhibiting Apolipoprotein E's protective effects towards amyloid-beta-induced toxicity.
    Article Snippet: .. Human recombinant ApoE2, 3, and 4 produced in S. frugiperda were obtained from Merck Millipore (Billerica, MA, USA) and human plasma purified ApoE3 (ApoE3L) from rPeptide (A-2001-1, Bogart, GA, USA). .. Human recombinant tTG (T002, Zedira GmbH, Darmstadt, Germany) was reconstituted in MilliQ water at a stock concentration of 1 mg/mL.

    other:

    Article Title: Synthesis of PCEC Copolymers with Controlled Molecular Weight Using Full Factorial Methodology
    Article Snippet: PEG with average molecular weight of 1, 2, 3 and 4 KDa, ε-caprolactone monomer, dichloromethane and n-hexane was purchased from Merck chemical company (Germany), stannous octoate was obtained from Alfa Aesar, A Johnson Matthey Company (Germany).

    Article Title: Selective sulfation of carrageenans and the influence of sulfate regiochemistry on anticoagulant properties.
    Article Snippet: Pyriine and 4-dimethylaminopyridine (4-DMAP) were purchased rom Merck (Germany).

    Recombinant:

    Article Title: Tissue transglutaminase-catalysed cross-linking induces Apolipoprotein E multimers inhibiting Apolipoprotein E's protective effects towards amyloid-beta-induced toxicity.
    Article Snippet: .. Human recombinant ApoE2, 3, and 4 produced in S. frugiperda were obtained from Merck Millipore (Billerica, MA, USA) and human plasma purified ApoE3 (ApoE3L) from rPeptide (A-2001-1, Bogart, GA, USA). .. Human recombinant tTG (T002, Zedira GmbH, Darmstadt, Germany) was reconstituted in MilliQ water at a stock concentration of 1 mg/mL.

    Produced:

    Article Title: Tissue transglutaminase-catalysed cross-linking induces Apolipoprotein E multimers inhibiting Apolipoprotein E's protective effects towards amyloid-beta-induced toxicity.
    Article Snippet: .. Human recombinant ApoE2, 3, and 4 produced in S. frugiperda were obtained from Merck Millipore (Billerica, MA, USA) and human plasma purified ApoE3 (ApoE3L) from rPeptide (A-2001-1, Bogart, GA, USA). .. Human recombinant tTG (T002, Zedira GmbH, Darmstadt, Germany) was reconstituted in MilliQ water at a stock concentration of 1 mg/mL.

    Clinical Proteomics:

    Article Title: Tissue transglutaminase-catalysed cross-linking induces Apolipoprotein E multimers inhibiting Apolipoprotein E's protective effects towards amyloid-beta-induced toxicity.
    Article Snippet: .. Human recombinant ApoE2, 3, and 4 produced in S. frugiperda were obtained from Merck Millipore (Billerica, MA, USA) and human plasma purified ApoE3 (ApoE3L) from rPeptide (A-2001-1, Bogart, GA, USA). .. Human recombinant tTG (T002, Zedira GmbH, Darmstadt, Germany) was reconstituted in MilliQ water at a stock concentration of 1 mg/mL.



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    GA-modified proteins act as a ligand of <t>apoE.</t> A, pulldown assay for detection of binding proteins for GA-modified proteins in mouse serum. BSA coupled to Dynabeads was incubated with 25 mm GA in PBS for 1 or 7 days to obtain GA-modified protein-coupled beads. The mouse serum was incubated with the ligand-coupled beads for 1 h at room temperature. The ligands used were BSA and GA-BSA. Proteins bound to the beads were eluted by addition of sample buffer, heating (95 °C, 5 min), and separation by SDS-PAGE. The proteins indicated by the arrowheads represent thrombospondin 1 (band 1), complement factor H–related protein C (band 2), coagulation factor XIII A chain (band 3), serotransferrin (band 4), antithrombin (band 5), apolipoprotein E (band 6), and metalloproteinase inhibitor 3 (band 7), as identified by LC-MS/MS analysis. B, binding of modified proteins to apoE. Serum proteins bound to the beads were prepared and separated by SDS-PAGE as described in A. ApoE was detected by immunoblotting with anti-apoE mAb E6D7 (Abcam). WB, Western blot. C, binding of GA-modified proteins or pentylamines to the apoE <t>isoforms.</t> The apoE isoforms (2 μg/ml) were immobilized on a plate and incubated with biotin-labeled BSA or GA-BSA (50 μg/ml) (left panel) or with biotin-labeled N-pentylamine (PA) or GA-PA (0.5 mm) (right panel) at 37 °C for 1 h. Data are from single experiments performed in triplicate wells and are representative of three individual experiments. The results shown are means ± S.D. (n = 3). D, pulldown assay for binding of GA-modified proteins to the apoE isoforms. Three apoE isoforms were incubated separately with ligand-coupled beads for 1 h at room temperature. The ligands used were BSA, BDA-BSA, and GA-BSA. Proteins bound to the beads were eluted by addition of sample buffer, heating, and separation by SDS-PAGE. The apoE isoforms were detected by immunoblotting with anti-apoE mAb E6D7. E, levels of the antibody titers against antigens (BSA, BDA-BSA, and GA-BSA) in sera from 12 weeks of male control and spontaneously hyperlipidemic mice. Elevations of IgG (left panel) or IgM (right panel) immune responses in the serum samples were measured by ELISA using native BSA, BDA-BSA, and GA-BSA as the coating antigens. *, p < 0.05; **, p < 0.01. The results shown are means ± S.D. (n = 3).
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    Image Search Results


    GA-modified proteins act as a ligand of apoE. A, pulldown assay for detection of binding proteins for GA-modified proteins in mouse serum. BSA coupled to Dynabeads was incubated with 25 mm GA in PBS for 1 or 7 days to obtain GA-modified protein-coupled beads. The mouse serum was incubated with the ligand-coupled beads for 1 h at room temperature. The ligands used were BSA and GA-BSA. Proteins bound to the beads were eluted by addition of sample buffer, heating (95 °C, 5 min), and separation by SDS-PAGE. The proteins indicated by the arrowheads represent thrombospondin 1 (band 1), complement factor H–related protein C (band 2), coagulation factor XIII A chain (band 3), serotransferrin (band 4), antithrombin (band 5), apolipoprotein E (band 6), and metalloproteinase inhibitor 3 (band 7), as identified by LC-MS/MS analysis. B, binding of modified proteins to apoE. Serum proteins bound to the beads were prepared and separated by SDS-PAGE as described in A. ApoE was detected by immunoblotting with anti-apoE mAb E6D7 (Abcam). WB, Western blot. C, binding of GA-modified proteins or pentylamines to the apoE isoforms. The apoE isoforms (2 μg/ml) were immobilized on a plate and incubated with biotin-labeled BSA or GA-BSA (50 μg/ml) (left panel) or with biotin-labeled N-pentylamine (PA) or GA-PA (0.5 mm) (right panel) at 37 °C for 1 h. Data are from single experiments performed in triplicate wells and are representative of three individual experiments. The results shown are means ± S.D. (n = 3). D, pulldown assay for binding of GA-modified proteins to the apoE isoforms. Three apoE isoforms were incubated separately with ligand-coupled beads for 1 h at room temperature. The ligands used were BSA, BDA-BSA, and GA-BSA. Proteins bound to the beads were eluted by addition of sample buffer, heating, and separation by SDS-PAGE. The apoE isoforms were detected by immunoblotting with anti-apoE mAb E6D7. E, levels of the antibody titers against antigens (BSA, BDA-BSA, and GA-BSA) in sera from 12 weeks of male control and spontaneously hyperlipidemic mice. Elevations of IgG (left panel) or IgM (right panel) immune responses in the serum samples were measured by ELISA using native BSA, BDA-BSA, and GA-BSA as the coating antigens. *, p < 0.05; **, p < 0.01. The results shown are means ± S.D. (n = 3).

    Journal: The Journal of Biological Chemistry

    Article Title: Glycolaldehyde is an endogenous source of lysine N -pyrrolation

    doi: 10.1074/jbc.RA120.013179

    Figure Lengend Snippet: GA-modified proteins act as a ligand of apoE. A, pulldown assay for detection of binding proteins for GA-modified proteins in mouse serum. BSA coupled to Dynabeads was incubated with 25 mm GA in PBS for 1 or 7 days to obtain GA-modified protein-coupled beads. The mouse serum was incubated with the ligand-coupled beads for 1 h at room temperature. The ligands used were BSA and GA-BSA. Proteins bound to the beads were eluted by addition of sample buffer, heating (95 °C, 5 min), and separation by SDS-PAGE. The proteins indicated by the arrowheads represent thrombospondin 1 (band 1), complement factor H–related protein C (band 2), coagulation factor XIII A chain (band 3), serotransferrin (band 4), antithrombin (band 5), apolipoprotein E (band 6), and metalloproteinase inhibitor 3 (band 7), as identified by LC-MS/MS analysis. B, binding of modified proteins to apoE. Serum proteins bound to the beads were prepared and separated by SDS-PAGE as described in A. ApoE was detected by immunoblotting with anti-apoE mAb E6D7 (Abcam). WB, Western blot. C, binding of GA-modified proteins or pentylamines to the apoE isoforms. The apoE isoforms (2 μg/ml) were immobilized on a plate and incubated with biotin-labeled BSA or GA-BSA (50 μg/ml) (left panel) or with biotin-labeled N-pentylamine (PA) or GA-PA (0.5 mm) (right panel) at 37 °C for 1 h. Data are from single experiments performed in triplicate wells and are representative of three individual experiments. The results shown are means ± S.D. (n = 3). D, pulldown assay for binding of GA-modified proteins to the apoE isoforms. Three apoE isoforms were incubated separately with ligand-coupled beads for 1 h at room temperature. The ligands used were BSA, BDA-BSA, and GA-BSA. Proteins bound to the beads were eluted by addition of sample buffer, heating, and separation by SDS-PAGE. The apoE isoforms were detected by immunoblotting with anti-apoE mAb E6D7. E, levels of the antibody titers against antigens (BSA, BDA-BSA, and GA-BSA) in sera from 12 weeks of male control and spontaneously hyperlipidemic mice. Elevations of IgG (left panel) or IgM (right panel) immune responses in the serum samples were measured by ELISA using native BSA, BDA-BSA, and GA-BSA as the coating antigens. *, p < 0.05; **, p < 0.01. The results shown are means ± S.D. (n = 3).

    Article Snippet: The recombinant human apoE isoforms (E2, E3, and E4) were obtained from PeproTech.

    Techniques: Modification, Binding Assay, Incubation, SDS Page, Coagulation, Liquid Chromatography with Mass Spectroscopy, Western Blot, Labeling, Control, Enzyme-linked Immunosorbent Assay