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Company:
Scripps research institute
Address:
10550 N Torrey Pines Rd, La Jolla, CA 92037
Phones:
8587841000
Position:
Educator
Industries:
Noncommercial Research Organizations
Name / Title
Company / Classification
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Stephen Mayfield Educator
Scripps Research Institute Noncommercial Research Organizations
10550 N Torrey Pines Rd, La Jolla, CA 92037
Stephen Mayfield Educator
THE SCRIPPS RESEARCH INSTITUTE, INC Noncommercial Research Organization · Noncommercial Research Organizations, Nsk · Internist · Pediatric Oncologist · Ophthalmology · Offices and Clinics of Medical Doctors · Noncommercial Research Organizations · Services, NEC
10550 N Torrey Pne Rd, La Jolla, CA 92037 10550 N Torrey Pne Rd Tpc-8, La Jolla, CA 92037 10650 N Torrey Pne Rd, La Jolla, CA 92037 10666 N Torrey Pne Rd, La Jolla, CA 92037 8585548653, 8587841000, 8587842937, 8587848228
Us Patents
Rna Binding Protein And Binding Site Useful For Expression Of Recombinant Molecules
The present invention relates to a gene expression system in eukaryotic and prokaryotic cells, preferably plant cells and intact plants. In particular, the invention relates to an expression system having a RB47 binding site upstream of a translation initiation site for regulation of translation mediated by binding of RB47 protein, a member of the poly(A) binding protein family. Regulation is further effected by RB60, a protein disulfide isomerase. The expression system is capable of functioning in the nuclear/cytoplasm of cells and in the chloroplast of plants. Translation regulation of a desired molecule is enhanced approximately 100 fold over that obtained without RB47 binding site activation.
Robust Expression Of A Bioactive Mammalian Protein In Chlamydomonas Chloroplast
Methods and compositions are disclosed to engineer chloroplast comprising heterologous mammalian genes via a direct replacement of chloroplast Photosystem II (PSII) reaction center protein coding regions to achieve expression of recombinant protein above 5% of total protein. When algae is used, algal expressed protein is produced predominantly as a soluble protein where the functional activity of the peptide is intact. As the host algae is edible, production of biologics in this organism for oral delivery or proteins/peptides, especially gut active proteins, without purification is disclosed.
Expression Of Eukaryotic Polypeptides In Chloroplasts
The present invention relates to a gene expression system in eukaryotic and prokaryotic cells, preferably plant cells and intact plants. In particular, the invention relates to an expression system having a RB47 binding site upstream of a translation initiation site for regulation of translation mediated by binding of RB47 protein, a member of the poly(A) binding protein family. Regulation is further effected by RB60, a protein disulfide isomerase. The expression system is capable of functioning in the nuclear/cytoplasm of cells and in the chloroplast of plants. Translation regulation of a desired molecule is enhanced approximately 100 fold over that obtained without RB47 binding site activation.
Expression Of Polypeptides In Chloroplasts, And Compositions And Methods For Expressing Same
Methods of producing one or more polypeptides in a plant chloroplast, including methods of producing polypeptides that specifically associate in a plant chloroplast to generate a functional protein complex, are provided. An isolated polynucleotide that includes (or encodes) a first ribosome binding sequence (RBS) operatively linked to a second RBS, such that the first RBS directs translation of a polypeptide in a prokaryote and the second RBS directs translation of the polypeptide in a chloroplast, also is provided, as is a vector containing such a polynucleotide, particularly a chloroplast vector and a chloroplast/prokaryote shuttle vector. Also provided is a synthetic polynucleotide, which is chloroplast codon biased. A plant cell that is genetically modified to contain a polynucleotide or vector as described above, as well as transgenic plants containing or derived from such a genetically modified cell, are provide. Polypeptides encoded by a synthetic polynucleotide as described also are provided.
Robust Expression Of A Bioactive Mammalian Protein In Chlamydomonas Chloroplast
Methods and compositions are disclosed to engineer chloroplast comprising heterologous mammalian genes via a direct replacement of chloroplast Photosystem II (PSII) reaction center protein coding regions to achieve expression of recombinant protein above 5% of total protein. When algae is used, algal expressed protein is produced predominantly as a soluble protein where the functional activity of the peptide is intact. As the host algae is edible, production of biologics in this organism for oral delivery of proteins/peptides, especially gut active proteins, without purification is disclosed.
Production Of Therapeutic Proteins In Photosynthetic Organisms
Beth A. Rasala - San Diego CA, US Rosa M. F. Cardoso - San Diego CA, US Machiko Muto - San Diego CA, US Stephen P. Mayfield - Cardiff by the Sea CA, US Philip A. Lee - San Diego CA, US Craig A. Behnke - San Diego CA, US Michael Mendez - San Diego CA, US
Assignee:
THE SCRIPPS RESEARCH INSTITUTE - La Jolla CA SAPPHIRE ENERGY, INC. - San Diego CA
International Classification:
C12P 21/00 C07K 14/00 C12N 1/13
US Classification:
530350, 4352572, 435 691
Abstract:
The present disclosure relates to methods of expressing therapeutic proteins in photosynthetic organisms and the therapeutic proteins produced by the methods. The therapeutic proteins include high-mobility group box 1 (HMGB1) protein, fibronectin domain (10) (10FN3), fibronectin domain (14) (14FN3), interferon beta (IFNβ), proinsulin and vascular endothelial growth factor (VEGF). The photosynthetic organisms include prokaryotes such as cyanobacteria and eukaryotes such as alga and plants. Transformation of eukaryotes is preferably the plastid genome, more preferably the chloroplast genome.
Rna Binding Protein And Binding Site Useful For Expression Of Recombinant Molecules
The present invention relates to recombinant protein disulfide isomerase, RB60, that functions as a translational regulator of the binding of a translational activator protein, RB47, to its binding site for the activation of translation. The recombinant RB60 protein is useful in a gene expression system in eukaryotic and prokaryotic cells, preferably plant cells and intact plants.
Rna Binding Protein And Binding Site Useful For Expression Of Recombinant Molecules
The present invention relates to a gene expression system in eukaryotic and prokaryotic cells, preferably plant cells and intact plants. In particular, the invention relates to an expression system having a RB47 binding site upstream of a translation initiation site for regulation of translation mediated by binding of RB47 protein, a member of the poly(A) binding protein family. Regulation is further effected by RB60, a protein disulfide isomerase. The expression system is capable of functioning in the nuclear/cytoplasm of cells and in the chloroplast of plants. Translation regulation of a desired molecule is enhanced approximately 100 fold over that obtained without RB47 binding site activation.
Resumes
Director, San Diego Center For Algae Biotechnology
majority of these fatal cases among African children, the World Health Organisation revealed."Realistically, the only way a malaria vaccine will ever be used is if it can be produced at a fraction of the cost of current vaccines," UCSD professor of biology and research leader Stephen Mayfield declared.
Malaria is caused by a parasite that makes complex proteins, but for whatever reason this parasite doesnt put sugars on those proteins, Stephen Mayfield, a professor of biology at UC San Diego and the leader of the research effort, said, according to Science Daily. If you have a protein covered
"It's too costly to vaccinate two billion people using current technologies," explained Stephen Mayfield, a professor of biology at UCSD. "Realistically, the only way a malaria vaccine will ever be used is if it can be produced at a fraction of the cost of current vaccines. Algae have this potential
Date: May 17, 2012
Category: Sci/Tech
Source: Google
Letters: green energy, Planned Parenthood, teachers, immigration and more
rtation fuels is tremendous, and I am delighted to see that this potential is now seen by both the White House and Congress. Stephen Mayfield, Director, San Diego Center for Algae Biotechnology and John Dove Isaacs Chair of Natural Philosophy Division of Biological Sciences, UC San Diego