The present invention includes a method for analyzing reactions. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The solution further includes at least one controller chemical that affects the reaction between the donor chemical and the acceptor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The donor chemical includes a functional group selected from ester, anhydride, imide, acyl halide, and amide. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Yet another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. An additional analytical method is also used to measure either the acceptor product or the donor chemical.

A mass spectrometry-based method for analyzing an acidic organic target compound includes directing a charged solvent (44) toward a pre-acidified sample (12) comprising the target compound, to thereby ionize the pre-acidified sample (12). The method further includes directing the ionized pre-acidified sample (54) to a mass spectrometer (18), the mass spectrometer (18) being configured to identify and quantify the target compound.

A method and apparatus for collecting signals and a method and apparatus for tracking cells by using light sensitive chip, relate to the technical field of signal collection, wherein the method for collecting signals by using light sensitive chip comprises closely fitting a luminous surface of a membrane carrying optical signals to be collected on a light sensitive chip (101), placing the light sensitive chip fitted with the membrane carrying optical signals to be collected in a dark room (102), collecting optical signals (103) by the light sensitive chip in the dark room, and processing and outputting the collected optical signals (104). The method and apparatus for collecting signals by using the light sensitive chip can collect signals by contacting the light sensitive chip to convert optical signals into digital signals so as to complete quantitative analysis.

Disclosed are methods and systems for the quantification of AngI and/or determination of plasma renin activity in a sample. The methods and systems disclosed herein can be useful for diagnosis of hypertension, aldosteronism and other abnormalities of the renin angiotensin aldosterone system (RAAS).

The present invention relates to methods and products associated with in vivo enzyme profiling. In particular, the invention relates to methods of in vivo processing of exogenous molecules followed by detection of signature molecules as representative of the presence of active enzymes associated with diseases or conditions. The invention also relates to products, kits, and databases for use in the methods of the invention.

A mass-spectrometry-based method and substrates are provided herein for large scale kinome activity profiling directly from crude lysates using 90 chemically synthesized peptide substrates with amino acid sequences derived from known phosphoproteins. Quantification of peptide phosphorylation rates was achieved via the use of stable isotope labeled synthetic peptides. Half of these peptides immediately or rapidly showed robust and site-specific phosphorylation after incubation with serum-starved HEK293 cell lysate. A method and substrates for obtaining 90 simultaneous activity measurements in a single-reaction format were developed and validated. Activating kinase pathways through insulin or EGF stimulation reproducibly altered the phosphorylation rates of peptides derived from known pathway protein substrates. While examining cell-cycle-specific activities with the panel, a peptide derived from phosphoinositide 3-kinase regulatory subunit demonstrated mitotic and tyrosine-specific phosphorylation, which was confirmed to be a Src kinase site in vivo. The kinome activity profiling strategy was successfully applied with lysates of each of: cells manipulated by various combination of mitogen stimulation, pharmacological perturbation and siRNA-directed kinase knockdown; seven different breast cancer cell lines treated with gefitinib; and each of normal and cancerous tissue samples from renal cell carcinoma patients. This method concurrently measures multiple peptide phosphorylation rates to provide a diagnostic fingerprint pattern for activated kinases, protein phosphatases, modulators of these enzymes, and pathways (kinome) from as little starting material as a few cells.

The invention provides a carrier and a method for obtaining, removing, or detecting extracellular membrane vesicle or virus present in a sample. In particular, the invention provides (a) a carrier (a Tim carrier) on which a protein (a Tim protein), selected from a T-cell immunoglobulin and mucin domain-containing molecule-4 (a Tim-4) protein, a Tim-3 protein, and a Tim-1 protein, is bound; (b) a method for obtaining the extracellular membrane vesicle or the virus in the sample; (c) a method for removing the extracellular membrane vesicle or the virus in the sample; (d) a method for detecting the extracellular membrane vesicle or the virus in the sample; (e) a kit for capturing the extracellular membrane vesicle or the virus, comprising the Tim carrier; and f) a kit for capturing the extracellular membrane vesicle or the virus, comprising a reagent containing the Tim protein and a reagent containing the carrier.

Compositions, kits, and methods are disclosed for determining one or more target polypeptides in a sample where the target polypeptides have undergone a post-translational modification. The compositions can include a first reagent including a cleavage-inducing moiety and a first binding agent for a binding site that includes a post-translational modification of a target polypeptide.

In one aspect, the invention provides a protein capture membrane comprising a first side and a second side and a plurality of interstices extending contiguously from the first side to the second side, wherein the interstices are coated with a protein-reactive coating; and the porous substrate comprises nanoporous alumina or porous glass. In another aspect the invention provides a method of detecting a protein of interest in a plurality of proteins.

A method for analyzing macromolecules, including peptides, polypeptides, and proteins, employing nucleic acid encoding is disclosed.