Table 1. Expression vectors for MCP-xFP fusion proteins for use in mammalian cells

2007 ◽  
Vol 2007 (11) ◽  
pp. pdb.tab194869
Keyword(s):  
Fusion Proteins ◽  
Mammalian Cells ◽  
Expression Vectors

scholarly journals Expression of Hirudin Fusion Proteins in Mammalian Cells

Circulation ◽  
1998 ◽  
Vol 98 (24) ◽  
pp. 2744-2752 ◽  
Author(s):  
Kristian Riesbeck ◽  
Daxin Chen ◽  
Geoffrey Kemball-Cook ◽  
John H. McVey ◽  
Andrew J. T. George ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Mammalian Cells

Overexpression of kin17 protein disrupts nuclear morphology and inhibits the growth of mammalian cells

1999 ◽  
Vol 112 (19) ◽  
pp. 3215-3224 ◽  
Author(s):  
P. Kannouche ◽  
J.F. Angulo
Keyword(s):  
Dna Replication ◽  
Mammalian Cells ◽  
Cell Cycle Progression ◽  
Reca Protein ◽  
S Phase ◽  
Expression Vectors ◽  
Nuclear Morphology ◽  
Functional Domain ◽  
Genetic Response ◽  
Cycle Progression

UVC or ionizing radiation of mammalian cells elicits a complex genetic response that allows recovery and cell survival. Kin17 gene, which is highly conserved among mammals, is upregulated during this response. Kin17 gene encodes a 45 kDa protein which binds to DNA and presents a limited similarity with a functional domain of the bacterial RecA protein. Kin17 protein is accumulated in the nucleus of proliferating fibroblasts and forms intranuclear foci. Using expression vectors, we show that overexpression of kin17 protein inhibits cell-cycle progression into S phase. Our results indicate that growth inhibition correlates with disruption of the nuclear morphology which seems to modify the intranuclear network required during the early steps of DNA replication. We report that a mutant encoding a protein deleted from the central domain of kin17 protein enhanced these effects whereas the deletion of the C-terminal domain considerably reduced them. These mutants will be used to elucidate the molecular mechanism by which kin17 protein alters cell growth and DNA replication.

Preparing mFc- and hFc-Fusion Proteins from Mammalian Cells

2021 ◽  
Vol 2021 (8) ◽  
pp. pdb.prot100040
Author(s):  
Edward A. Greenfield ◽  
James DeCaprio ◽  
Mohan Brahmandam
Keyword(s):  
Fusion Proteins ◽  
Mammalian Cells

Expression Vectors for Enzyme Restriction- and Ligation-Independent Cloning for Producing Recombinant His-Fusion Proteins

2008 ◽  
Vol 23 (3) ◽  
pp. 680-686 ◽  
Author(s):  
Blanca de las Rivas ◽  
José Antonio Curiel ◽  
José Miguel Mancheño ◽  
Rosario Muñoz
Keyword(s):  
Fusion Proteins ◽  
Expression Vectors ◽  
Ligation Independent Cloning

scholarly journals Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells.

1994 ◽  
Vol 14 (3) ◽  
pp. 1721-1732 ◽  
Author(s):  
C A Bunker ◽  
R E Kingston
Keyword(s):  
Binding Sites ◽  
Transcriptional Repression ◽  
Fusion Proteins ◽  
Mammalian Cells ◽  
Polycomb Group ◽  
Polycomb Group Proteins ◽  
Related Gene ◽  
Activation Domains ◽  
Sex Combs ◽  
Significant Homology

The Polycomb group (Pc-G) genes are essential for maintaining the proper spatially restricted expression pattern of the homeotic loci during Drosophila development. The Pc-G proteins appear to function at target loci to maintain a state of transcriptional repression. The murine oncogene bmi-1 has significant homology to the Pc-G gene Posterior sex combs (Psc) and a highly related gene, Suppressor two of zeste [Su(z)2]. We show here that the proteins encoded by bmi-1 and the Pc-G genes Polycomb (Pc) and Psc as well as Su(z)2 mediate repression in mammalian cells when targeted to a promoter by LexA in a cotransfection system. These fusion proteins repress activator function by as much as 30-fold, and the effect on different activation domains is distinct for each Pc-G protein. Repression is observed when the LexA fusion proteins are bound directly adjacent to activator binding sites and also when bound 1,700 bases from the promoter. These data demonstrate that the products of the Pc-G genes can significantly repress activator function on transiently introduced DNA. We suggest that this function contributes to the stable repression of targeted loci during development.

scholarly journals Different expression levels of two KgmB-His fusion proteins

2005 ◽  
Vol 70 (12) ◽  
pp. 1401-1407 ◽  
Author(s):  
Sandra Markovic ◽  
Sandra Vojnovic ◽  
Milija Jovanovic ◽  
Branka Vasiljevic
Keyword(s):  
Recombinant Proteins ◽  
Fusion Proteins ◽  
Kanamycin Resistance ◽  
Expression Vectors ◽  
E Coli ◽  
C Terminus ◽  
N Terminus ◽  
Different Levels ◽  
Streptomyces Tenebrarius

The KgmB methylase from Streptomyces tenebrarius was expressed and purified using the QIAexpress System. Two expression vectors were made: pQEK-N, which places a (His)6 tag at the N-terminus, and pQEK-C, which places a (His)6 tag at the C-terminus of the recombinant KgmB protein. Kanamycin resistance of the E. coli cells containing either the pQEK-N or the pQEK-C recombinant plasmids confirmed the functionality of both KgmB-His fusion proteins in vivo. Interestingly, different levels of expression were observed between these two recombinant proteins. Namely, KgmB methylase with the (His)6 tag at the N-terminus showed a higher level of expression. Purification of the (His)6-tagged proteins using Ni-NTA affinity chromatography was performed under native conditions and the KgmB methylase with (His)6 tag at the N-terminus was purified to homogeneity >95 %. The recombinant KgmB protein was detected on a Western blot using anti-Sgm antibodies.

scholarly journals Virus-based pharmaceutical production in plants: an opportunity to reduce health problems in Africa

2019 ◽  
Vol 16 (1) ◽  
Author(s):  
Pingdwende Kader Aziz Bamogo ◽  
Christophe Brugidou ◽  
Drissa Sérémé ◽  
Fidèle Tiendrébéogo ◽  
Florencia Wendkuuni Djigma ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Developing World ◽  
Neglected Tropical Diseases ◽  
Scale Up ◽  
Plant Viruses ◽  
Health Problems ◽  
Expression Vectors ◽  
Neglected Diseases ◽  
Main Body ◽  
Viral Expression

Abstract Background Developing African countries face health problems that they struggle to solve. The major causes of this situation are high therapeutic and logistical costs. Plant-made therapeutics are easy to produce due to the lack of the safety considerations associated with traditional fermenter-based expression platforms, such as mammalian cells. Plant biosystems are easy to scale up and inexpensive, and they do not require refrigeration or a sophisticated medical infrastructure. These advantages provide an opportunity for plant-made pharmaceuticals to counteract diseases for which medicines were previously inaccessible to people in countries with few resources. Main body The techniques needed for plant-based therapeutic production are currently available. Viral expression vectors based on plant viruses have greatly enhanced plant-made therapeutic production and have been exploited to produce a variety of proteins of industrial, pharmaceutical and agribusiness interest. Some neglected tropical diseases occurring exclusively in the developing world have found solutions through plant bioreactor technology. Plant viral expression vectors have been reported in the production of therapeutics against these diseases occurring exclusively in the third world, and some virus-derived antigens produced in plants exhibit appropriate antigenicity and immunogenicity. However, all advances in the use of plants as bioreactors have been made by companies in Europe and America. The developing world is still far from acquiring this technology, although plant viral expression vectors may provide crucial help to overcome neglected diseases. Conclusion Today, interest in these tools is rising, and viral amplicons made in and for Africa are in progress. This review describes the biotechnological advances in the field of plant bioreactors, highlights factors restricting access to this technology by those who need it most and proposes a solution to overcome these limitations.

scholarly journals Preparation and Characterization of Anti-CeTNT-1 and Anti-CeTNT-4 Antibodies

1970 ◽  
Vol 44 (3) ◽  
pp. 371-376
Author(s):  
M Ziaul Amin ◽  
Hiroaki Kagawa ◽  
Mohammed A Satter
Keyword(s):  
Fusion Proteins ◽  
Tissue Specificity ◽  
Body Wall ◽  
Troponin T ◽  
Specific Interaction ◽  
The Body ◽  
Expression Vectors ◽  
Antibody Specificity ◽  
Sds Page

Among the four CeTNT isoforms, CeTNT-1, CeTNT-2 are body wall types, CeTNT-4 is pharynx type and CeTNT-3 is expressed in both the body wall and pharyngeal tissue. In our previous study, we used body wall and pharynx type anti-CeTNI, anti-CeTNC and anti-CeTM antibodies to observe the tissue specific interaction of the TNI isoforms with others TN subunits and tropomyosin isoforms. To extent the interaction study of CeTNT isoforms, in this study, we prepared and characterized the body wall type anti-CeTNT-1 and pharynx type anti- CeTNT-4 antibodies. For the preparation of the anti-CeTNT-1 and anti-CeTNT-4 antibodies, in this study we constructed the pCTNT-1 and pCTNT-4 expression vectors. The sub-cloned of the pCTNT-1 and pCTNT-4 expression vectors were verified by DNA sequencing. These expression vectors were used to generate fusion proteins of the body wall, TNT-1 and pharyngeal TNT-4 isoforms in Escherichia Ecoli. The expression of these fusion proteins were confirmed by SDS-PAGE analysis. The anti-CeTNT-1 and anti-CeTNT-4 antibodies were prepared in the rabbit by using the gel cut of the CeTNT-1 and CeTNT-4 fusion proteins. The antibody specificity of the CeTNT-1 and CeTNT-4 fusion proteins was also judged by Western-analysis using prepared anti-CeTNT-1 and anti-CeTNT-4 antibodies. The antibody specificity results indicated that anti-sera against each of both the body wall type TNT-1 and pharynx type TNT-4 isoforms had tissue specificity. Key words: Troponin T, Caenorhabditis elegans, Body wall, Pharynx DOI: 10.3329/bjsir.v44i3.4413 Bangladesh J. Sci. Ind. Res. 44(3), 371-376, 2009

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