51 results about "Proteome profiling" patented technology

Full-length cDNAs of plants and their uses are provided. Source plants are preferably monocot plants, more preferably poaceous plants, and most preferably rice. Vectors carrying said cDNAs and transformants containing said cDNAs or said vectors, transgenic plants containing said transformants, polypeptides encoded by said cDNAs are also provided. The full-length cDNA clones play important roles in the annotation of correct gene coding region, determination of exons and introns, comprehensive expression analysis on the transcription level and proteome analysis. Furthermore, full-length cDNA clones are industrially useful in producing plants having different properties from those of the wild type due to the inhibition of expression and functional suppression in plant bodies.

The present invention relates to phosphate-binding compounds that find use in binding, detecting and isolating phosphorylated target molecules including the subsequent identification of target molecules that interact with phosphorylated target molecules or molecules capable of being phosphorylated. A binding solution is provide that comprises a phosphate-binding compound, an acid and a metal ion wherein the metal ion simultaneously interacts with an exposed phosphate group on a target molecule and the metal chelating moiety of the phosphate-binding compound forming a bridge between the phosphate-binding compound and a phosphorylated target molecule resulting in a ternary complex. The binding solution of the present invention finds use in binding and detecting immobilized and solubilized phosphorylated target molecules, isolation of phosphorylated target molecules from a complex mixture and aiding in proteomic analysis wherein kinase and phosphatase substrates and enzymes can be identified.

The present invention is directed to a biochemical assay for simultaneous genomic and proteomic analysis.

A method for the detection of an early biomarker for assessing a change in renal status in a mammalian subject following a renal event. The method typically includes the steps of (a) providing a body fluid sample obtained from a mammalian subject; (b) analyzing the molecular weight of the proteins in the sample using proteome analysis; and (c) identifying the presence of a protein in the sample selected from the group consisting of a 6.4 kDa protein, a 28.5 kDa protein, a 33 kDa protein, a 44 kDa protein, a 67 kDa protein, and combinations thereof. The presence of one of these proteins can serve as an early biomarker for assessing a change in renal status. The levels of these proteins can be compared to predetermined levels, and thus provide a determination of the subject's renal status. The invention also includes a method of assessing the administration of aprotinin during cardio-pulmonary bypass surgery and provides for methods where the level of the 6.4 kDa biomarker in the subject's urine directs a caregiver's therapeutic decision regarding the intra-operative administration of aprotinin.

The present invention provides a library of membrane protein-embedded liposomes suitable for proteome analysis, a method for preparing same and a proteome analysis method using same.

The present invention is directed to a high throughput method for producing a large number of different antibodies, more specifically organized antibody microarrays. These antibodies and antibody microarrays can be used to rapidly assay protein abundance and identify types of proteins that are expressed in cells and tissues under a variety of conditions, or to compare protein expression profiles of different cells.

The invention provides methods for identifying a polypeptide. The method can include determining two or more characteristics associated with the polypeptide, or a fragment thereof, one of the characteristics being mass of a fragment of the polypeptide, the fragment mass being determined by mass spectrometry; comparing the characteristics associated with the polypeptide to an annotated polypeptide index; and identifying one or more polypeptides in the annotated polypeptide index having the characteristics. The method can further include the steps of determining one or more additional characteristics associated with the polypeptide; comparing the determined characteristics to the annotated polypeptide index; optionally repeating the steps one or more times, wherein a set of characteristics is determined that identifies a single polypeptide in the annotated polypeptide index, and optionally quantitating the amount of identified polypeptide in a sample containing the polypeptide. The invention also provides methods for generating a polypeptide identification index.

Provided herein is a system and method for analyzing microarray data (transcriptome profiles), metabolite data (metabolome profiles), protein level data (proteome profiles), or any combination thereof to determine the biochemical pathways affected by a treatment. The system and method can be used to generate biochemical pathway information for any organism for which metabolic profile data can be obtained. The system and method may allow users to query the pathways generated and to filter the results of queries based on the -omic profile data, pathways involving molecules of interest, notions of biochemical importance, milestone molecules, and other factors. The system and method may also be suitable for discovery of regulatory sequences in genes. In an exemplary use, the system and method can be utilized to identify three genes involved in “de novo” ammonia “biosynthesis” that are induced by light, and was able to identify a putative cis-element, GWTTGTGG, that is likely involved in the regulation of those genes.

The present invention intends to provide a high sensitivity method for identifying the type of a protein contained in each cell with a diameter of ten to several tens μm and a sample treatment solution required for it. The above is achieved by three steps of (1) treating a slice of a diseased tissue with an aqueous solution containing gold particles and a digestive enzyme, and digesting restrictively a protein of interest, (2) measuring a 2-dimensional distribution of fragmented peptides by TOF-SIMS, and (3) visualizing a 2-dimensional distribution of the target protein in the slice of the diseased tissue using the results of the proteome analysis and by means of a numerical analysis.

Disclosed are: a marker for the diagnosis of a liver disease, which can determine the disease in a simple manner; an antibody directed against the marker; a diagnostic agent; a diagnosis method; and a method for marker detection in blood or serum. Proteome analysis revealed that quantities of the full-length kininogen and three partial peptides thereof (sequence A: position-440 to position-456, sequence B: position-439 to position-456, and sequence C: position-438 to position-456) in sera of patients with non-alcoholic fatty liver disease are significantly different from those in sera of healthy individuals; and a diagnostic agent and a detecting method for the non-alcoholic fatty liver disease that can be conveniently used for medical examination are established. The use of a combination of a kininogen-based marker and a C4-based marker (the full length sequence or partial peptides thereof) enables identification of chronic hepatitis and an asymptomatic virus carrier, as well as non-alcoholic fatty liver disease.

This invention refers to a new method for optimizing the composition of cell culture media. This new method comprises two main stages. In the first stage, a functional enviromics map is built through the joint screening of cell functions and medium factors by the execution of a specific cell culture protocol and exometabolome assays protocol. The functional enviromics map consists of a data array of intensity values of elementary cellular functions against medium factors. In the second stage, optimized cell culture medium formulations are developed that either enhance or repress target elementary cellular functions from columns of the functional enviromics map. The main advantage of this method lies in enabling metabolic engineering through the culture media composition manipulation, wherein an arbitrarily high number of cell functions are optimized through manipulation of medium factors, as opposed to previous methods, which are eminently empirical, are not cell function oriented, and require a much higher number of experiments. Furthermore, this new method is based on cost-effective exometabolome assays and does not require costly intracellular genomic or proteomic assays.

The invention relates to a sample preparation method for proteomic analysis. Specifically, the method comprises the following steps: reducing and alkylating proteins in a sample to be detected, addingacetone to precipitate the reduced and alkylated proteins, redissolving the proteins, adding the redissolved protein solution to a 96-well plate with a PVDF membrane, and carrying out enzymolysis onthe 96-well plate with the PVDF membrane. The sample obtained according to the method of the invention can be used for proteome analysis.

This invention also relates to protein dactylography method for analyzing for the protein group got by retention chromatography. This method adopts mass spectroscopy to distinguish and detect protein group. The analysis data takes the form of bar code (protein dactylography) read by computer. This invention method is used to detect the protein fingerprint in the normal cell, restocarcinoma patient cell and rectal polyp patient cell.

The invention provides a method for quantifying a trace amount of biological sample proteome by utilizing an isotope labeling technology. An accompanying sample is designed for a target sample, the accompanying sample is marked again, protein detection loss is transferred to the accompanying sample, detection of trace amount of biological sample protein is achieved, the technical obstacles existing in proteome analysis of trace amount of biological samples in the prior art are overcome, and practical information capable of being used for identification or quantification is obtained.

Proteins specific for prostate epithelial cells, normal or neoplastic, are identified and used for diagnosis, development of antibodies, and for evaluating drugs that react with the neoplastic specific proteins. Affinity based probes are used that react specifically with the active site to provide a measure of the enzyme activity of the cells. Prostate epithelial neoplastic cells can be used in screening candidate drugs for their effect in changing the proteome profile as to the serine-threonine hydrolase enzymes, using the affinity based probes for determining the profile.