Dedicated LCMSMS protein modification characterization, protein structure phi analysis and disulfide validation

Martin-Protean LLC is a contract research organization dedicated to performing the most challenging liquid chromatography tandem mass spectrometry analyses of complex peptide mixtures.  Our focused capability enables highly competitive offerings for three sought after services:  quantitative characterization of chemically modified protein ensembles including antibodies; protein structure phi analyses and biologic disulfide validation.  We are known for responsive customer service, our careful and thorough analyses and our commitment to working with clients (see some below) to get them the data they need.

                                        
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chemically modified protein analysis

Chemically modified proteins are ubiquitous reagents in life science discovery.  While these proteins are generally used without characterization this practice produces confounding factors that limit the probity of experimental results.  Whether your SPR data that does not produce a satisfying fit to the simple 1:1 stoichiometry that you think is correct or it is the punctate antibody fluorescence in the endoplasmic reticulum that you expected to see only on the golgi, uncharacterized chemically modified proteins can be largely responsible. Let Martin-Protean characterize these reagents, and improve your ability to perform and analyze experiments with them.

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protein structure phi value analysis

Probing protein structure by measuring differential intrinsic rates of reactivity to chemical probes at different amino acid residues is used to elucidate the folding pathways of proteins of interest.  The extensive expertise in understanding protein structure, the chemical modification of proteins, and LCMSMS  analysis of chemically modified proteins makes Martin-Protean the goto CRO for comprehensive, sensitive LCMSMS readout of all your phi value analysis experiments.

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biologic disulfide validation

Developing a unique biologic can involve extended periods of uncertainty regarding your molecular entity's conforming to design specifications. A powerful and robust method for insuring that your expression/post-translational modification/mutation change still produces the properly folded protein is to confirm that the protein still retains its native disulfides at native levels of occupancy. The Martin-Protein expertise in protein processing for LCMSMS, protein fragmentation and crosslinked peptide assignments has made us the leader in identifying even double disulfide tripeptides from LCMSMS fragmentation spectra.

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