Author
SCHULLER, SIMONE - University College Dublin | |
SERGEANT, KJELL - Luxembourg Institute Of Science & Technology | |
RENAUT, JENNY - Luxembourg Institute Of Science & Technology | |
CALLANAN, JOHN - University College - Ireland | |
SCAIFE, CAITRIONA - University College - Ireland | |
Nally, Jarlath |
Submitted to: Data in Brief
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 4/13/2015 Publication Date: 5/27/2015 Citation: Schuller, S., Sergeant, K., Renaut, J., Callanan, J.J., Scaife, C., Nally, J.E. 2015. A 2-D guinea pig lung proteome map. Data in Brief. 4:140-145. DOI: 10.1016/j.dib.2015.04.009. Interpretive Summary: The guinea pig (Cavia porcellus) is an important experimental laboratory animal model of infection. The recent completion of the complete genome allows for the use of a range of additional experimental tools including gel based proteomics to study pathogenic mechanisms of disease. In this study, the tools of proteomics were used to create and characterize a 2-dimensional gel proteomic map of lung tissue from guinea pigs comprising 486 protein identifications and post translational modifications. Results provide a framework for future proteomic research applications on guinea pig lung tissue. Technical Abstract: Guinea pigs represent an important model for a number of infectious and non-infectious pulmonary diseases. The guinea pig genome has recently been sequenced to full coverage, opening up new research avenues using genomics, transcriptomics and proteomics techniques in this species. In order to further annotate the guinea pig genome and to facilitate future pulmonary proteomics in this species we constructed a 2-D guinea pig proteome map including 486 protein identifications and post translational modifications (PTMs). The map has been up-loaded to the UCD 2D-PAGE open access database (http://proteomics-portal.ucd.ie/). Transit peptides, N-terminal acetylations and other PTMs are available via Peptideatlas (ftp://PASS00619:NM455hi@ftp.peptideatlas.org/)). This dataset is associated with a research article published in the Journal of Proteomics. |