GST-fusion Protein Purification

SciVee ◽  
2010 ◽  
Author(s):  
Abnova Corp
Keyword(s):  
Fusion Protein ◽  
Protein Purification ◽  
Gst Fusion Protein

Vector Engineering Anomalies: Impact on Fusion Protein Purification Performance

1999 ◽  
Vol 17 (3) ◽  
pp. 449-455 ◽  
Author(s):  
Richard S. Pasquinelli ◽  
Richard R. Koepsel ◽  
Naxin Wu ◽  
Mohammad M. Ataai
Keyword(s):  
Fusion Protein ◽  
Protein Purification

scholarly journals Real-Time Assay of the Interaction of a GST Fusion Protein with a Protein Ligate Using Resonant Mirror Technique

BioTechniques ◽  
1997 ◽  
Vol 22 (2) ◽  
pp. 269-271 ◽  
Author(s):  
Ignacio Rubio ◽  
Philip Buckle ◽  
Hans Trutnau ◽  
Reinhard Wetzker
Keyword(s):  
Fusion Protein ◽  
Real Time ◽  
Gst Fusion Protein

scholarly journals Functional Expression and One-Step Protein Purification of Manganese Peroxidase 1 (rMnP1) from Phanerochaete chrysosporium Using the E. coli-Expression System

2020 ◽  
Vol 21 (2) ◽  
pp. 416
Author(s):  
Angel De La Cruz Pech-Canul ◽  
Javier Carrillo-Campos ◽  
María de Lourdes Ballinas-Casarrubias ◽  
Rosa Lidia Solis-Oviedo ◽  
Selena Karina Hernández-Rascón ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Protein Purification ◽  
Phanerochaete Chrysosporium ◽  
Manganese Peroxidase ◽  
Expression System ◽  
White Rot Fungi ◽  
Functional Expression ◽  
White Rot ◽  
E Coli ◽  
One Step

Manganese peroxidases (MnP) from the white-rot fungi Phanerochaete chrysosporium catalyse the oxidation of Mn2+ to Mn3+, a strong oxidizer able to oxidize a wide variety of organic compounds. Different approaches have been used to unravel the enzymatic properties and potential applications of MnP. However, these efforts have been hampered by the limited production of native MnP by fungi. Heterologous expression of MnP has been achieved in both eukaryotic and prokaryotic expression systems, although with limited production and many disadvantages in the process. Here we described a novel molecular approach for the expression and purification of manganese peroxidase isoform 1 (MnP1) from P. chrysosporium using an E. coli-expression system. The proposed strategy involved the codon optimization and chemical synthesis of the MnP1 gene for optimised expression in the E. coli T7 shuffle host. Recombinant MnP1 (rMnP1) was expressed as a fusion protein, which was recovered from solubilised inclusion bodies. rMnP1 was purified from the fusion protein using intein-based protein purification techniques and a one-step affinity chromatography. The designated strategy allowed production of an active enzyme able to oxidize guaiacol or Mn2+.

Production of Recombinant Melittin by Auto-Induction in Escherichia coli

2013 ◽  
Vol 798-799 ◽  
pp. 1007-1012
Author(s):  
Wen He Zhu ◽  
Wei Zhang ◽  
Yan Li ◽  
Jun Jie Xu ◽  
Shi Jie Lv
Keyword(s):  
Fusion Protein ◽  
Large Scale ◽  
Expression Vector ◽  
Human Cancer ◽  
Expression System ◽  
Scale Production ◽  
Recognition Sequence ◽  
Large Scale Production ◽  
N Terminus ◽  
Gst Fusion Protein

Melittin is a novel peptide of biological activity isolated from bee venom. It has potential application value in medicine and agriculture. Here we encoded melittin gene with the EK recognition sequence in the N-terminus into expression vector pGEX-2T.The expressed fusion protein, which is about 29KDa, identified by Western Blot. To facilitate large-scale production of recombinant GST-fusion protein, we optimized different expression conditions to increase the overall production of the fusion protein. The production of the protein had increased about 10-fold when we used an auto-inducing medium. The GST fusion protein showed an equivalent activity with the natural melittin after digested by EK and can inhibited the proliferations of several human cancer lines. The expression system described in this study provides a feasible way for producing melittin in further studies.

scholarly journals Expression in Bacteria of the Gene Encoding the gp43 Antigen of Paracoccidioides brasiliensis: Immunological Reactivity of the Recombinant Fusion Proteins

2002 ◽  
Vol 9 (6) ◽  
pp. 1200-1204 ◽  
Author(s):  
Susana N. Diniz ◽  
Kátia C. Carvalho ◽  
Patrícia S. Cisalpino ◽  
José F. Silveira ◽  
Luiz R. Travassos ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Fusion Protein ◽  
Fusion Proteins ◽  
Inclusion Bodies ◽  
Paracoccidioides Brasiliensis ◽  
Immunological Reactivity ◽  
Gene Encoding ◽  
Recombinant Fusion Proteins ◽  
Gst Fusion Protein

ABSTRACT gp43 is the major diagnostic antigen of Paracoccidioides brasiliensis, the agent of paracoccidioidomycosis (PCM) in humans. In the present study, cDNA of the gp43 gene (PbGP43) was obtained by reverse transcriptase PCR, inserted into a pGEX vector in frame with the glutathione S-transferase (GST) gene, and expressed in Escherichia coli as inclusion bodies. Immunoblotting showed that all sera from patients with chronic pulmonary and acute lymphatic forms of PCM reacted with the recombinant fusion protein of the mature gp43 (381 amino acids). Reactivity with fusion proteins containing subfragments of the N-terminal, internal, or C-terminal regions occurred eventually, and the C-terminal region was the most antigenic. Lack of reactivity with the subfragments may be due to the conformational nature of the gp43 epitopes. Sera from patients with aspergillosis, candidiasis, and histoplasmosis did not react with the gp43-GST fusion protein. Our results suggest that recombinant gp43 corresponding to the processed antigen can be a useful tool in the diagnosis of PCM.

scholarly journals Isolation of Dihydroflavonol 4-Reductase cDNA Clones from Angelonia x angustifolia and Heterologous Expression as GST Fusion Protein in Escherichia coli

PLoS ONE ◽  
2014 ◽  
Vol 9 (9) ◽  
pp. e107755 ◽  
Author(s):  
Christian Gosch ◽  
Karthik Mudigere Nagesh ◽  
Jana Thill ◽  
Silvija Miosic ◽  
Sylvia Plaschil ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Heterologous Expression ◽  
Cdna Clones ◽  
Gst Fusion Protein

Expression of an autoprocessing cat-HIV-1 proteinase fusion protein: Purification to homogeneity of the released 99 residue proteinase

1991 ◽  
Vol 175 (3) ◽  
pp. 784-794 ◽  
Author(s):  
Douglas S. Montgomery ◽  
Onkar M.P. Singh ◽  
Norman M. Gray ◽  
Colin W. Dykes ◽  
Malcolm P. Weir ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Protein Purification ◽  
Hiv 1
Sign in / Sign up

Export Citation Format

Share Document