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	Provedor de dados BJMBR (4) J. Venom. Anim. Toxins (1) Autor Ho,P.L. (5) Carvalho,E. (2) Nascimento,A.L.T.O. (2) Abreu,P.A.E. (1) Assni,A. (1) Camargo,L.E.A. (1) Campos,A.C.M.R. (1) Carmona,E. (1) Digiampietri,L.A. (1) Haake,D.A. (1) Harstkeerl,R.A. (1) Hauk,P. (1) Marques,M.V. (1) Martins,E.A.L. (1) Miyaji,E.N. (1) Monteiro-Vitorello,C.B. (1) Oliveira,M.C. (1) Oliveira,M.L.S. (1) Ramos,C.R.R. (1) Raw,I (1) Mais... Palavra-chave Vaccine (2) Adjuvant (1) Antigen (1) DAMP (1) Diagnosis (1) Escherichia coli (1) Expression vector (1) Immobilized metal affinity chromatography (1) Innate immunity (1) Leptospira interrogans (1) LipL32 (1) Lipopolysaccharides (1) Non-tagged protein purification (1) Outer membrane proteins (1) PAMP (1) Pathogenic Leptospira (1) Protein purification (1) Regulatory systems (1) Transport (1) Mais... Tipo do documento Info:eu-repo/semantics/article (4) Info:eu-repo/semantics/other (1) Ano 2011 (2) 2004 (2) 1997 (1) País Brazil (5) Idioma Inglês (5)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 5 Primeira ... 1 ... Última A high-copy T7 Escherichia coli expression vector for the production of recombinant proteins with a minimal N-terminal His-tagged fusion peptide BJMBR Ramos,C.R.R.; Abreu,P.A.E.; Nascimento,A.L.T.O.; Ho,P.L.. We report here the construction of a vector derived from pET3-His and pRSET plasmids for the expression and purification of recombinant proteins in Escherichia coli based on T7 phage RNA polymerase. The resulting pAE plasmid combined the advantages of both vectors: small size (pRSET), expression of a short 6XHis tag at N-terminus (pET3-His) and a high copy number of plasmid (pRSET). The small size of the vector (2.8 kb) and the high copy number/cell (200-250 copies) facilitate the subcloning and sequencing procedures when compared to the pET system (pET3-His, 4.6 kb and 40-50 copies) and also result in high level expression of recombinant proteins (20 mg purified protein/liter of culture). In addition, the vector pAE enables the expression of a fusion... Tipo: Info:eu-repo/semantics/article Palavras-chave: Escherichia coli; Expression vector; Immobilized metal affinity chromatography; Protein purification. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000800001 CLONING AND EXPRESSION OF A POTENTIAL PRESYNAPTIC NEUROTOXIN PHOSPHOLIPASE A2-TYPE FROM THE CORAL SNAKE Micrurus corallinus J. Venom. Anim. Toxins Assni,A.; Carmona,E.; Campos,A.C.M.R.; Raw,I; Ho,P.L.. Tipo: Info:eu-repo/semantics/other Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79301997000200024 Expression and purification of the non-tagged LipL32 of pathogenic Leptospira BJMBR Hauk,P.; Carvalho,E.; Ho,P.L.. Leptospirosis is a reemerging infectious disease and the most disseminated zoonosis worldwide. A leptospiral surface protein, LipL32, only occurs in pathogenic Leptospira, and is the most abundant protein on the bacterial surface, being described as an important factor in host immunogenic response and also in bacterial infection. We describe here an alternative and simple purification protocol for non-tagged recombinant LipL32. The recombinant LipL32(21-272) was expressed in Escherichia coli without His-tag or any other tag used to facilitate recombinant protein purification. The recombinant protein was expressed in the soluble form, and the purification was based on ion exchange (anionic and cationic) and hydrophobic interactions. The final purification... Tipo: Info:eu-repo/semantics/article Palavras-chave: Antigen; LipL32; Pathogenic Leptospira; Non-tagged protein purification; Diagnosis; Vaccine. Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2011000400005 Genome features of Leptospira interrogans serovar Copenhageni BJMBR Nascimento,A.L.T.O.; Verjovski-Almeida,S.; Van Sluys,M.A.; Monteiro-Vitorello,C.B.; Camargo,L.E.A.; Digiampietri,L.A.; Harstkeerl,R.A.; Ho,P.L.; Marques,M.V.; Oliveira,M.C.; Setubal,J.C.; Haake,D.A.; Martins,E.A.L.. We report novel features of the genome sequence of Leptospira interrogans serovar Copenhageni, a highly invasive spirochete. Leptospira species colonize a significant proportion of rodent populations worldwide and produce life-threatening infections in mammals. Genomic sequence analysis reveals the presence of a competent transport system with 13 families of genes encoding for major transporters including a three-member component efflux system compatible with the long-term survival of this organism. The leptospiral genome contains a broad array of genes encoding regulatory system, signal transduction and methyl-accepting chemotaxis proteins, reflecting the organism's ability to respond to diverse environmental stimuli. The identification of a complete set... Tipo: Info:eu-repo/semantics/article Palavras-chave: Leptospira interrogans; Outer membrane proteins; Lipopolysaccharides; Transport; Regulatory systems. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000400003 Trends in adjuvant development for vaccines: DAMPs and PAMPs as potential new adjuvants BJMBR Miyaji,E.N.; Carvalho,E.; Oliveira,M.L.S.; Raw,I.; Ho,P.L.. Aluminum salts have been widely used in vaccine formulations and, after their introduction more than 80 years ago, only few vaccine formulations using new adjuvants were developed in the last two decades. Recent advances in the understanding of how innate mechanisms influence the adaptive immunity opened up the possibility for the development of new adjuvants in a more rational design. The purpose of this review is to discuss the recent advances in this field regarding the attempts to determine the molecular basis and the general mechanisms underlying the development of new adjuvants, with particular emphasis on the activation of receptors of innate immune recognition. One can anticipate that the use of these novel adjuvants will also provide a window of... Tipo: Info:eu-repo/semantics/article Palavras-chave: Adjuvant; Vaccine; Innate immunity; DAMP; PAMP. Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2011000600003 Registros recuperados: 5 Primeira ... 1 ... Última

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