Protein Digest

When plants react to changing hormonal or environmental conditions, the protein composition in their cells change. Post-translational modifications of proteins will also change. For example, ubiquitination seems to be an important part of plant response to stress.1 For proteomic studies or amino acid sequencing, proteins must be reproducibly fragmented into peptides. Two different limit digests are often needed to allow the primary structure to be deduced from overlapping peptide sequences. Trysin, a serine endoproteinase, normally provides one set of peptides. It cleaves carboxy-terminal to arginine and lysine. Other peptide sets are obtained by cyanogen bromide treatment that splits proteins after methionine, or by digestion with endoproteinases of different specificity. In addition to our sequencing grade trypsin, we offer four highly purified endoproteinases with different cleavage site specificities, including glu-X or asp-X. Most can be used for in-gel digestion, convenient when comparing 2-D gels. Our Trypsin Profile IGD kit contains all the necessary reagents for preparing peptides ready for MALDI-MS. Excised gel-spots are destained, treated with proteomics grade typsin, and the resultant peptides are extracted into the appropriate solvents.

1.Li-Rong Zeng, Miguel E Vega-Sánchez, Tong Zhu and Guo-Liang Wang. Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions. Cell Research (2006) 16: 413–426

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P6056 Endoproteinase Arg-C from mouse submaxillary gland suitable for protein sequencing, lyophilized powder
P3303 Endoproteinase Asp-N from Pseudomonas fragi mutant strain suitable for protein sequencing, lyophilized powder
P6181 Endoproteinase Glu-C from Staphylococcus aureus V8 suitable for protein sequencing, lyophilized powder
EMS0004 SOLu-Trypsin recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid
T6567 Trypsin from porcine pancreas Proteomics Grade, BioReagent, Dimethylated
PP0100 Trypsin Profile IGD Kit