Production of Full-Length Antibody by Pichia pastoris

2017 ◽  
pp. 37-48 ◽  
Author(s):  
Adam Nylen ◽  
Ming-Tang Chen
Keyword(s):  
Pichia Pastoris ◽  
Full Length

Cloning and Expression of Functional Full-Length Human Tissue Plasminogen Activator in Pichia pastoris

2010 ◽  
Vol 162 (7) ◽  
pp. 2037-2048 ◽  
Author(s):  
Keivan Majidzadeh-A ◽  
Vahid Khalaj ◽  
Davami Fatemeh ◽  
Hemayatkar Mahdi ◽  
Barkhordari Farzaneh ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Human Tissue ◽  
Full Length ◽  
Cloning And Expression ◽  
Tissue Plasminogen

Secreted Expression and Purification of Dengue 2 Virus Full-length Nonstructural Glycoprotein NS1 in Pichia. pastoris

Virus Genes ◽  
2006 ◽  
Vol 33 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Jun-mei Zhou ◽  
Yun-xia Tang ◽  
Dan-yun Fang ◽  
Jing-jiao Zhou ◽  
Yu Liang ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Full Length ◽  
Expression And Purification ◽  
Secreted Expression

scholarly journals Characterization of Full-Length and Truncated Recombinant κ-Carrageenase Expressed in Pichia pastoris

2017 ◽  
Vol 8 ◽  
Author(s):  
Yuan Yu ◽  
Zhemin Liu ◽  
Min Yang ◽  
Meng Chen ◽  
Zhihan Wei ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Full Length

scholarly journals Expression of recombinant full-length plant phytochromes assembled with phytochromobilin in Pichia pastoris

FEBS Letters ◽  
2014 ◽  
Vol 588 (17) ◽  
pp. 2964-2970 ◽  
Author(s):  
Ah-Young Shin ◽  
Yun-Jeong Han ◽  
Pill-Soon Song ◽  
Jeong-Il Kim
Keyword(s):  
Pichia Pastoris ◽  
Full Length

Recombinant full-length factor H from Pichia pastoris—Building on fragmentary knowledge

2010 ◽  
Vol 47 (13) ◽  
pp. 2271-2271
Author(s):  
Christoph Q. Schmidt ◽  
Fern Slingsby ◽  
Mara Guariento ◽  
Haydyn D.T. Mertens ◽  
Dimitri I. Svergun ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Factor H ◽  
Full Length

High-level secretion of recombinant full-length streptavidin in Pichia pastoris and its application to enantioselective catalysis

2014 ◽  
Vol 93 ◽  
pp. 54-62 ◽  
Author(s):  
Elisa S. Nogueira ◽  
Thomas Schleier ◽  
Marc Dürrenberger ◽  
Kurt Ballmer-Hofer ◽  
Thomas R. Ward ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Full Length ◽  
Enantioselective Catalysis ◽  
High Level

scholarly journals Analogous effects of recombinant human full-length amelogenin expressed by Pichia pastoris yeast and enamel matrix derivative in vitro

2012 ◽  
Vol 45 (5) ◽  
pp. 456-465 ◽  
Author(s):  
L. Cheng ◽  
Z. K. Lin ◽  
R. Shu ◽  
D. L. Liu ◽  
X. L. Zhang ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Full Length ◽  
Enamel Matrix Derivative ◽  
Enamel Matrix ◽  
Pichia Pastoris Yeast ◽  
Matrix Derivative

scholarly journals Cloning and Expression of Highly Pathogenic Avian Influenza Virus Full-Length Nonstructural Gene inPichia pastoris

2011 ◽  
Vol 2011 ◽  
pp. 1-5 ◽  
Author(s):  
M. B. Abubakar ◽  
I. Aini ◽  
A. R. Omar ◽  
M. Hair-Bejo
Keyword(s):  
Influenza Virus ◽  
Pichia Pastoris ◽  
Recombinant Protein ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Western Blotting ◽  
Recombinant Plasmid ◽  
Full Length ◽  
Cloning And Expression ◽  
Nucleotide Sequence Analysis

Avian influenza (AI) is a highly contagious and rapidly evolving pathogen of major concern to the poultry industry and human health. Rapid and accurate detection of avian influenza virus is a necessary tool for control of outbreaks and surveillance. The AI virus A/Chicken/Malaysia/5858/2004 (H5N1) was used as a template to produce DNA clones of the full-length NS1 genes via reverse transcriptase synthesis of cDNA by PCR amplification of the NS1 region. Products were cloned into pCR2.0 TOPO TA plasmid and subsequently subcloned into pPICZαA vector to construct a recombinant plasmid. Recombinant plasmid designated as pPICZαA-NS1 gene was confirmed by PCR colony screening, restriction enzyme digestion, and nucleotide sequence analysis. The recombinant plasmid was transformed intoPichia pastoris GS115strain by electroporation, and expressed protein was identified by SDS-PAGE and western blotting. A recombinant protein of approximately ~28 kDa was produced. The expressed protein was able to bind a rabbit polyclonal antibody of nonstructural protein (NS1) avian influenza virus H5N1. The result of the western blotting and solid-phase ELISA assay using H5N1 antibody indicated that the recombinant protein produced retained its antigenicity. This further indicates thatPichia pastoriscould be an efficient expression system for a avian influenza virus nonstructural (NS1).

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