Architecture of low human and environmental impact.

Diante de um cenário de degradação ambiental global, escassez de matéria prima, água, energia, aumento da poluição, crise social e econômica, é feita a proposição de uma Arquitetura de Baixo Impacto Humano e Ambiental - ABIHA.Todas estas variáveis trazem novos elementos à Arquitetura aumentando a sua complexidade e fazendo com que haja necessidade de adaptação.Apesar de todas as incertezas e contradições envolvendo as questões de sustentabilidade, seus conceitos e sua aplicação na Arquitetura são abordados neste contexto.Além das questões conceituais, são apresentadas aplicações práticas da ABIHA, no Jardim Sustentável, na Reciclagem do Galpão da POLI e no MINI labiratório de Conforto e Eficiência Energética.Estas aplicações seriram de base para a proposta de Sistematização que é apresentada no final deste trabalho como parte das conclusões finais. Esta proposta é apenas início de muitas pesquisas que ainda devem ser feiras rumo a uma Arquitetura mais Sustentável.The actual global environmental context is one of fierce degradation : reflecting in the exhaustion of natural sources, increase of air, soil and water pollution, and social and economic crises.Facing such a scenario, it is proposed in this work, principles of architecture of low human environmental impact (arquitetura de baixo impacto humano e ambiental) - ABIHA.All these variables bring new parameters to the design of building, including their entire life cycles.Under these new ciecunstances it is observed an increae of the complexity in this design process, making necessary discussions for change.Despite all the uncertainties and contradictions about issues of sustainability, their concepts, as well as their applications are approached in the context of this work.Besides the conceptual matters, practions applications of ABIHA are carried out, in the example of the sustainable garden, warehouse recycling and the movable environmental laboratory (sensors and data lggers).Such experiences of practical application were fundamental to create the basis for the methodological assessment proposed as part of the final conclusions of this research.However, this procedure of evaluation is understood merely as the beginning of a big range of other researchs, which shlould be developed towards a more sustainable architecture

MOESM3 of Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer

Additional file 3. MS/MS Spectra from the Mascot DAT file imported in Skyline software as MS/MS library

MOESM4 of Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer

Additional file 4. MS/MS Filtering–transition setting tabs in Skyline software

MOESM7 of Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer

Additional file 7. Table summary of patients selected for the absolute quantification of the two isoforms of tAP-F13A1 by LC-PRM

MOESM5 of Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer

Additional file 5. Representative mass spectra of the AP-F13A1 activation peptide

Interaction of epitope-tagged Vangl2 and Vangl1 proteins.

<p>(<b>A</b>) Schematic diagram of Vangl1 and full-length and truncated mutants of Vangl2 used for this study. (<b>B</b>) Transient co-expression of myc-Vangl1 with GFP-Vangl2, GFP-Vangl2ΔN, GFP-Vangl2ΔC, GFP-Vangl2ΔNΔC a control protein (GFP in T47D cells and immunoprecipitation with myc antibody shows co-immunoprecitation of Vangl2 with Vangl1). (<b>C</b>) Colocalization of ectopically expressed Myc-Vangl1 and GFP-Vangl2 in T47D cells and analysis by immunofluorescence and confocal analysis. All images were taken under a 40×objective. Scale bar corresponds to 10 µm and is labelled in white. (<b>D</b>) Vangl2 homodimerization is displayed by immunoprecipitation with Myc antibody shows co-immunoprecitation of Myc-Vangl2 with GFP-Vangl2. Protein complexes were separated using SDS-PAGE and western blot analysis.</p

Generation of a highly specific anti-Vangl2 monoclonal antibody.

<p>(<b>A</b>) Expression of GST, GST-NVangl1 and GST-NVangl2 fusion proteins verified by SDS-PAGE and Coomassie staining. (<b>B</b>) Selected hybridomas were screened using an ELISA against GST, GST-NVangl1 and GST-NVangl2. mAb: monoclonal antibody. (<b>C</b>) Specificity of 2G4 mAb for GST-NVangl2 shown by western blot experiments, using antibodies specific for GST, Vangl2 and Vangl1/2. (<b>D</b>) SPR analysis using 2G4 mAb (10 µg/ml) injected over immobilized GST, GST-NVangl1 or GST-NVangl2. Sensorgrams show total signal from GST fusion proteins normalised with the non-specific signal (GST).</p

List of peptides observed for Vangl2 identification.

<p>List of peptides observed for Vangl2 identification.</p

List of peptides observed for Vangl1 identification.

<p>List of peptides observed for Vangl1 identification.</p

Identification of an endogenous protein complex containing the Vangl2 and Vangl1 proteins.

<p>(<b>A</b>) Specificity of 2G4 mAb was verified in western blot using T47D cell extracts expressing GFP, GFP-Vangl1, Vangl2 or GFP. Proteins were separated on SDS-PAGE and analyzed with western blot with specific antibodies. Specificity of 2G4 mAb in immunoprecipitation experiments GFP-Vangl1, GFP-Vangl2 or GFP expressed in T47D cells. Western blotting was carried out using 2G4 mAb, anti-GFP and Vangl1/2 antibodies. (<b>B</b>) SKBR7 cells were treated with shLuc or shVangl2 and assessed for Vangl expression. Vangl2 was immunoprecipitated from cell lysates and detected with the same 2G4 antibody. (<b>C</b>) Proteins were subsequently separated using Bis-Tris gradient gels and silver stained. Bands specific to 2G4 mAb were excised followed by in-gel trypsin digestion, chromatographic separation and orbitrap analysis. An asterisk indicates the bands corresponding to Vangl2. (<b>D</b>) Endogenous Vangl2 and Vangl1 were identified with the presence of multiple peptides and associated with a high probability Mascot scores (at least 40 arbitrary units). Bold characters indicate the peptides identified by mass spectrometry as shown with alignment of the two sequences. Regions shaded in grey correspond to the amino-terminal regions of Vangl1 and Vangl2.</p