| 1. |
- Sköldberg, Håkan, et al.
(author)
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BIO-CCS I FJÄRRVÄRMESEKTORN – SYNTES
- 2022
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Reports (other academic/artistic)abstract
- Den svenska fjärrvärmesektorn har stor potential att bidra med negativa koldioxidutsläpp genom bio-CCS, minst 10 Mton per år. Den största osäkerheten beträffande möjligheterna för bio-CCS gäller marknads förutsättningarna. Uppvärmningsbranschen har en vision om att år 2045 utgöra en kolsänka. Ett sätt att åstadkomma detta är genom att avskilja och lagra koldioxidutsläpp med biogent ursprung. Ett antal fjärrvärmeföretag har redan olika långt gångna planer på att satsa på bio-CCS. De har sett ett värde i att samarbeta kring hur detta kan åstadkommas. Ett led i detta är projektet Bio-CCS i fjärrvärmesektorn som består av ett gediget underlag baserat på forskning kring olika aspekter av frågan samt en strategi baserad på det underlaget. I denna rapport redovisas en syntes av detta forskningsarbete. Projektet visar att fjärrvärmesektorn har stor teoretisk potential att bidra med negativa koldioxidutsläpp, minst 10 Mton per år. I huvudsak är avskiljning, transport och lagring av koldioxid beprövad teknik även om tillämpningen i detta fall är ny. Även om bio-CCS är förknippad med energianvändning så bidrar tekniken sett ur ett systemperspektiv med stor nytta för att minska koldioxid[1]utsläppen. Bio-CCS är en relativt dyr teknik och det är angeläget att utnyttja samverkan och kluster för att exempelvis skapa ökad kostnadseffektivitet i transport och mellanlagring. Tillgång till lagringsplatser är en förutsättning för framgång och flera alternativ bedöms bli tillgängliga. Det kan dock uppstå konkurrens om tillgången till lagringsplatserna. De regelmässiga förutsättningarna för bio-CCS i Sverige har förbättrats avsevärt de senaste dryga decenniet. Flera regelmässiga hinder kvarstår dock. En del utgör mindre barriärer, andra är av mer betydande karaktär. Den största osäkerheten beträffande möjligheterna för bio-CCS gäller ekonomin. Flera potentiella finansieringsmetoder har studerats, både stöd, regleringar och frivilligmarknader. Det finns fortfarande oklarheter kring syftet med planerade stöd och det framtida ägandet av de negativa utsläppen. Det genomförda projektet har skapat ett forum för kunskapsuppbyggnad, erfarenhetsutbyte och nätverkande, vilket de deltagande företagen bedömt vara mycket värdefullt.
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| 2. |
- Osong, Sinke Henshaw, et al.
(author)
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Crill : A novel technique to characterize nano-ligno-cellulose
- 2014
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In: Nordic Pulp & Paper Research Journal. - : Walter de Gruyter GmbH. - 0283-2631 .- 2000-0669. ; 29:2, s. 190-194
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Journal article (peer-reviewed)abstract
- The CrillEye is a technique for qualitatively assessing loose slender and fibrillar particles created during pulping. It has also been demonstrated that the crill measurement technique can easily be used to measure the degree of fibrillation of mechanical pulp based nano-ligno-cellulose (NLC). The measurement technique is based on an optical response of a suspension at two wavelengths of light; UV and IR. The UV light contains information on both fibres and crill, while IR only contains information on fibres. The resolution on the CrillEye module is based on optical response of the pulp and on an analogue signal analysis making it concentration independent. Characterization of particle-size distribution of nano-ligno-cellulose is both important and challenging. The objective of the work presented in this paper was to study the crill values of TMP and CTMP based nano-ligno-celluloses as a function of homogenization time. Results showed that the crill value of both TMP-NLC and CTMP-NLC correlated fairly well with the homogenization time.
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| 3. |
- Osong, Sinke Henshaw, et al.
(author)
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Development of nano-ligno-cellulose produced from mechanical pulp
- 2014
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In: International Mechanical Pulping Conference, IMPC 2014. - 9780000000002
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Conference paper (peer-reviewed)abstract
- The objective in this work was to develop a methodology for producing mechanical pulp based nano-ligno-cellulose (NLC) from fines fractions. Also there has been a great deal of enthusiasm to evaluate particle size distribution of NLC. In this work the crill characterisation technique was used. The crill values of TMP and CTMP based nano-ligno-celluloses were measured as a function of the homogenisation time. Results showed that the crill value of both TMP-NLC and CTMP-NLC correlated with the homogenisation time. Another objective was to utilise NLC as strength additives in paper and board grades. Laboratory sheets of CTMP and bleached kraft pulp (BKP), with the addition of their respective NLC, were made in a Rapid Kothen sheet former. It was found that handsheets of pulp fibres blended with NLC improved the z- strength and other important mechanical properties for similar sheet densities.
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| 4. |
- Gourdon, Mathias, 1980, et al.
(author)
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Pulp mill biorefineries
- 2013
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In: International Process Integration Jubilee Conference, Gothenburg, Sweden, March 18-20 2013.
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Conference paper (other academic/artistic)
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| 5. |
- Barbe, Laurent, et al.
(author)
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Toward a confocal subcellular atlas of the human proteome
- 2008
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In: Molecular and cellular proteomics. - 1535-9476 .- 1535-9484. ; 7:3, s. 499-508
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Journal article (peer-reviewed)abstract
- Information on protein localization on the subcellular level is important to map and characterize the proteome and to better understand cellular functions of proteins. Here we report on a pilot study of 466 proteins in three human cell lines aimed to allow large scale confocal microscopy analysis using protein-specific antibodies. Approximately 3000 high resolution images were generated, and more than 80% of the analyzed proteins could be classified in one or multiple subcellular compartment(s). The localizations of the proteins showed, in many cases, good agreement with the Gene Ontology localization prediction model. This is the first large scale antibody-based study to localize proteins into subcellular compartments using antibodies and confocal microscopy. The results suggest that this approach might be a valuable tool in conjunction with predictive models for protein localization.
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| 6. |
- Berglund, Lisa, et al.
(author)
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A genecentric Human Protein Atlas for expression profiles based on antibodies
- 2008
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In: Molecular & Cellular Proteomics. - 1535-9476 .- 1535-9484. ; 7:10, s. 2019-2027
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Research review (peer-reviewed)abstract
- An attractive path forward in proteomics is to experimentally annotate the human protein complement of the genome in a genecentric manner. Using antibodies, it might be possible to design protein-specific probes for a representative protein from every protein-coding gene and to subsequently use the antibodies for systematical analysis of cellular distribution and subcellular localization of proteins in normal and disease tissues. A new version (4.0) of the Human Protein Atlas has been developed in a genecentric manner with the inclusion of all human genes and splice variants predicted from genome efforts together with a visualization of each protein with characteristics such as predicted membrane regions, signal peptide, and protein domains and new plots showing the uniqueness (sequence similarity) of every fraction of each protein toward all other human proteins. The new version is based on tissue profiles generated from 6120 antibodies with more than five million immunohistochemistry-based images covering 5067 human genes, corresponding to approximately 25% of the human genome. Version 4.0 includes a putative list of members in various protein classes, both functional classes, such as kinases, transcription factors, G-protein-coupled receptors, etc., and project-related classes, such as candidate genes for cancer or cardiovascular diseases. The exact antigen sequence for the internally generated antibodies has also been released together with a visualization of the application-specific validation performed for each antibody, including a protein array assay, Western blot analysis, immunohistochemistry, and, for a large fraction, immunofluorescence-based confocal microscopy. New search functionalities have been added to allow complex queries regarding protein expression profiles, protein classes, and chromosome location. The new version of the protein atlas thus is a resource for many areas of biomedical research, including protein science and biomarker discovery.
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| 7. |
- Fagerberg, Linn, et al.
(author)
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Mapping the subcellular protein distribution in three human cell lines
- 2011
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In: Journal of Proteome Research. - : American Chemical Society (ACS). - 1535-3893 .- 1535-3907. ; 10:8, s. 3766-3777
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Journal article (peer-reviewed)abstract
- The subcellular locations of proteins are closely related to their function and constitute an essential aspect for understanding the complex machinery of living cells. A systematic effort has been initiated to map the protein distribution in three functionally different cell lines with the aim to provide a subcellular localization index for at least one representative protein from all human protein-encoding genes. Here, we present the results of over 4,000 proteins mapped to 16 subcellular compartments. The results indicate a ubiquitous protein expression with a majority of the proteins found in all three cell lines and a large portion localized to two or more compartments. The inter-relationships between the subcellular compartments are visualized in a protein-compartment network based on all detected proteins. Hierarchical clustering was performed to determine how closely related the organelles are in terms of protein constituents and compare the proteins detected in each cell type. Our results show distinct organelle proteomes, well conserved across the cell types, and demonstrate that biochemically similar organelles are grouped together.
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| 8. |
- Lundberg, Emma, et al.
(author)
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A novel method for reproducible fluorescent labeling of small amounts of antibodies on solid phase
- 2007
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In: JIM - Journal of Immunological Methods. - : Elsevier BV. - 0022-1759 .- 1872-7905. ; 322:1-2, s. 40-49
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Journal article (peer-reviewed)abstract
- Fluorescently labeled antibodies are very important tools in cell biology, providing for specific and quantitative detection of antigens. To date, fluorophore labeling of antibodies has been performed in solution and has been limited by low-throughput methods requiring a substantial amount of pure antibody sample at a high concentration. We have developed a novel solid-phase labeling protocol for small amounts (i.e. micrograms) of antibodies with fluorescent dyes. Protein A affinity medium was used as solid support in a micropipette tip format. This solid-phase approach, including the advantage of the strong and specific interaction between Protein A and antibodies, allows for simultaneous purification, labeling and concentration of the antibody sample, making it possible to start with unpure antibody samples at low concentrations. We have optimized the protocol with regard to reaction pH, time, temperature and amount of amine reactive dye. In addition, we have evaluated the stability and activity of the labeled antibodies. To evaluate the reproducibility and robustness of this method we labeled eight antibodies with amine reactive fluorescent dyes followed by evaluation of antibody specificity on protein arrays. Interestingly, this gave an extremely high conformity in the degree of labeling, showing the robustness of the method. The solid-phase method also gave predictable and reproducible results and by varying the amount of reactive dye, the desired degree of labeling can easily be achieved. Antibodies labeled using this solid-phase method were similar in stability and activity to antibodies labeled in solution. This novel solid-phase antibody labeling method may also be applicable for other conjugation chemistries and labels, and has potential for throughput applications.
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| 9. |
- Lundberg, Emma, 1980-
(author)
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Bioimaging for analysis of protein expression in cells and tissues using affinity reagents
- 2008
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Doctoral thesis (other academic/artistic)abstract
- The detection and analysis of biomolecules, such as proteins, are of great interest since these molecules are fundamental for life and our health. Due to the complexity of biological processes, there is a great advantage of studying proteins in their natural context, for example by using bioimaging. The objective of this doctoral thesis has been to develop, implement and evaluate techniques for the use of proteinspecific affinity reagents in diverse bioimaging platforms for analysis of protein expression in situ in cells and tissues. To be able to visualize a desired protein in situ using affinity reagents, reporter labels are needed. A novel technique for labeling of antibodies on solid phase was developed. This method offers simultaneous purification, concentration and labeling of an antibody sample, giving highly predictable and reproducible results, in a miniaturized format. Another study demonstrates the use of an alternative affinity reagent, the Affibody molecule, in bioimaging as well as other immunoassays. As a relevant proof-of-principle, an Affibody molecule binding the HER2 receptor was site-specificly labeled and employed for analysis of HER2 protein expression in cells and tissue using immunofluorescence (IF), immunohistochemistry (IHC), immunoprecipitation and flow cytometry. Furthermore, it is shown how antibody-based bioimaging approaches can be applied for systematic analysis of protein expression in terms of subcellular localization and expression levels in cell lines. The systematic subcellular localization of nearly 500 proteins was performed using IF and confocal microscopy. Global analysis of expression levels of nearly 2000 proteins in a panel of cell lines using IHC and automated image analysis, revealed that most proteins are expressed in a cell size dependent manner. Two normalization approaches were evaluated and found to allow for protein profiling across the panel of morphologically diverse cells, revealing patterns of protein over- and underexpression, and proteins with stable as well as with lineage specific expression were identified. Finally, the value of antibody-based, bioimaging proteomics as a platform for biomarker discovery is demonstrated. The identification and in depth study of a candidate biomarker for colorectal cancer, SATB2, is described using both IHC and IF bioimaging. Results from extended analyses of tumor biopsies showed that detection of SATB2 protein using IHC provides a clinically relevant diagnostic tool with high specificity and sensitivity to aid in diagnosis of colorectal cancer. Furthermore, the study demonstrated a potential prognostic role of SATB2, as decreased expression was associated with a significantly shorter overall survival in patients with advanced colorectal cancer.
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| 10. |
- Lundberg, Emma, et al.
(author)
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Site-specifically conjugated anti-HER2 Affibody® molecules as one-step reagents for target expression analyses on cells and xenograft samples
- 2007
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In: JIM - Journal of Immunological Methods. - : Elsevier BV. - 0022-1759 .- 1872-7905. ; 319:1-2, s. 53-63
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Journal article (peer-reviewed)abstract
- Affibody (R) molecules are a class of small and robust affinity proteins that can be generated to interact with a variety of antigens, thus having the potential to provide useful tools for biotechnological research and diagnostic applications. In this study, we have investigated Affibody-based reagents interacting specifically with the tyrosine kinase receptor HER2. A head-to-tail dimeric construct was site-specifically conjugated with different fluorescent and enzymatic groups resulting in reagents that were used for detection and quantification. The amount of cell surface expressed HER2 oil eleven (11) well characterized cell lines was quantified relative to each other by flow cytometry and shown to correlate well with results from parallel analyses of HER2 mRNA levels measured by real-time PCR. Further, immunofluorescence I microscopy studies of the cell lines and immunohistochemical analyses of cryosections of HER2 expressing SKOV-3 xenografts showed strong staining of the plasma membrane of tumor cells with little background staining. Full-length HER2 protein Could also be efficiently recovered from a cell extract by an immunoprecipitation procedure, using an Affibody ligand-based resin. These novel non-IgG derived reagents could be used to detect and quantify HER2 expression. By adapting the methods for use with Affibody molecules binding to other cell surface receptors, it is anticipated that also these receptors can be detected and quantified in a similar manner.
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