PROTEOMICS
Protein expression, purification, and proteomics core
- Biophysical characterization of purified proteins
- Construction of fusion tagged proteins either chromosomal or using exogenous plasmid vectors.
- Affinity purification using protein specific antibody or epitope tags fused with bait proteins of interest to identify interacting partners through mass spectrometry
- Offer range of chromatography separation techniques:
- Affinity Chromatography
- Ion Exchange Chromatography
- Size Exclusion Chromatography
- Hydrophobic Interaction Chromatography
- Reversed Phase Chromatography
- Sample preparation (desalting, digestion, and fractionation)
- Custom packed LC column services (based on the user needs) for any chromatography separation type and dimension.
- Determination of intact proteins and protein identification from silver-stain or SDS-PAGE gels.
- Protein identification in complex mixtures using a combination of easy Nano-LC and high-resolution mass spectrometer workflow.
- Relative protein quantification based on label-fee, SILAC, or iTRAQ
- Identification and quantification of proteins, peptides, and post-translational modifications (through TiO2 and IMAC).
- Mass spectrometry based proteomics and bioinformatics analysis (to identify reliable interacting proteins using database search engines) includes:
- SEQUEST
- STATQUEST
- MaxQuant
- Xtandem!
- MS-GF+
- and other data-processing and analysis tools such as Proteome Discoverer and Scaffold.
- For the protein interactions studies, the report will include scores assigned to each interacting protein pair to emphasize the significance and reliability of the interactions using algorithms such as
- purification enrichment score
- hypergeometric distribution
- COMPASS
- SAINT among others.