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Emma A Arigi

from Fayetteville, NC
Age ~47
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Also known as:
Emma Arigi Appresai
Related to:
Florence Arigi
Connected to:
Thomas J Arigi, 61Regina F Arigo, 76Suzanne Arigoni, 66Muthukumaran Arigovindan, 46Brian U Ariguzo, 37Hiroko Arikawa, 61Peter Arike, 64Alan J Arikian, 82Jeanette Arikian, 94Jon S Arima, 60

Emma Arigi Phones & Addresses

  • Fayetteville, NC
  • Norwalk, OH
  • El Paso, TX
  • Milton, NH
  • Newmarket, NH
  • Durham, NH
  • Beckley, WV

Resumes

Resumes

Emma Arigi Photo 1

Emma Arigi

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Location:
305 White Oak Ct, Fayetteville, NC 28303
Industry:
Higher Education
Work:
University of Texas since Jul 2010
MS Research Specialist
University of Copenhagen Feb 2008 - Mar 2010
Post Doc
University of New Hampshire 2002 - 2007
Graduate Student
Education:
University of New Hampshire 2002 - 2007
PhD, Chemistry Egerton University
Skills:
Analytical Chemistry
Chromatography
Esi Ms
Mass Spectrometry
Cell Culture
Western Blotting
Chemistry
Hplc
Lc Ms
Proteomics
Maldi Tof
Emma Arigi Photo 2

Freelance Medical Writer

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Location:
Raleigh, NC
Industry:
Professional Training & Coaching
Work:

Freelance Medical Writer

Publications

Us Patents

Methods For Glyco-Engineering Plant Cells For Controlled Human O-Glycosylation

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US Patent:
20110237782, Sep 29, 2011
Filed:
Mar 23, 2011
Appl. No.:
13/070248
Inventors:
Zhang Yang - Vanlose, DK
Damian Paul Drew - Gawler East, AU
Emma Adhiambo Arigi - El Paso TX, US
Peter Ulvskov - Charlottenlund, DK
Steven B. Levery - Holte, DK
Eric Paul Bennett - Lyngby, DK
Henrik Clausen - Holte, DK
Brent Larsen Petersen - Roskilde, DK
International Classification:
C07K 14/00
C12N 15/82
C12P 21/00
US Classification:
530395, 435468, 435 691
Abstract:
This invention discloses the development of a novel platform for recombinant production of bioactive glycoproteins and cancer specific vaccines in plants. Plants and plant cell cultures have been humanized with respect to human mucin-type protein O-glycosylation. A panel of plant cell factories for production of recombinant glycoproteins with designed human O-glycosylation, including an improved cancer vaccine candidate, has been developed. The platform provides basis for i) production of an essentially unlimited array of O-glycosylated human glycoprotein therapeutics, such as human interferon α2B and podoplanin, and ii) for further engineering of additional cancer specific O-glycans on glycoproteins of therapeutical value. Currently, mammalian cells are required for human O-glycosylation, but plants offer a unique cell platform for engineering O-glycosylation since they do not perform human type O-glycosylation. Introduction of O-glycosylation into plant cells requires i) that wild-type plant cells do not modify the target peptide substrates and ii) that the appropriate enzymes and substrates are introduced into of plant cells such that O-glycosylation in the secretory pathway proceed and the glycosylated peptide substrates are preferentially exported to the exterior of the cell or accumulated in the cell. In this invention i) the integrity of transiently and stably expressed ‘mucin’ type target peptides in plants cells has been determined and ii) mucin-type O-glycosylation has been established in plants by transient and stable introduction of a C4-epimerase, the human polypeptide GalNAc-transferases T2 and T4 (GalNAc-T2 and T4) and various human target peptides or proteins. In the present invention GalNAc-T2 and -T4 have been used to produce a Tn cancer glycoform of MUC1.
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Emma A Arigi from Fayetteville, NC, age ~47 Get Report