Title

Expression of Fluorescently Tagged Proteins in Pichia pastoris

Poster Number

34

Lead Author Major

Chemistry-Biology and Pre-Pharmacy

Format

Poster Presentation

Faculty Mentor Name

Joan Lin-Cereghino

Faculty Mentor Department

Biological Sciences

Additional Faculty Mentor Name

Geoffrey Lin-Cereghino

Abstract/Artist Statement

The aim of this study was to recombinantly express Pyriform Spidroin 1 (PySp1) and Protein Kinase C (PKC1) in the yeast Pichia pastoris. PySp1 is a spider silk protein that we believe can be expressed and secreted in large amounts by Pichia pastoris for potential industrial and medical purposes. Because PKC1 is involved in intracellular signaling, the localization of PKC1 in Pichia pastoris could provide a better understanding of the ability of Pichia pastoris to super secrete. EGFP fusion proteins were quantified and analyzed by Western Blot and fluorescent microscopy.

Location

DeRosa University Center, Ballroom

Start Date

26-4-2014 2:00 PM

End Date

26-4-2014 4:00 PM

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Apr 26th, 2:00 PM Apr 26th, 4:00 PM

Expression of Fluorescently Tagged Proteins in Pichia pastoris

DeRosa University Center, Ballroom

The aim of this study was to recombinantly express Pyriform Spidroin 1 (PySp1) and Protein Kinase C (PKC1) in the yeast Pichia pastoris. PySp1 is a spider silk protein that we believe can be expressed and secreted in large amounts by Pichia pastoris for potential industrial and medical purposes. Because PKC1 is involved in intracellular signaling, the localization of PKC1 in Pichia pastoris could provide a better understanding of the ability of Pichia pastoris to super secrete. EGFP fusion proteins were quantified and analyzed by Western Blot and fluorescent microscopy.