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Journal articles on the topic 'Recombinant protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Niazi, Sarfaraz K., and Matthias Magoola. "mRNA and Synthesis-Based Therapeutic Proteins: A Non-Recombinant Affordable Option." Biologics 3, no. 4 (2023): 355–79. http://dx.doi.org/10.3390/biologics3040020.

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Recombinant technology has been around for nearly three quarters of a century and has revolutionized protein therapy. However, the cost of developing recombinant therapeutic proteins and the manufacturing infrastructure keeps their cost unaffordable for most patients. Proteins are produced in the body via messenger RNA (mRNA) translation. This process can be readily replicated through administering a chemical nucleic acid product to manufacture the same protein recombinantly. The progress made in creating these proteins ex vivo in a cell-free system also offers a lower-cost option to produce t

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2

Rodrigues, M., S. Li, K. Murata, et al. "Influenza and vaccinia viruses expressing malaria CD8+ T and B cell epitopes. Comparison of their immunogenicity and capacity to induce protective immunity." Journal of Immunology 153, no. 10 (1994): 4636–48. http://dx.doi.org/10.4049/jimmunol.153.10.4636.

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Abstract We compared the effectiveness of several recombinant influenza and vaccinia viruses to induce a malaria-specific immune response. The CD8+ T cell epitope of the circumsporozoite (CS) protein of Plasmodium yoelii, a rodent malaria parasite, was expressed in two distinct influenza virus proteins, the hemagglutinin and the neuraminidase. These recombinant viruses were found to be equally efficient at inducing CS-specific CD8+ T cells in mice. A third recombinant virus, which expresses a B cell epitope of the CS protein, induced neutralizing anti-sporozoite Abs. Expression in the same rec

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3

Astuti, R. W., N. Wijayanti, and A. Haryanto. "Expression of Recombinant Fusion Protein from Local Isolate of Newcastle Disease Virus and Antibody Response to Recombinant Fusion Protein in Broiler Chickens Post-Vaccination." Journal of the Indonesian Tropical Animal Agriculture 45, no. 2 (2020): 78–90. http://dx.doi.org/10.14710/jitaa.45.2.78-90.

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This research aimed to express and purify the recombinant Fusion (F) protein of Newcastle Disease Virus (NDV) from a local isolate in Galur, Kulon Progo, Indonesia (0663/04/2013) from recombinant vector plasmid pBT7-N-His F, and to study the antibody response in the broiler sera which were injected with pure recombinant F protein compared with treated broilers that were vaccinated with commercial inactive NDV vaccines and control broilers without vaccination. The results showed that the recombinant F protein of NDV was successfully expressed, purified and visualized by SDS-PAGE with Coomassie

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4

Jawad, J., R. W. Astuti, A. Haryanto, and N. Wijayanti. "Antibody response to Newcastle disease virus recombinant fusion protein in post-vaccinated laying hens." Journal of the Indonesian Tropical Animal Agriculture 48, no. 1 (2022): 20–27. http://dx.doi.org/10.14710/jitaa.48.1.20-27.

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This research was aimed to analyze antibody response in laying hens post vaccinated by Newcastle Disease Virus (NDV) recombinat Fusion (F) protein which has been succesfully expressed from the F gene of local isolates of NDV from Kulon Progo strain (0663/04/2013), Yogyakarta, Indonesia. The F gene cloned into expression vector plasmid pBT7-N-His. Two types of NDV recombinant vaccine, a concentrated and pure F recombinant protein were used for vaccination. A concentrated recombinant F protein was collected from the centrifugal ultrafiltration process and a pure recombinant F protein was collect

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Ferrari, Luca, and Stefan G. D. Rüdiger. "Recombinant production and purification of the human protein Tau." Protein Engineering, Design and Selection 31, no. 12 (2018): 447–55. http://dx.doi.org/10.1093/protein/gzz010.

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Abstract Tau protein is a microtubule-stabilising protein whose aggregation is linked to Alzheimer’s Disease and other forms of dementia. Tau biology is at the heart of cytoskeletal dynamics and neurodegenerative mechanisms, making it a crucial protein to study. Tau purification, however, is challenging as Tau is disordered, which makes it difficult to produce in recombinant system and is degradation-prone. It is thus challenging to obtain pure and stable preparations of Tau. Here, we present a fast and robust protocol to purify Tau recombinantly in Escherichia coli. Our protocol allows purify

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Lewis, Peter. "Recombinant protein drugs." British Journal of Clinical Pharmacology 53, no. 4 (2002): 411. http://dx.doi.org/10.1046/j.1365-2125.2002.01571.x.

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Yu, Xue-Jie, Patricia A. Crocquet-Valdes, Louis C. Cullman, Vsevolod L. Popov, and David H. Walker. "Comparison of Ehrlichia chaffeensisRecombinant Proteins for Serologic Diagnosis of Human Monocytotropic Ehrlichiosis." Journal of Clinical Microbiology 37, no. 8 (1999): 2568–75. http://dx.doi.org/10.1128/jcm.37.8.2568-2575.1999.

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Diagnosis of human monocytotropic ehrlichiosis (HME) generally depends on serology that detects the antibody response to immunodominant proteins of Ehrlichia chaffeensis. Protein immunoblotting was used to evaluate the reaction of the antibodies in patients’ sera with the recombinant E. chaffeensis 120- and 28-kDa proteins as well as the 106- and the 37-kDa proteins. The cloning of the genes encoding the latter two proteins is described in this report. Immunoelectron microscopy demonstrated that the 106-kDa protein is located at the surfaces of ehrlichiae and on the intramorular fibrillar stru

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8

Koval, Olga, Galina Kochneva, Anastasiya Tkachenko, et al. "Recombinant Vaccinia Viruses Coding Transgenes of Apoptosis-Inducing Proteins Enhance Apoptosis But Not Immunogenicity of Infected Tumor Cells." BioMed Research International 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/3620510.

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Genetic modifications of the oncolytic vaccinia virus (VV) improve selective tumor cell infection and death, as well as activation of antitumor immunity. We have engineered a double recombinant VV, coding human GM-CSF, and apoptosis-inducing protein apoptin (VV-GMCSF-Apo) for comparing with the earlier constructed double recombinant VV-GMCSF-Lact, coding another apoptosis-inducing protein, lactaptin, which activated different cell death pathways than apoptin. We showed that both these recombinant VVs more considerably activated a set of critical apoptosis markers in infected cells than the rec

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Volkova, N. V., A. V. Ivanova, A. A. Isaeva, et al. "Obtaining Recombinant Antigens for the Development of Serological Diagnosis of Marburg Fever." Problems of Particularly Dangerous Infections, no. 4 (February 7, 2021): 47–52. http://dx.doi.org/10.21055/0370-1069-2020-4-47-52.

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Aim. Production of recombinant viral antigens of the main immunodominant proteins: glycoprotein (GPΔMLD), nucleoprotein (NP) and matrix protein (VP40) of the Marburg virus, as well as the study of their antigenic and immunogenic properties.Materials and methods. To create recombinant proteins GPΔMLD, NP and VP40 of the Marburg virus, synthesized nucleotide sequences encoding these proteins cloned into the pET21a expression vector were used. The immunogenic and antigenic properties of the obtained recombinant proteins were tested using a number of biomodels (mice, chickens, and guinea pigs).Res

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Huang, Li-Fen, Desyanti Saulina Sinaga, Chia-Chun Tan, Shu-Ju Micky Hsieh, and Chi-Hung Huang. "Expression of Recombinant Human Octamer-Binding Transcription Factor 4 in Rice Suspension Cells." International Journal of Molecular Sciences 22, no. 3 (2021): 1409. http://dx.doi.org/10.3390/ijms22031409.

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The rice cell suspension culture system is a good way to produce recombinant human proteins, owing to its high biosafety and low production cost. Human Octamer-binding Transcription Factor 4 (Oct4) is a fundamental transcription factor responsible for maintaining human pluripotent embryonic stem cells. Recombinant Oct4 protein has been used to induce pluripotent stem cells. In this study, recombinant Oct4 proteins are produced via a sugar starvation-inducible αAmy3/RAmy3D promoter–signal peptide-based rice recombinant protein expression system. Oct4 mRNAs accumulate in the transgenic rice susp

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11

Kim, Yoo-Gon, Woo-Jong Lee, Chan-Hee Won, et al. "A study on short-term stability of recombinant protein A." Analytical Science and Technology 24, no. 3 (2011): 193–99. http://dx.doi.org/10.5806/ast.2011.24.3.193.

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12

Mihailova, N. A., E. M. Zimina, A. V. Soldatenkova, and A. A. Kaloshin. "DEVELOPMENT OF THE VACCINE BASED ON THE RECOMBINANT ANTIGENS OF PSEUDOMONAS AERUGINOSA." Journal of microbiology epidemiology immunobiology 1, no. 1 (2019): 74–80. http://dx.doi.org/10.36233/0372-9311-2019-1-74-80.

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Aim. The aim is obtaining, investigation and selection of recombinant antigens for inclusion theirs into the against Pseudomonas vaccine. Materials and methods. The genes encoding of the outer membrane proteins F, L and I and Exotoxin A were synthesized by PCR with the genomic DNA of Pseudomonas aeruginosa. The amplified sequences were cloned into plasmid vectors for expression in cells of Escherichia coli. As the result of expression were the synthesized recombinant proteins that were purified in columns with a nickel-activated sorbent. The authenticity of the recombinant antigens was assesse

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13

Kühn, S., C. Skerka, and P. F. Zipfel. "Mapping of the complement regulatory domains in the human factor H-like protein 1 and in factor H1." Journal of Immunology 155, no. 12 (1995): 5663–70. http://dx.doi.org/10.4049/jimmunol.155.12.5663.

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Abstract The human factor H-like protein 1 (FHL-1) is composed of seven repetitive domains (short consensus repeats; SCRs) that are identical in sequence to the seven NH2-terminal SCRs of the complement regulatory protein factor H. We have identified the native FHL-1 protein as a 42-kDa human plasma protein by immunoblotting and by comparing the mobility to that of a recombinant FHL-1 protein. Here, we demonstrate the existence of two distinct co-migrating human plasma proteins that represent the 42-kDa FHL-1 protein and the previously identified 43-kDa factor H-related 1 beta protein. Similar

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14

Oulton, Tate, Joshua Obiero, Isabel Rodriguez, et al. "Plasmodium falciparum serology: A comparison of two protein production methods for analysis of antibody responses by protein microarray." PLOS ONE 17, no. 8 (2022): e0273106. http://dx.doi.org/10.1371/journal.pone.0273106.

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The evaluation of protein antigens as putative serologic biomarkers of infection has increasingly shifted to high-throughput, multiplex approaches such as the protein microarray. In vitro transcription/translation (IVTT) systems–a similarly high-throughput protein expression method–are already widely utilised in the production of protein microarrays, though purified recombinant proteins derived from more traditional whole cell based expression systems also play an important role in biomarker characterisation. Here we have performed a side-by-side comparison of antigen-matched protein targets f

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15

Mei, Liu, Lu Lin-Jing, Huang Jun-Yan, Zhang Shu-Huan, Bi Ding-Ren, and Sun Ming. "Display of H5N1Avian influenza virushaemagglutinin HA1 onBacillus thuringiensiscell surface and its immunogenicity for mice." Chinese Journal of Agricultural Biotechnology 4, no. 3 (2007): 221–28. http://dx.doi.org/10.1017/s1479236207001702.

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AbstractThe S-layer protein CTC surface display system ofBacillus thuringiensiswas used to test the possibility of displaying H5N1Avian influenza virus(AIV) haemagglutinin HA1 on the cell surface ofB. thuringiensis. Two recombinant plasmids, pCTC-HA1P and pCSHA1P, were constructed by replacing the central part below the surface anchor sequenceslhof S-layer protein genectcwith partha1gene(ha1p). pCTC-HA1P harboured the fusion genectc-ha1pand pCSHA1P the fusion genecsa-ctc-ha1p,csarepresenting thecsaABoperon (very important in anchoring S-layer protein on the bacterial cell surface). Two recombi

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Schönherr, Robert, Janine Mia Rudolph, and Lars Redecke. "Protein crystallization in living cells." Biological Chemistry 399, no. 7 (2018): 751–72. http://dx.doi.org/10.1515/hsz-2018-0158.

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AbstractProtein crystallization in living cells has been observed surprisingly often as a native assembly process during the past decades, and emerging evidence indicates that this phenomenon is also accessible for recombinant proteins. But only recently the advent of high-brilliance synchrotron sources, X-ray free-electron lasers, and improved serial data collection strategies has allowed the use of these micrometer-sized crystals for structural biology. Thus,in cellulocrystallization could offer exciting new possibilities for proteins that do not crystallize applying conventional approaches.

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17

Urbanowicz, Anna, Dominik Lewandowski, and Marek Figlerowicz. "Oral Lyme disease vaccine." BioTechnologia 95, no. 4 (2015): 255–58. https://doi.org/10.5114/bta.2014.56595.

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The present invention relates to a Lyme disease vaccine, a genetic construct, recombinant protein, method for genetic construct design, method for vaccine delivery, method for recombinant proteins delivery, use of recombinant proteins in the production of Lyme disease vaccine. In particular, the method concerns the use of TROSPA and TROSPA- Salpl 5 recombinant proteins derived from castor bean tick (<i>Ixodes riccinus</i> ) as a component of Lyme disease vaccine for animals. The antibodies present in blood of an immunized vertebrate directed against the TROSPA proteins considerably

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18

Glass, Pamela J., Laura J. White, Judith M. Ball, Isabelle Leparc-Goffart, Michele E. Hardy, and Mary K. Estes. "Norwalk Virus Open Reading Frame 3 Encodes a Minor Structural Protein." Journal of Virology 74, no. 14 (2000): 6581–91. http://dx.doi.org/10.1128/jvi.74.14.6581-6591.2000.

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ABSTRACT Norwalk virus (NV) is a causative agent of acute epidemic nonbacterial gastroenteritis in humans. The inability to cultivate NV has required the use of molecular techniques to examine the genome organization and functions of the viral proteins. The function of the NV protein encoded by open reading frame 3 (ORF 3) has been unknown. In this paper, we report the characterization of the NV ORF 3 protein expressed in a cell-free translation system and in insect cells and show its association with recombinant virus-like particles (VLPs) and NV virions. Expression of the ORF 3 coding region

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Alatortseva, G. I., A. V. Sidorov, L. N. Nesterenko, et al. "DESIGN OF HEPATITIS E VIRUS GENOTYPE 1 RECOMBINANT CAPSID PROTEIN: CLONING, EXPRESSION, PURIFICATION, EVALUATION OF THE ANTIGENIC PROPERTIES." Journal of microbiology epidemiology immunobiology, no. 6 (December 28, 2017): 72–80. http://dx.doi.org/10.36233/0372-9311-2017-6-72-80.

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Aim. The development of the hepatitis E virus (HEV) genotype 1 recombinant capsid protein. Materials and methods. Escherichia coli strains, plasmid vectors, serological and clinical samples, ELISA reagent kits, molecular biological, bioinformatic, biotechnological, biochemical and serological methods. Results. Using HEV genotype 1 DNA copy of subgenomic virus RNA we made E.coli strains producing recombinabt capsid protein, containing C-terminal fragment of ORF2 protein fused to E.coli beta-galactosidase. Recombinant protein ORF2 had been isolated from the inclusion bodies of the E.coli biomass

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Abed, Y., G. St-Laurent, H. Zhang, R. M. Jacobs, and D. Archambault. "Development of a Western Blot Assay for Detection of Bovine Immunodeficiency-Like Virus Using Capsid and Transmembrane Envelope Proteins Expressed from Recombinant Baculovirus." Clinical Diagnostic Laboratory Immunology 6, no. 2 (1999): 168–72. http://dx.doi.org/10.1128/cdli.6.2.168-172.1999.

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ABSTRACT A 120-amino-acid polypeptide selected from the transmembrane protein region (tTM) and the major capsid protein p26 of bovine immunodeficiency-like virus (BIV) were expressed as fusion proteins from recombinant baculoviruses. The antigenic reactivity of both recombinant fusion proteins was confirmed by Western blot with bovine and rabbit antisera to BIV. BIV-negative bovine sera and animal sera positive for bovine syncytial virus and bovine leukemia virus failed to recognize the recombinant fusion proteins, thereby showing the specificity of the BIV Western blot. One hundred and five b

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Fischer, Rainer, Neil Emans, Flora Schuster, Stephan Hellwig, and Jürgen Drossard. "Towards molecular farming in the future: using plant‐cell‐suspension cultures as bioreactors." Biotechnology and Applied Biochemistry 30, no. 2 (1999): 109–12. http://dx.doi.org/10.1111/j.1470-8744.1999.tb00899.x.

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Plant‐suspension cells are an in vitro system that can be used for recombinant protein production under carefully controlled certified conditions. Plant‐suspension cells can be grown in shake flasks or fermenters to produce secondary metabolites, like vincristine and vinblastine, and to produce recombinant proteins after transformation. This review article focuses on discussing the generation of transformed suspension‐cell lines expressing recombinant proteins, like antibodies, and recombinant‐protein downstream processing and purification.

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Svraka, Lejla, Hakim Ben Abdallah, and Claus Johansen. "When recombinant proteins go wrong: The hidden pitfall of recombinant protein contamination." Cytokine 186 (February 2025): 156830. https://doi.org/10.1016/j.cyto.2024.156830.

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Fisher, Adam C., Charles H. Haitjema, Cassandra Guarino, et al. "Production of Secretory and Extracellular N-Linked Glycoproteins inEscherichia coli." Applied and Environmental Microbiology 77, no. 3 (2010): 871–81. http://dx.doi.org/10.1128/aem.01901-10.

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ABSTRACTTheCampylobacter jejuni pglgene cluster encodes a complete N-linked protein glycosylation pathway that can be functionally transferred intoEscherichia coli. In this system, we analyzed the interplay between N-linked glycosylation, membrane translocation and folding of acceptor proteins in bacteria. We developed a recombinant N-glycan acceptor peptide tag that permits N-linked glycosylation of diverse recombinant proteins expressed in the periplasm of glycosylation-competentE. colicells. With this “glycosylation tag,” a clear difference was observed in the glycosylation patterns found o

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Goo, Tae Won, Eun Young Yun, Sung Wan Kim, et al. "Secretion of the Antibacterial Recombinant Protein Enbocin." Zeitschrift für Naturforschung C 63, no. 3-4 (2008): 284–88. http://dx.doi.org/10.1515/znc-2008-3-420.

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The insect baculovirus expression vector system (BEVS) is useful for the production of biologically active recombinant proteins. However, the overexpression of foreign proteins in this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we have developed a versatile baculovirus expression and secretion system using the Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion improved the secretion and antibacterial activity of recombinant enbocin proteins. Thus, bPDI gene fusion is a useful addition to the

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Llompart, Blanca, Immaculada Llop-Tous, Pablo Marzabal, et al. "Protein production from recombinant protein bodies." Process Biochemistry 45, no. 11 (2010): 1816–20. http://dx.doi.org/10.1016/j.procbio.2010.01.016.

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Duffy, Michael F., Kevin G. Whithear, Amir H. Noormohammadi, et al. "Indirect Enzyme-Linked Immunosorbent Assay for Detection of Immunoglobulin G Reactive with a Recombinant Protein Expressed from the Gene Encoding the 116-Kilodalton Protein ofMycoplasma pneumoniae." Journal of Clinical Microbiology 37, no. 4 (1999): 1024–29. http://dx.doi.org/10.1128/jcm.37.4.1024-1029.1999.

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Serology remains the method of choice for laboratory diagnosis ofMycoplasma pneumoniae infection. Currently available serological tests employ complex cellular fractions of M. pneumoniae as antigen. To improve the specificity of M. pneumoniae diagnosis, a recombinant protein was assessed as a serodiagnostic reagent. A panel of recombinant proteins were expressed from a cloned M. pneumoniae gene that encodes a 116-kDa surface protein antigen. The recombinant proteins were assessed for reactivity with patient sera and the most antigenic was further assessed for its serodiagnostic potential by in

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Sankar, S. Gowri, K. J. Dhanajeyan, R. Paramasivan, V. Thenmozhi, B. K. Tyagi, and S. John Vennison. "High-Level Expression of Functionally Active Dengue-2 Non-Structural Antigen 1 Production inEscherichia coli." BioMed Research International 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/343195.

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Detection of nonstructural protein (NS1) is an important diagnostic marker during acute phase of dengue infection. Not only for diagnostic purpose, the protein had important role in vaccine design as well, as a candidate for studying virus assembly and maturation. Various researchers employed different expression systems and strategies for recombinant NS1 protein production. Attempts to express NS1 protein in prokaryotic and yeast expression system result in formation of insoluble protein which needs to undergo refolding to attain native structural and functional forms. Here, we report the pro

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Kaloshin, A. A., A. V. Soldatenkova, E. M. Zimina та N. A. Mikhailova. "OBTAINING FUSED RECOMBINANT PROTEINS OprF-ΔOprI, ΔOprF-ΔOprI AND OprF-aTox-ΔOprl OF PSEUDOMONAS AERUGINOSA". Journal of microbiology epidemiology immunobiology, № 5 (28 жовтня 2017): 32–38. http://dx.doi.org/10.36233/0372-9311-2017-5-32-38.

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Aim. Obtaining fused recombinant proteins of Pseudomonas aeruginosa that have protective properties against experimental pseudomonas infection. Materials and methods. Fused sequences of P. aeruginosa genes oprF, oprl and deleted form of toxA were cloned in plasmids for the expression in Escherichia coli. The synthesized recombinant proteins were purified in Ni-sepharose columns. Recombinant proteins were administered to mice intraperitonealiy twice with a 2 week interval to evaluate protective properties. Virulent culture of P. aeruginosa strain PA103 was injected into the animals intraperiton

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Ju, Xiaoli, Meijia Ren, Keping Chen, and Qiang Wang. "Overexpression of c-Myc enhances recombinant protein production in High Five cells after baculovirus infection." Zeitschrift für Naturforschung C 73, no. 3-4 (2018): 147–51. http://dx.doi.org/10.1515/znc-2017-0076.

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AbstractDue to their numerous advantages, baculovirus expression vector systems (BEVS) have been widely used to express recombinant proteins for different purposes. Different strategies have been adopted to increase recombinant protein production. In this study, we transiently or stably expressed mousec-Mycin High Five cells using a commercial pIB/V5 vector. Under the control of theOpIE2promoter, this vector could enhance recombinant protein production. We found that transient expression ofc-Mycin High Five cells improved recombinant protein production. Furthermore, we established two stable c

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Li, Tian-Cheng, Naokazu Takeda, Tatsuo Miyamura, et al. "Essential Elements of the Capsid Protein for Self-Assembly into Empty Virus-Like Particles of Hepatitis E Virus." Journal of Virology 79, no. 20 (2005): 12999–3006. http://dx.doi.org/10.1128/jvi.79.20.12999-13006.2005.

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ABSTRACT Hepatitis E virus (HEV) is a noncultivable virus that causes acute liver failure in humans. The virus's major capsid protein is encoded by an open reading frame 2 (ORF2) gene. When the recombinant protein consisting of amino acid (aa) residues 112 to 660 of ORF2 is expressed with a recombinant baculovirus, the protein self-assembles into virus-like particles (VLPs) (T.-C. Li, Y. Yamakawa, K. Suzuki, M. Tatsumi, M. A. Razak, T. Uchida, N. Takeda, and T. Miyamura, J. Virol. 71:7207-7213, 1997). VLPs can be found in the culture medium of infected Tn5 cells but not in that of Sf9 cells, a

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Zagursky, Robert J., Peggy Ooi, Kevin F. Jones, Michael J. Fiske, Robert P. Smith, and Bruce A. Green. "Identification of a Haemophilus influenzae5′-Nucleotidase Protein: Cloning of the nucA Gene and Immunogenicity and Characterization of the NucA Protein." Infection and Immunity 68, no. 5 (2000): 2525–34. http://dx.doi.org/10.1128/iai.68.5.2525-2534.2000.

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ABSTRACT We report on the identification of a surface-exposed, highly conserved, immunogenic nontypeable Haemophilus influenzae(NTHi) protein, which elicits cross-reactive bactericidal antibodies against NTHi. The protein was extracted from NTHi strain P860295 with KSCN and purified; it migrated as a single band on a sodium dodecyl sulfate-polyacrylamide gel with an apparent molecular mass of 63 kDa. Mouse antiserum generated against the purified protein was reactive on whole-cell enzyme-linked immunosorbent assay (ELISA) with seven NTHi strains and type b Eagan and Whittier strains and exhibi

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Sitasiwi, Agung Janika, Wayan Tunas Artama, Agung Budiyanto, and Edy Dharmana. "MOLECULAR EXPRESSION OF WINGLESS-TYPE MMTV INTEGRATION SITE FAMILY MEMBER 4 GENE USING Escherichia coli BL21." Jurnal Kedokteran Hewan - Indonesian Journal of Veterinary Sciences 11, no. 1 (2017): 11–14. http://dx.doi.org/10.21157/j.ked.hewan.v11i1.5891.

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This research was conducted to find out the Wnt4 recombinant proteins which expressed by Escherichia coli (E. coli) BL21 carrying the recombinant DNA wnt4 (E. coli transformation). Research materials were E. coli BL21 transformation and E. coli BL21 non-transformation (negative control). The expression of recombinant protein was conducted by culturing E. coli for 24 hours in Luria-Bertani (LB) media with isopropyl β-D-1-thiogalactopyranoside (IPTG) induction. Recombinant protein was isolated by sonication of pellet bacteria. Protein analysis performed by 15% sodium dodecyl sulphate polyacrylam

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Feng, Ziru, Xifeng Li, Baofang Fan, Cheng Zhu, and Zhixiang Chen. "Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability." International Journal of Molecular Sciences 23, no. 21 (2022): 13516. http://dx.doi.org/10.3390/ijms232113516.

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The production of therapeutic and industrial recombinant proteins in plants has advantages over established bacterial and mammalian systems in terms of cost, scalability, growth conditions, and product safety. In order to compete with these conventional expression systems, however, plant expression platforms must have additional economic advantages by demonstrating a high protein production yield with consistent quality. Over the past decades, important progress has been made in developing strategies to increase the yield of recombinant proteins in plants by enhancing their expression and redu

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Lobb, Leslie, Boguslaw Stec, Evan K. Kantrowitz, et al. "Expression, purification and characterization of recombinant crambin." "Protein Engineering, Design and Selection" 9, no. 12 (1996): 1233–39. http://dx.doi.org/10.1093/protein/9.12.1233.

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Jamrichová, Daniela, Lenka Tišáková, Veronika Jarábková, and Andrej Godány. "How to approach heterogeneous protein expression for biotechnological use: An overview." Nova Biotechnologica et Chimica 16, no. 1 (2017): 1–11. http://dx.doi.org/10.1515/nbec-2017-0001.

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AbstractProduction of recombinant proteins in Escherichia coli expression systems has shown many advantages, as well as disadvantages, especially for biotechnological and other down-stream applications. The choice of an appropriate vector depends on the gene, to be cloned for purification procedures and other analyses. Selection of a suitable production strain plays an important role in the preparation of recombinant proteins. The main criteria for the selection of the host organism are the properties of the recombinant produced protein, its subsequent use and the total amount desired. The mos

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Sims, Andrew H., Manda E. Gent, Karin Lanthaler, Nigel S. Dunn-Coleman, Stephen G. Oliver, and Geoffrey D. Robson. "Transcriptome Analysis of Recombinant Protein Secretion by Aspergillus nidulans and the Unfolded-Protein Response In Vivo." Applied and Environmental Microbiology 71, no. 5 (2005): 2737–47. http://dx.doi.org/10.1128/aem.71.5.2737-2747.2005.

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ABSTRACT Filamentous fungi have a high capacity for producing large amounts of secreted proteins, a property that has been exploited for commercial production of recombinant proteins. However, the secretory pathway, which is key to the production of extracellular proteins, is rather poorly characterized in filamentous fungi compared to yeast. We report the effects of recombinant protein secretion on gene expression levels in Aspergillus nidulans by directly comparing a bovine chymosin-producing strain with its parental wild-type strain in continuous culture by using expressed sequence tag micr

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Chi, Yu-Hsiang, and Li-Fen Huang. "Current Strategies to Improve Yield of Recombinant Protein Production in Rice Suspension Cells." Processes 10, no. 6 (2022): 1120. http://dx.doi.org/10.3390/pr10061120.

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A plant cell-based recombinant glucocerebrosidase was approved by the FDA in 2012 for the treatment of human inherited Gaucher disease, indicating that plant suspension cells have advantages in biosafety and a low production cost as a commercial pharmaceutical recombinant protein expression system. A low allergenic rice suspension cell-based recombinant protein expression system controlled by the αAmy3/RAmy3D promoter has been shown to result in relatively high protein yields in plant cell-based systems. Although several recombinant proteins have been produced in rice suspension cell-based sys

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Ohtake, Satoshi, and Tsutomu Arakawa. "Recombinant Therapeutic Protein Vaccines." Protein & Peptide Letters 20, no. 12 (2013): 1324–44. http://dx.doi.org/10.2174/092986652012131112122245.

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Fuerst, Walter. "Recombinant Activated Protein C." Critical Care Medicine 32, no. 1 (2004): 311–12. http://dx.doi.org/10.1097/01.ccm.0000104932.57061.ad.

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Stein, M.D.,, Richard A. "Recombinant Protein Expression Advances." Genetic Engineering & Biotechnology News 31, no. 16 (2011): 34–36. http://dx.doi.org/10.1089/gen.31.16.14.

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Bill, Roslyn M., Alan D. Goddard, and Alice J. Rothnie. "Recombinant Membrane Protein Methods." Methods 147 (September 2018): 1–2. http://dx.doi.org/10.1016/j.ymeth.2018.08.007.

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Heidary, Somayyeh, Amir Yaghoubi Nezhad, and Atefeh Mehrabi Far. "Colonization and Investigation of Vibrio Cholera Recombination Protein in E-Coli." International Journal of Engineering & Technology 7, no. 4.7 (2018): 32. http://dx.doi.org/10.14419/ijet.v7i4.7.20375.

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Background and aim: Vibrio cholerae is a gram-negative bacterial pathogen that causes diarrheal disease. One of the most pathogenic factors of V. cholerae is toxin-coregulated pili. This pilus is required as the first factor in the colonization and bacterial persistence in the small intestine. Materials and Methods: In this study, V. cholerae toxin-coregulated pili A (TCPA) gene was amplified using PCR method. The above genes were purified and then expressed by being cloned into the pGEX4T-1 plasmid. Then the recombinant plasmid structure was introduced into the E. coli bacterium. Protein prod

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Tuan, Rocky S. "RECOMBINANT GENE EXPRESSION PROTOCOLS AND RECOMBINANT PROTEIN PROTOCOLS." Shock 8, no. 4 (1997): 311. http://dx.doi.org/10.1097/00024382-199710000-00013.

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Zhang, Ren-wen, Yong Qiao, Xiao-hua Hao, et al. "Identification of Human Hepatocyte Proliferation Related Gene C2orf69." Infection International 3, no. 1 (2014): 1–9. http://dx.doi.org/10.1515/ii-2017-0066.

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Abstract Objective To construct the prokaryotic expression vector pET-32a(+)-C2orf69 and induce the expression of recombinant proteins in vitro. Then the possible effects of recombinant protein on cell proliferation was observed and rabbit-anti-C2orf69 protein polyclonal antibodies was obtained. Methods Gene fragment of C2orf69 was amplified by PCR and then prokaryotic expression plasmid pET-32a(+)-C2orf69 was constructed. Recombinant protein C2orf69 expression was identified by SDS-PAGE and Western blot. The white-ear rabbits were immunized with purified recombinant protein C2orf69, and the p

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Sproles, Ashley E., Anthony Berndt, Francis J. Fields, and Stephen P. Mayfield. "Improved high-throughput screening technique to rapidly isolate Chlamydomonas transformants expressing recombinant proteins." Applied Microbiology and Biotechnology 106, no. 4 (2022): 1677–89. http://dx.doi.org/10.1007/s00253-022-11790-9.

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Abstract The single-celled eukaryotic green alga Chlamydomonas reinhardtii has long been a model system for developing genetic tools for algae, and is also considered a potential platform for the production of high-value recombinant proteins. Identifying transformants with high levels of recombinant protein expression has been a challenge in this organism, as random integration of transgenes into the nuclear genome leads to low frequency of cell lines with high gene expression. Here, we describe the design of an optimized vector for the expression of recombinant proteins in Chlamydomonas, that

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Koupriyanov, V. V., L. I. Nikolaeva, A. A. Zykova, et al. "IMMUNOGENIC PROPERTIES OF RECOMBINANT MOZAIC PROTEINS BASED ON ANTIGENS NS4A AND NS4B OF HEPATITIS C VIRUS." Problems of Virology, Russian journal 63, no. 3 (2018): 138–43. http://dx.doi.org/10.18821/0507-4088-2018-63-3-138-143.

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The aim of the study was to investigate immunogenic properties of mosaic recombinant proteins constructed on the data of hepatitis C virus NS4A and NS4B antigens. Four mosaic recombinant proteins, containing the T and B epitopes of the NS4A and NS4B antigens, were created by genetic engineering methods in the E. coli system. To enhance the immune response they were linked in different variations to the nucleotide sequences of murine interleukin-2 (IL-2), the Neisseria meningiditis lipopeptide, and the T helper epitope of the core protein of hepatitis C virus. The immunogenic properties of thes

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Hayat, Seyed Mohammad Gheibi, Najmeh Farahani, Behrouz Golichenari, and Amirhossein Sahebkar. "Recombinant Protein Expression in Escherichia coli (E.coli): What We Need to Know." Current Pharmaceutical Design 24, no. 6 (2018): 718–25. http://dx.doi.org/10.2174/1381612824666180131121940.

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Background: Host, vector, and culture conditions (including cultivation media) are considered among the three main elements contributing to a successful production of recombinant proteins. Accordingly, one of the most common hosts to produce recombinant therapeutic proteins is Escherichia coli. Methodology: A comprehensive literature review was performed to identify important factors affecting production of recombinant proteins in Escherichia coli. Results: Escherichia coli is taken into account as the easiest, quickest, and cheapest host with a fully known genome. Thus, numerous modifications

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Грудинин, Михаил, Mihail Grudinin, Андрей Комиссаров, et al. "Generation and characterization of the VP1 recombinant protein of the chicken anemia virus." Russian veterinary journal 2019, no. 2 (2019): 12–20. http://dx.doi.org/10.32416/article_5cd16d06b14db8.99635578.

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The aim of this study is to obtain a VP1 recombinant protein of the chicken anemia virus, capable of specifically detecting antibodies in the blood sera of sick chickens.  Materials and methods. Cloning of a fragment of the VP1 gene of an infectious anemia virus of chickens was performed in the expression plasmids pET15b and pGEX-3T in the context of reading the polyhistidine sequence and glutathione-S-transferase, respectively. The recombinant proteins 6HIS-ΔVP1 and GST-ΔVP1 expressed in E. coli Rosetta (DE3) strains were purified by metal affinity chromatography. Amino acid seque

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Kim, Kangsan, Donghui Choe, Dae-Hee Lee, and Byung-Kwan Cho. "Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins." International Journal of Molecular Sciences 21, no. 3 (2020): 990. http://dx.doi.org/10.3390/ijms21030990.

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A large proportion of the recombinant proteins manufactured today rely on microbe-based expression systems owing to their relatively simple and cost-effective production schemes. However, several issues in microbial protein expression, including formation of insoluble aggregates, low protein yield, and cell death are still highly recursive and tricky to optimize. These obstacles are usually rooted in the metabolic capacity of the expression host, limitation of cellular translational machineries, or genetic instability. To this end, several microbial strains having precisely designed genomes ha

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Clissold, P. M. "Recombinant glycosyl-phosphatidylinositol-anchored proteins are not associated with protein kinases in transfected thymoma cells." Biochemical Journal 304, no. 3 (1994): 853–59. http://dx.doi.org/10.1042/bj3040853.

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The cross-linking by antibody of some glycosyl-phosphatidyl-inositol (GPI)-anchored proteins on the plasma membrane of T cells leads to cell activation. Phosphorylation of proteins on tyrosine residues has a central role in the control of T cell activation, and non-receptor protein tyrosine kinases can be coprecipitated with immune complexes of GPI-anchored proteins in T cell lysates. In order to investigate the nature of this interaction, two recombinant GPI-anchored proteins were constructed (using the GPI signal sequence from Thy-1), and their associations with protein tyrosine kinases in s

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