Abstract: An indicator system comprising permanganate, an organic reducing agent, an acid, and optionally an inorganic salt is provided herein, as well as methods for using the indicator system for monitoring the integrity of a biospecimen are provided herein.

Abstract: The present disclosure relates to methods of using plasma and serum (P/S) glycomics based on glycan linkage analysis that captures unique glycan features such as ?2-6 sialylation, ?1-6 branching, and core fucosylation as single analytical signals to evaluate the behavior of P/S glycans in all stages of lung cancer and across various stages of bladder, prostate, ovarian, and pancreatic cancer.

Abstract: The present disclosure provides a method for analyzing glyeart-derived monosaccharides in a sample. The present disclosure also provides a method for detecting or monitoring a disease or disorder in a patient. In addition, the present disclosure provides a method of determining aberrant glycotransferase activity. The present disclosure further provides a system for analyzing or comparing glycates in a sample.

Abstract: Methods for quantifying biospecimen sample integrity using markers of oxidation (FIG. 1). Under conditions of incomplete blood plasma/serum (P IS) sample freezing (including storage at ?20 ?C), two different forms of oxidation occur spontaneously at protein sulfur atoms—namely S-cysteinylation of free cysteine residues (in which the oxidative event is disulfide bond formation) and sulfoxidation of methionine. Oxidized forms of albumin and apoA-1, SCA and MOA1 are useful markers of biospecimen integrity. The oxidative chemistries of SCA and MOAI are operational in other proteins and polypeptides. Thus, for rare cases in which the use of SCA or MOA1 may be contraindicated, custom designed surrogate peptide probes based on SCA and MOA1 oxidation chemistry may be fortified into samples at collection to serve as exogenous markers of P/S sample integrity.

Abstract: Methods for quantifying biospecimen sample integrity using oxidation. Embodiments include assessing ex vivo oxidation of a biospecimen sample by quantifying a difference in protein oxidation of the biospecimen sample in comparison to protein oxidation of a portion of the biospecimen sample intentionally incubated to cause oxidation to hit its maximum value. The difference in a level of oxidation in the biospecimen sample and the portion of the biospecimen sample is then inversely proportional to the degree of ex vivo oxidation.

Abstract: Methods for quantifying biospecimen sample integrity using oxidation. Embodiments include assessing ex vivo oxidation of a biospecimen sample by quantifying a difference in protein oxidation of the biospecimen sample in comparison to protein oxidation of a portion of the biospecimen sample intentionally incubated to cause oxidation to hit its maximum value. The difference in a level of oxidation in the biospecimen sample and the potion of the biospecimen sample is then inversely proportional to the degree of ex vivo oxidation.

Abstract: Methods for quantifying biospecimen sample integrity using markers of oxidation (FIG. 1). Under conditions of incomplete blood plasma/serum (P IS) sample freezing (including storage at ?20 ?C), two different forms of oxidation occur spontaneously at protein sulfur atoms—namely S-cysteinylation of free cysteine residues (in which the oxidative event is disulfide bond formation) and sulfoxidation of methionine. Oxidized forms of albumin and apoA-1, SCA and MOA1 are useful markers of biospecimen integrity. The oxidative chemistries of SCA and MOAI are operational in other proteins and polypeptides. Thus, for rare cases in which the use of SCA or MOA1 may be contraindicated, custom designed surrogate peptide probes based on SCA and MOA1 oxidation chemistry may be fortified into samples at collection to serve as exogenous markers of P/S sample integrity.

Abstract: The present disclosure provides a method for analyzing glycan-derived monosaccharides in a sample. The present disclosure also provides a method for detecting or monitoring a disease or disorder in a patient. In addition, the present disclosure provides a method of determining aberrant glycotransferase activity. The present disclosure further provides a system for analyzing or comparing glycates in a sample.

Abstract: Methods and systems for detecting and quantifying signal peaks from ESI-TOF-MS data may include creating a signal model and a noise model for mass spectrometry (MS) data. The method may also include detecting a signal peak based, at least in part, on the signal model and the noise model for the MS data. The method may further include determining an amplitude of the detected signal peak based, at least in part, on the signal model and the noise model for the MS data.

Abstract: The present invention provides reagents and methods for limiting adsorptive and/or oxidative protein losses in a sample.