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Protein Engineering Market by Technologies, End Uses, Trends and Forecast to 2021, Upcoming Report by iHealthcareAnalyst, Inc. Protein Engineering Market by Technology (Rational Product Design, Directed Evolution), and End User (Academic Research Institutes, Biotechnology Companies, Contract Research Organizations, Pharmaceutical Enterprises) and Forecast 2017-2021. Maryland Heights, MO, May 17, 2017 --( Visit Protein Engineering Market by Technology (Rational Product Design, Directed Evolution), and End User (Academic Research Institutes, Biotechnology Companies, Contract Research Organizations, Pharmaceutical Enterprises) and Forecast 2017-2021 at https://www.ihealthcareanalyst.com/report/protein-engineering-market/ The global protein (antibody) engineering market segmentation is based on technology (rational product design, directed evolution), and end user (academic research institutes, biotechnology and pharmaceutical companies, contract research organizations). The global protein (antibody) engineering market report provides market size (Revenue USD Million 2014 to 2021), market share, trends and forecasts growth trends (CAGR%, 2017 to 2021). The global protein (antibody) engineering market research report is further segmented by geography into North America (U.S., Canada), Latin America (Brazil, Mexico, Rest of LA), Europe (U.K., Germany, France, Italy, Spain, Rest of EU), Asia Pacific (Japan, China, India, Rest of APAC), and Rest of the World. The global protein (antibody) market report also provides the detailed market landscape (market drivers, restraints, opportunities), market attractiveness analysis and also tracks the major competitors operating in the market by company overview, financial snapshot, key products, technologies and services offered, market share analysis and recent trends in the global market. Major players operating in the global protein (antibody) engineering market and included in this report are BioXcell, Covalab, Emerald Bio, Fusion Antibodies, GenTarget, Inc., IBL International, ImaginAb, Precision Antibody, and ProSci, Inc. 1. Technology 1.1. Rational Product Design 1.2. Directed Evolution 2. End User 2.1. Academic Research Institutes 2.2. Biotechnology and Pharmaceutical Companies 2.3. Contract Research Organizations 3. Company Profiles 3.1. BioXcell 3.2. Covalab 3.3. Emerald Bio 3.4. Fusion Antibodies 3.5. GenTarget, Inc. 3.6. IBL International 3.7. ImaginAb 3.8. Precision Antibody 3.9. ProSci, Inc. To request Table of Contents and Sample Pages of this report visit: https://www.ihealthcareanalyst.com/report/protein-engineering-market/ About Us iHealthcareAnalyst, Inc. is a global healthcare market research and consulting company providing market analysis, and competitive intelligence services to global clients. The company publishes syndicate, custom and consulting grade healthcare reports covering animal healthcare, biotechnology, clinical diagnostics, healthcare informatics, healthcare services, medical devices, medical equipment, and pharmaceuticals. In addition to multi-client studies, we offer creative consulting services and conduct proprietary single-client assignments targeted at client’s specific business objectives, information needs, time frame and budget. Please contact us to receive a proposal for a proprietary single-client study. Contact Us iHealthcareAnalyst, Inc. 2109, Mckelvey Hill Drive, Maryland Heights, MO 63043 United States Email: sales@ihealthcareanalyst.com Website: https://www.ihealthcareanalyst.com Maryland Heights, MO, May 17, 2017 --( PR.com )-- Protein engineering is the design of new enzymes or proteins with new or desirable functions. It is the conception and production of unnatural polypeptides, often through modification of amino acid sequences that are found in nature. Synthetic protein structures and functions can now be designed entirely on a computer or produced through directed evolution in the laboratory. In rational protein design, the scientist uses detailed knowledge of the structure and function of the protein to make desired changes. In general, this has the advantage of being inexpensive and technically easy, since site-directed mutagenesis techniques are well-developed. In directed evolution, random mutagenesis is applied to a protein, and a selection regime is used to pick out variants that have the desired qualities, where further rounds of mutation and selection are then applied. This method mimics natural evolution and, in general, may produce superior results to rational design.Visit Protein Engineering Market by Technology (Rational Product Design, Directed Evolution), and End User (Academic Research Institutes, Biotechnology Companies, Contract Research Organizations, Pharmaceutical Enterprises) and Forecast 2017-2021 at https://www.ihealthcareanalyst.com/report/protein-engineering-market/The global protein (antibody) engineering market segmentation is based on technology (rational product design, directed evolution), and end user (academic research institutes, biotechnology and pharmaceutical companies, contract research organizations).The global protein (antibody) engineering market report provides market size (Revenue USD Million 2014 to 2021), market share, trends and forecasts growth trends (CAGR%, 2017 to 2021). The global protein (antibody) engineering market research report is further segmented by geography into North America (U.S., Canada), Latin America (Brazil, Mexico, Rest of LA), Europe (U.K., Germany, France, Italy, Spain, Rest of EU), Asia Pacific (Japan, China, India, Rest of APAC), and Rest of the World. The global protein (antibody) market report also provides the detailed market landscape (market drivers, restraints, opportunities), market attractiveness analysis and also tracks the major competitors operating in the market by company overview, financial snapshot, key products, technologies and services offered, market share analysis and recent trends in the global market.Major players operating in the global protein (antibody) engineering market and included in this report are BioXcell, Covalab, Emerald Bio, Fusion Antibodies, GenTarget, Inc., IBL International, ImaginAb, Precision Antibody, and ProSci, Inc.1. Technology1.1. Rational Product Design1.2. Directed Evolution2. End User2.1. Academic Research Institutes2.2. Biotechnology and Pharmaceutical Companies2.3. Contract Research Organizations3. Company Profiles3.1. BioXcell3.2. Covalab3.3. Emerald Bio3.4. Fusion Antibodies3.5. GenTarget, Inc.3.6. IBL International3.7. ImaginAb3.8. Precision Antibody3.9. ProSci, Inc.To request Table of Contents and Sample Pages of this report visit:https://www.ihealthcareanalyst.com/report/protein-engineering-market/About UsiHealthcareAnalyst, Inc. is a global healthcare market research and consulting company providing market analysis, and competitive intelligence services to global clients. The company publishes syndicate, custom and consulting grade healthcare reports covering animal healthcare, biotechnology, clinical diagnostics, healthcare informatics, healthcare services, medical devices, medical equipment, and pharmaceuticals.In addition to multi-client studies, we offer creative consulting services and conduct proprietary single-client assignments targeted at client’s specific business objectives, information needs, time frame and budget. Please contact us to receive a proposal for a proprietary single-client study.Contact UsiHealthcareAnalyst, Inc.2109, Mckelvey Hill Drive,Maryland Heights, MO 63043United StatesEmail: sales@ihealthcareanalyst.comWebsite: https://www.ihealthcareanalyst.com


Ward C.,Fusion Antibodies | Kuehn D.,Fusion Antibodies | Burden R.E.,Fusion Antibodies | Burden R.E.,Queen's University of Belfast | And 9 more authors.
PLoS ONE | Year: 2010

Background: Angiogenesis is a key hallmark of tumourigenesis and its inhibition is a proven strategy for the development of novel anti-cancer therapeutics. An important aspect of early angiogenesis is the co-ordinated migration and invasion of endothelial cells through the hypoxic tumour tissue. Cathepsin S has been shown to play an important role in angiogenesis as has vascular endothelial growth factor (VEGF). We sought to assess the anti-angiogenic effect of Fsn0503, a novel cathepsin S inhibitory antibody, when combined with anti-VEGF on vascular development. Methodology/Principal Findings: Cathepsin S expression and secretion from endothelial cells was characterised using RTPCR and western blotting. We further show that cathepsin S promotes pericellular hydrolysis of extracellular matrix components in the tumour microenvironment and facilitates endothelial invasion. The cathepsin S inhibitory antibody, Fsn0503, blocks extracellular proteolysis, inhibiting endothelial invasion and tube formation in cell-based assays. The antiangiogenic effects of Fsn0503 were also shown in vivo where it significantly retarded the development of vasculature in human xenograft models. Furthermore, when Fsn0503 was combined with an anti-VEGF antibody, a synergistic inhibition of microvascular development was observed. Conclusions/Significance: Taken together, this data demonstrates that the antibody-mediated targeting of cathepsin S represents a novel method of inhibiting angiogenesis. Furthermore, when used in combination with anti-VEGF therapies, Fsn0503 has the potential to significantly enhance current treatments of tumour neovascularisation and may also be of use in the treatment of other conditions associated with inappropriate angiogenesis. © 2010 Ward et al.


Gormley J.A.,Fusion Antibodies | Hegarty S.M.,Queen's University of Belfast | O'Grady A.,Royal College of Surgeons in Ireland | Stevenson M.R.,Queen's University of Belfast | And 10 more authors.
British Journal of Cancer | Year: 2011

Background: The aim of this pilot retrospective study was to investigate the immunohistochemical expression of Cathepsin S (CatS) in three cohorts of colorectal cancer (CRC) patients (n=560). Methods: Prevalence and association with histopathological variables were assessed across all cohorts. Association with clinical outcomes was investigated in the Northern Ireland Adjuvant Chemotherapy Trial cohort (n=211), where stage II/III CRC patients were randomised between surgery-alone or surgery with adjuvant fluorouracil/folinic acid (FU/FA) treatment. Results: Greater than 95% of tumours had detectable CatS expression with significantly increased staining in tumours compared with matched normal colon (P=0.001). Increasing CatS was associated with reduced recurrence-free survival (RFS; P=0.03) among patients treated with surgery alone. Adjuvant FU/FA significantly improved RFS (hazard ratio (HR), 0.33; 95% CI, 0.12-0.89) and overall survival (OS; HR, 0.25; 95% CI, 0.08-0.81) among 36 patients with high CatS. Treatment did not benefit the 66 patients with low CatS, with a RFS HR of 1.34 (95% CI, 0.60-3.19) and OS HR of 1.33 (95% CI, 0.56-3.15). Interaction between CatS and treatment status was significant for RFS (P=0.02) and OS (P=0.04) in a multivariate model adjusted for known prognostic markers. Conclusion: These results signify that CatS may be an important prognostic biomarker and predictive of response to adjuvant FU/FA in CRC. © 2011 Cancer Research UK All rights reserved.


Caswell J.,Fusion Antibodies | Caswell J.,Queen's University of Belfast | Snoddy P.,Fusion Antibodies | McMeel D.,Fusion Antibodies | And 2 more authors.
Protein Expression and Purification | Year: 2010

The use of Escherichia coli protein expression systems has many benefits, including the ease of propagation, amounts of protein that can be generated and cost. However, this host has some drawbacks due to difficulties in the production of soluble foreign proteins with their alternate codon usage bias, reductive cytoplasmic environment and lack of complex post-translational modifications. We have designed a novel fusion protein tag derived from the sequence of sortase (SrtA) which we have named Solubility 'eNhancing' Ubiquitous Tag (SNUT). Here we demonstrate its application and effectiveness as an N-terminal fusion tag for the expression and purification of proteins that could not be effectively produced with other tags. We show this tag can be utilized for the purification of proteins through both native and refolding immobilized metal ion chromatography and in combination with an anti-SNUT monoclonal antibody, can also be used as a detection tag. This tag may prove useful in circumventing expression and purification issues with the production of proteins in bacterial expression hosts. © 2009 Elsevier Inc. All rights reserved.


Burden R.E.,Fusion Antibodies | Burden R.E.,Queen's University of Belfast | Gormley J.A.,Fusion Antibodies | Kuehn D.,Fusion Antibodies | And 9 more authors.
Biochimie | Year: 2012

Cathepsin S is a lysosomal cysteine protease implicated in tumourigenesis with key roles in invasion and angiogenesis. We have previously shown that the specific inhibition of Cathepsin S using a monoclonal antibody (Fsn0503) blocks colorectal carcinoma tumour growth and angiogenesis in vivo. We investigated whether Cathepsin S expression levels were affected by chemotherapy in human cancer cell lines by RT-PCR. Using colorectal xenograft models, we examined the therapeutic benefit of Cathepsin S inhibition using Fsn0503 in combination with a metronomic dosing regimen of CPT-11. We analysed the effects of the combination therapy on tumour progression and on tumour vascularisation by immunohistochemical staining of tumours. Cathepsin S expression levels are upregulated in HCT116, LoVo, Colo205 cell lines and HUVECs after exposure to CPT-11 in vitro. The administration of Fsn0503 in combination with CPT-11 significantly attenuated tumour growth in comparison to CPT-11 alone in colorectal HCT116 xenograft models. Furthermore, analysis of tumour vascularisation revealed that this was also significantly disrupted by the combination treatment. These results show that the combination of Cathepsin S inhibition with CPT-11 enhances the therapeutic effect of the chemotherapy. This rationale may have clinical application in the treatment of colorectal cancer upon further evaluation. © 2011 Elsevier Masson SAS. All rights reserved.


Abdelghany S.M.,Queen's University of Belfast | Schmid D.,Queen's University of Belfast | Deacon J.,Queen's University of Belfast | Jaworski J.,Queen's University of Belfast | And 7 more authors.
Biomacromolecules | Year: 2013

meso-Tetra(N-methyl-4-pyridyl) porphine tetra tosylate (TMP) is a photosensitizer that can be used in photodynamic therapy (PDT) to induce cell death through generation of reactive oxygen species in targeted tumor cells. However, TMP is highly hydrophilic, and therefore, its ability to accumulate intracellularly is limited. In this study, a strategy to improve TMP uptake into cells has been investigated by encapsulating the compound in a hydrogel-based chitosan/alginate nanoparticle formulation. Nanoparticles of 560 nm in diameter entrapping 9.1 μg of TMP per mg of formulation were produced and examined in cell-based assays. These particles were endocytosed into human colorectal carcinoma HCT116 cells and elicited a more potent photocytotoxic effect than free drug. Antibodies targeting death receptor 5 (DR5), a cell surface apoptosis-inducing receptor up-regulated in various types of cancer and found on HCT116 cells, were then conjugated onto the particles. The conjugated antibodies further enhanced uptake and cytotoxic potency of the nanoparticle. Taken together, these results show that antibody-conjugated chitosan/alginate nanoparticles significantly enhanced the therapeutic effectiveness of entrapped TMP. This novel approach provides a strategy for providing targeted site-specific delivery of TMP and other photosensitizer drugs to treat colorectal tumors using PDT. © 2013 American Chemical Society.


Whelan C.,Enfer Scientific | Whelan A.O.,Veterinary Laboratories Agency VLA Weybridge | Shuralev E.,Enfer Scientific | Kwok H.F.,Fusion Antibodies | And 3 more authors.
Clinical and Vaccine Immunology | Year: 2010

Rapid, simple, and accurate antemortem tests for tuberculosis (TB) in cattle need to be developed in order to augment the existing screening methods. In particular, as cattle vaccines are developed, such tests would allow the continuation of test-and-slaughter policies alongside vaccination. Therefore, the development of an assay that distinguishes infected from vaccinated animals (a DIVA test) is an urgent research requirement. In this study, we assessed the performance of a novel multiplex serological test with sera collected from 96 skin-tested animals with bovine tuberculosis, 93 TB-free animals, and 39 cattle vaccinated with Mycobacterium bovis BCG. Our results indicate that the test has a relative sensitivity range of 77.0% to 86.5% at corresponding specificity levels of 100.0% to 77.6%. Comparison with the Bovigam gamma interferon antemortem test revealed that this serology test was significantly more sensitive at specificities above 97.9%, while the Bovigam test was, on average, about 10% more sensitive when the test specificity was set below 97%. Importantly, this serological multiplex assay does not react with sera from BCG-vaccinated calves and is therefore suitable as a DIVA test alongside BCG-based vaccine strategies. Copyright © 2010, American Society for Microbiology. All Rights Reserved.


Patent
Fusion Antibodies | Date: 2011-05-04

Described are specific binding members e.g. antibodies which may be used in the treatment of diseases associated with cathepsin S activity. The specific binding members bind cathepsin S and inhibit its proteolytic activity. The binding members may be used in the treatment of diseases such as cancer, inflammatory diseases, neurodegenerative disorders, autoimmune disorders, and other diseases associated with excessive, deregulated or inappropriate angiogenesis.


Patent
Fusion Antibodies | Date: 2011-03-18

Described are specific binding members e.g. antibodies which may be used in the treatment of diseases associated with cathepsin S activity. The specific binding members bind cathepsin S and inhibit its proteolytic activity. The binding members may be used in the treatment of diseases such as cancer, inflammatory diseases, neurodegenerative disorders, autoimmune disorders, and other diseases associated with excessive, deregulated or inappropriate angiogenesis


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