G01N33/6848

METHODS OF PREPARING SAMPLES FOR PROTEOMIC ANALYSIS

Provided herein are methods of preparing a protein sample for proteomic analysis. In exemplary embodiments, the method comprises (a) contacting a blood sample comprising proteins with a protective agent comprising an anticoagulant (AC) and an aldehyde releaser (AR), to obtain a mixture, optionally, wherein the blood sample is added to a blood collection tube (BCT) comprising the protective agent, and (b) isolating a fraction comprising proteins or a source of proteins from the mixture to yield a protein sample or a source of a protein sample, wherein steps of the method are carried out in the absence of exogenous proteolytic enzyme inhibitors, wherein the protein sample is suitable for proteomic and peptidomic analysis.

METHOD OF PROCESSING A BIOLOGICAL SAMPLE

A method of processing of a biological sample containing multiple metabolites is described The method comprising the steps of pre-treating the biological sample with a metabolite extraction solvent to provide a pre-treated sample, separating a first aliquot of the pre-treated sample by reverse phase liquid chromatography (RPLC) to provide a first eluent containing resolved hydrophobic metabolites, and separating a second aliquot of the pre-treated sample by hydrophilic interaction liquid interaction chromatography (HILIC) to provide a second eluent containing resolved hydrophilic metabolites. The first and second eluents are assayed using targeted tandem mass spectroscopy operated in multiple reaction monitoring mode. Each liquid chromatography step(LC) is directly hyphenated with the tandem mass spectrometry (MS/MS) into a single LC-MS/MS analysis. The extraction solvent typically comprises methanol, isopropanol and an acetate buffer.

Method to analyze compounds in biological samples

Various embodiments of the present disclosure relate to a method for analyzing target compounds from a fluid or dried biological sample by using a microfluidic sample device including a hollow cartridge and an absorbent body unit.

APTAMER BASED AFFINITY CAPTURE METHODS FOR THE SELECTIVE ENRICHMENT OF HUMAN IMMUNOGLOBULIN FC DOMAINS

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 .Math.M to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

Systems and Methods for Assaying Large Molecules with Improved Sensitivity
20230296620 · 2023-09-21 · ·

The present application relates to systems and methods for assaying presence of large molecule analytes, such as proteins, e.g., antibodies, antigens, receptors, and the like, using a targeted two-dimensional liquid chromatography, tandem mass spectrometry (2D-LC-MS/MS) system, optionally combined with affinity capture. In some aspects, the system is partially or fully automated. In some aspects, the system may allow detection of protein biomarkers (e.g., antibodies or antigens) from clinical or nonclinical biological tissue or fluid samples in the pg/mL to ng/mL range.

EGG DETERMINING METHOD AND DEVICE

The present invention relates to a method for determining a characteristic of one or more eggs in an automated manner, comprising the steps of: a. extracting a sample from one or more eggs in an automated manner; i. holding and transferring the sample through one or more instruments to a unit for holding one or more samples; ii. ejecting an aliquot from the sample by applying sound or light energy to at least an amount of the sample; iii. entraining the ejected aliquot in a gas or liquid stream; and iv. transporting the ejected aliquot to a mass spectrometer using the gas or liquid stream; and b. analyzing the sample or an aliquot thereof in an automated manner in a mass spectrometer for the absence or presence and the amount of one or more molecules, to determine one or more characteristics of the egg.

NANOTIP ION SOURCES AND METHODS

The present disclosure generally relates in certain embodiments to the creation of ionized molecules, e.g., for detection in a mass spectrometer, or for other uses such as lithography, sputtering machines, propulsion etc. Some embodiments include an ion source comprising a capillary tip that may allow for direct ion evaporation of samples with an applied electric field. In some cases, the tip may have an opening with a cross-section less than 100 nm. In addition, certain aspects are directed to using a capillary tip that allow for detection of samples (e.g. amino acids), and in some cases allows for sequencing. For instance, some embodiments are directed to allowing single ions and ionic clusters to be evaporated at a high rate directly from aqueous samples in a mass spectrometer. Other aspects are directed to methods for making or using such ionized molecules, methods for making or using devices to create such ionized molecules, or the like.

BARCODED XTEN POLYPEPTIDES AND COMPOSITIONS THEREOF, AND METHODS FOR MAKING AND USING THE SAME

Disclosed herein are polypeptides comprising an extended recombinant polypeptide (XTEN) comprised of a plurality of overlapping sequence motifs and one or more barcode fragments releasable upon protease digestion and detectable from ail other proteolytic-ally releasable fragments. Certain embodiments of these polypeptides further comprise a biologically active polypeptide, wherein advantageous embodiments thereof comprise a releasable segment capable of proteolytic cleavage that cleaves the linkage between the XTEN polypeptide and the biologically active polypeptide. Methods of making and methods of using said polypeptides are also disclosed.

METHOD FOR MEASURING PHARMACOKINETICS OF AGENT LABELED WITH NON-RADIOACTIVE SUBSTANCE
20230296612 · 2023-09-21 ·

The present invention provides a method for labeling an agent, the method comprising: (i) a step of chelating a non-radioactive substance by a chelating agent having a reactive group, and (ii) a step of binding the chelating agent that chelated the non-radioactive substance in step (i) to the agent via the reactive group, the method being for use in the evaluation of pharmacokinetics, and the like.

Method for analyzing microorganism
11774448 · 2023-10-03 · ·

[OBJECT] To enable accurate identification of a specific serotype of Salmonella bacteria in a method for analyzing a microorganism using a MALDI-MS. [MEANS FOR SOLVING PROBLEM] The present invention is a method for analyzing a microorganism including an identification step for determining which of Abony and Pakistan which are two serotypes of Salmonella bacteria is contained in a sample which contains either Abony or Pakistan, based on the presence or absence of a peak (or peaks) at a predetermined mass-to-charge ratio (or ratios) in a mass spectrum obtained by a mass spectrometric analysis of the sample, or a method for analyzing a microorganism including an identification step for determining which of Minnesota. Infantis and Brandenburg which are three serotypes of Salmonella bacteria is contained in a sample which contains Minnesota. Infantis or Brandenburg, based on the presence or absence of a peak (or peaks) at a predetermined mass-to-charge ratio (or ratios) in a mass spectrum obtained by a mass spectrometric analysis of the sample, or a method for analyzing a microorganism including an identification step for determining which of Schwarzengrund and Montevideo which are two serotypes of Salmonella bacteria is contained in a sample which contains either Schwarzengrund or Montevideo, based on the presence or absence of a peak (or peaks) at a predetermined mass-to-charge ratio (or ratios) in a mass spectrum obtained by a mass spectrometric analysis of the sample.