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11 results on '"Krimer, Alejandro"'

2. Additional file 1: of Production and purification of chimeric HBc virus-like particles carrying influenza virus LAH domain as vaccine candidates

Author

Kazaks, Andris, I-Na Lu, Farinelle, Sophie, Ramirez, Alex, Crescente, Vincenzo, Blaha, Benjamin, Olotu Ogonah, Tarit Mukhopadhyay, Mapi De Obanos, Krimer, Alejandro, Akopjana, Inara, Bogans, Janis, Ose, Velta, Kirsteina, Anna, Kazaka, Tatjana, Stonehouse, Nicola, Rowlands, David, Muller, Claude, Tars, Kaspars, and Rosenberg, William

Abstract

Determination of copy number for integrated expression units in selected P. pastoris clones. Description of the methodology used for quantification of copy number for expression cassettes integrated in selected P. pastoris clones. The method is based on real time PCR amplification of zeocin gene. (DOCX 186 kb)

Published
2017
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3. Additional file 2: of Production and purification of chimeric HBc virus-like particles carrying influenza virus LAH domain as vaccine candidates

Author

Kazaks, Andris, I-Na Lu, Farinelle, Sophie, Ramirez, Alex, Crescente, Vincenzo, Blaha, Benjamin, Olotu Ogonah, Tarit Mukhopadhyay, Mapi De Obanos, Krimer, Alejandro, Akopjana, Inara, Bogans, Janis, Ose, Velta, Kirsteina, Anna, Kazaka, Tatjana, Stonehouse, Nicola, Rowlands, David, Muller, Claude, Tars, Kaspars, and Rosenberg, William

Subjects
viruses, parasitic diseases, virus diseases
Abstract

Serum IgG reactivity against the â emptyâ K1-K1 HBc VLPs and against irrelevant antigens (Cytomegalovirus antigen, purified EBV capsid protein, Toxoplasma gondii antigen). Reactivity of mouse sera with carrier HBc-derived VLPs (positive control) in comparison with irrelevant antigens (negative control) demonstrating specificity of ELISA method used. (PPTX 91 kb)

Published
2017
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4. Production and purification of chimeric HBc virus-like particles carrying influenza virus LAH domain as vaccine candidates

Author

Kazaks, Andris, primary, Lu, I-Na, additional, Farinelle, Sophie, additional, Ramirez, Alex, additional, Crescente, Vincenzo, additional, Blaha, Benjamin, additional, Ogonah, Olotu, additional, Mukhopadhyay, Tarit, additional, de Obanos, Mapi Perez, additional, Krimer, Alejandro, additional, Akopjana, Inara, additional, Bogans, Janis, additional, Ose, Velta, additional, Kirsteina, Anna, additional, Kazaka, Tatjana, additional, Stonehouse, Nicola J., additional, Rowlands, David J., additional, Muller, Claude P., additional, Tars, Kaspars, additional, and Rosenberg, William M., additional

Published
2017
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8. Expression of Human Proacrosin in Escherichia coliand Binding to Zona Pellucida1

Author

Furlong, Laura I., Hellman, Ulf, Krimer, Alejandro, Tezón, Jorge G., Charreau, Eduardo H., and Vazquez-Levin, Mónica H.

Abstract

Proacrosin is a multifunctional protein present in the sperm acrosome. This study characterizes the expression of human proacrosin in bacteria and assesses zona pellucida binding activity. The cDNA encoding human proacrosin was subcloned in pGEX-3X and pET-22b vectors. In the pGEX system, expression of the full-length fusion protein was not detected. In the pET system, an expression product with an apparent molecular size similar to that expected for the proenzyme (Rec-40, 42–44 kDa) was recognized by a monoclonal antibody to human acrosin, AcrC5F10. A 32–34-kDa protein (Rec-30), not recognized by AcrC5F10 on Western blots, was the major expression product. Proteins of 21 (Rec-20) and 18 (Rec-10) kDa were recovered as insoluble expression products as were Rec-40 and Rec-30, and truncated products from the C terminus were detected in the soluble fraction. Rec-40 and Rec-30 coexisted at any culture time tested. Immune serum raised against Rec-30 (AntiRec-30) stained the acrosomal region of permeabilized human spermatozoa and recognized the recombinant proteins and proacrosin from human sperm extracts. Amino acid sequence analysis indicated that Rec-30, Rec-20, and Rec-10 are N-terminal fragments of proacrosin. The recombinant proteins Rec-40, -30, -20, and -10 were found to interact with homologous 125I-zona pellucida glycoproteins.

Published
2000
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9. Additional file 2: of Production and purification of chimeric HBc virus-like particles carrying influenza virus LAH domain as vaccine candidates

Author

Kazaks, Andris, I-Na Lu, Farinelle, Sophie, Ramirez, Alex, Crescente, Vincenzo, Blaha, Benjamin, Olotu Ogonah, Tarit Mukhopadhyay, Mapi De Obanos, Krimer, Alejandro, Akopjana, Inara, Bogans, Janis, Ose, Velta, Kirsteina, Anna, Kazaka, Tatjana, Stonehouse, Nicola, Rowlands, David, Muller, Claude, Tars, Kaspars, and Rosenberg, William

Subjects
viruses, parasitic diseases, virus diseases, 3. Good health
Abstract

Serum IgG reactivity against the â emptyâ K1-K1 HBc VLPs and against irrelevant antigens (Cytomegalovirus antigen, purified EBV capsid protein, Toxoplasma gondii antigen). Reactivity of mouse sera with carrier HBc-derived VLPs (positive control) in comparison with irrelevant antigens (negative control) demonstrating specificity of ELISA method used. (PPTX 91 kb)

10. Additional file 1: of Production and purification of chimeric HBc virus-like particles carrying influenza virus LAH domain as vaccine candidates

Author

Kazaks, Andris, I-Na Lu, Farinelle, Sophie, Ramirez, Alex, Crescente, Vincenzo, Blaha, Benjamin, Olotu Ogonah, Tarit Mukhopadhyay, Mapi De Obanos, Krimer, Alejandro, Akopjana, Inara, Bogans, Janis, Ose, Velta, Kirsteina, Anna, Kazaka, Tatjana, Stonehouse, Nicola, Rowlands, David, Muller, Claude, Tars, Kaspars, and Rosenberg, William

Subjects
3. Good health
Abstract

Determination of copy number for integrated expression units in selected P. pastoris clones. Description of the methodology used for quantification of copy number for expression cassettes integrated in selected P. pastoris clones. The method is based on real time PCR amplification of zeocin gene. (DOCX 186 kb)

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