30 results about "FHIT protein" patented technology

The present invention relates to nucleotide sequences of FHIT genes and amino acid sequences of their encoded proteins, as well as derivatives and analogs thereof, and antibodies thereto. The FHIT gene sequence is mutated in diseases involving cell overproliferation, particularly malignancies of the digestive tract. The present invention further relates to compositions of FHIT nucleic acids and a pharmaceutically acceptable carrier.

The present invention relates to nucleotide sequences of FHIT genes and amino acid sequences of their encoded proteins, as well as derivatives and analogs thereof, and antibodies thereto. The FHIT gene sequence is mutated in diseases involving cell overproliferation, particularly malignancies of the digestive tract. The present invention further relates to the use of FHIT genes and their encoded proteins as diagnostic and therapeutic reagents for the detection and treatment of disease states associated with cell overproliferation.

The present invention discloses twenty two 22 protein biomarkers of breast cancer. More specifically, the present invention discloses the identities, specificities, and uses of up to twenty two (22) protein biomarkers in blood serum for distinguishing between patients with earlier and later stages of breast cancer, patients with benign breast diseases or abnormalities, and normal individuals lacking breast abnormalities. More specifically, the present invention relates to specificities of isoforms of up to 22 protein biomarkers in blood serum for distinguishing between patients with earlier and later stages of breast cancer, patients with benign breast diseases or abnormalities, and normal individuals lacking breast abnormalities.

The present invention relates to a method for renaturating protein by adopting penetrating matter and hydrophobic chromatography combination system. Its basic process includes the following steps: adopting high-concentration salt and denaturant to gradient adsorb the denatured protein on the hydrophobic chromatographic column, then using penetrating matter with a certain concentration to make elution so as to make the protein progressively be renaturated in the course of elution, after correct folding, can obtain the natural activity protein. Said invention can obtain active protein with high concentration, and can retain high protein recovery and activity recovery.

The invention relates to a glycosylated modifying method for improving the antioxidant activity of a whey protein. The method comprises the following step of: by using xylose, glucose, fructose, lactose, maltose, saccharose and the whey protein as reaction raw materials, performing a damp and hot glycosylated reaction according to a certain proportion. The result shows that the reducing capacity of a whey protein-xylose compound, the DPPH free radical scavenging capacity, the.OH free radical scavenging capacity and the anti-lipid peroxidation capacity are improved to the maximum extent along with increase of pH. SDS-PAGE displays that the molecular weight of the whey protein-xylose compound after reaction is remarkably increased. Fourier Transform Infrared Spectroscopy (FTIR) results show that amides I and II in the whey protein-xylose compound are remarkably reduced. The method provided by the invention aims to obtain the glycosylated modifying method for the whey protein with stronger antioxidant function. The antioxidant function characteristic of the whey protein is improved, a novel functional whey protein ingredient is developed, and the application range is expanded and a novel functional additive is increased.

Protein binding assays are provided for determining IP3 in a sample employing as reagents a conjugate of IP3 joined at the 2-oxy through a bond or linking group to a detectable label and a truncated portion of the extracellular fragment of an IP3R. The reagents are combined with the sample and the amount of IP3 determined by means of the detectable label. The conjugate with the enzyme donor fragment of beta-galactosidase or a fluorescer is specifically described.

Methods are described for improvement of the serum half life of therapeutic nucleic acids by 3′ conjugation to useful target proteins, or other large molecules with useful function. In one embodiment, a 3′ A, C or G overhang is added to ds-DNA and the primary amines conjugated using biocompatible bifunctional linkers to proteins. The resulting nucleic acid-3′ conjugates are serum nuclease-resistant and retained in vivo for long periods without rapid kidney clearance. Further, the choice of conjugate imparts additional functionality to the nucleic acid-3′ conjugate.

The invention relates to the enrichment and purification of phosphopeptide in phosphoproteome, in particular to the application of ZrO2 in the enrichment and purification of phosphopeptide. ZrO2 nano material shows high specificity, selectivity, binding capacity and sensitivity at a phosphopeptide section; meanwhile, the affinity of the ZrO2 nano material to the specificity of phosphopeptide ensures that the material can be used in phosphoproteome during protein post-translational modification. Due to the specificity combination of ZrO2 with the phosphopeptide section in complex proteolysis sample, large-scale identification of phosphorylated protein and determination of phosphorylation sites can be realized through combining with MALDI-TOF MS and nano-LC MS / MS.

The invention relates to a protein fluorescence detection technology, in particular to the application of the berberine and the derivatives in the protein fluorescence detection. The invention also provides a method to apply the berberine to the protein fluorescence gel detection, and the method comprises the steps of: fixing the electrophoresis gel of the protein sample in the stationary liquid, washing by the deionized water; dyeing, washing by the deionized water; detection. The invention has the advantages of high sensitive, simple and rapid operation, good reproducibility, good dyeing background, good linear relationship, good reversibility, good compatibility, safe using and low cost, etc.

The invention relates to a protein separation and purification process method in the biological product technology, in particular to a human serum albumin separation method, comprising protein separation and purification process. The method is characterized in that the method takes plasma as raw material; first of all, composition I, composition II and composition III are respectively precipitated; then the composition I, II and III are separated together; finally compositions IV-1 and IV-4 are precipitated respectively and separated together; the solid-liquid separation uses a pressure filtration technology, with the fluid intake pressure no more than 0.2MPa. The method of the invention adopts the pressure filtration technology in the separation process, adjusts and controls the ethanol albumin concentration, temperature, pH value and other parameters in the albumin separation, and overcomes the disadvantages that the existing technology which produces human albumin through low-temperature ethanol separation has lower albumen composition yield and the unstable substances (such as lipoprotein) in the albumin composition are not completely removed. Compared with the low-temperature ethanol method, the method of the invention has high yield of albumin (not less than 2.9g / 100ml) and good product quality.

The present invention relates to a proteinaceous construct comprising a blood coagulation factor, e.g., Factor VIII (FVIII), being bound to at least one water soluble polymer, including a poly(alkylene oxide) such as polyethylene glycol (PEG). Further the present invention relates to methods of preparing PEGylated blood coagulation factor, e.g., FVIII, in the presence of bound antibodies. The invention also relates to methods for prolonging the in vivo-half-life of blood coagulation factor, e.g., FVIII, in the blood of a mammal having a bleeding disorder associated with functional defects or deficiencies of blood coagulation factor, e.g., FVIII.

The invention relates to a device for protein and / or peptide concentration, which device comprises electroconcentration means (23); at least two electrodes having a positive (7) and a negative charge (35), respectively; and protein and / or peptide capture means (17); wherein said electroconcentration means (23) comprises a funnel shaped cavity and at least one electrode is located on each side of the electroconcentration means. The invention also relates to a method for concentrating a protein and / or a peptide in a sample, which method can be performed in a device according to the invention.

The instant invention involves the use of a combination of preparatory steps in conjunction with mass spectroscopy and time-of-flight detection procedures to maximize the diversity of biopolymers which are verifiable within a particular sample. The cohort of biopolymers verified within such a sample is then viewed with reference to their ability to evidence at least one particular disease state; thereby enabling a diagnostician to gain the ability to characterize either the presence or absence of at least one disease state relative to recognition of the presence and / or the absence of the biopolymer, predict disease risk assessment, and develop therapeutic avenues against the disease.

The present invention addresses the first problem of providing an Fc-binding protein having improved stability, especially stability to heat and acid, of the Fc-binding protein, a method for producing this protein, and an antibody adsorbent using this protein. The present invention also addresses the second problem of providing a method that makes it possible to identify the presence or absence of glycosylation of an antibody, and a material to be used in this method. The first problem is solved by an Fc-binding protein having improved stability to heat and acid obtained by substituting amino acid residues at specific positions in the extracellular domain within human FcγRIIIa with other specific amino acids, a method for producing this protein, and an antibody adsorbent using this protein. The second problem is solved by using an adsorbent capable of specifically adsorbing an antibody having a sugar chain, the adsorbent being obtained by immobilizing human FcγRIIIa on an insoluble carrier.

A new protein derived from acid hydrolyzed IgG concentrate which has a molecular weight of about 55,000, and is activated by heat within the defined narrow temperature range provides resulting product that has a protective mechanism for bacterial and viral invasion of living cells.

The invention relates to proteins comprising HIV fusion inhibiting peptides, such as T-20 and / or T-1249 peptides (including, but not limited to, fragments and variants thereof), which exhibit anti-retroviral activity, fused to albumin (including, but not limited to fragments or variants of albumin). These fusion proteins exhibit extended shelf-life and / or extended or therapeutic activity.

Disclosed herein are nucleic acid sequences that encode pro-apoptotic polypeptides. Also disclosed are polypeptides encoded by these nucleic acid sequences, and antibodies, which immunospecifically-bind to the polypeptide, as well as derivatives, variants, mutants, or fragments of the aforementioned polypeptide, polynucleotide, or antibody. The invention further discloses therapeutic, diagnostic and research methods for diagnosis, treatment, and prevention of proliferative disorders and bacterial infections using the nucleic acids and proteins of the invention.

The present invention describes a methods, uses, compositions such as adhesive, sealants and coatings, scaffold material, composite material, all comprising amyloid-like materials such as fibrils, in particular those made from fruit or vegetable proteins. The amyloid-like materials impart good mechanical strength to the materials in which it is employed. Inhibition of amyloid formation is also described.

A method for the in vitro biosynthesis of proteins in native conformation which improves the technique which is well known in the art by immobilizing on the surface of an affinity matrix at discrete locations a ligand for which the protein being synthesized has an affinity and adding to the reaction mixture said affinity matrix having said immobilized ligand so that each molecule that is in the process of folding into a functional protein molecule may bind an immobilized ligand and be kept separated from other protein molecules as the folding proceeds. The technique works with either a batch method or a continuous method.

The invention provides a method for the separation and purification of two or three cellular components selected from genomic DNA, RNA and proteins from a single biological sample. The method comprises generating an aqueous solution containing the cellular components by lysing cells with a lysis solution; contacting the aqueous solution with an ion exchanger for genomic DNA and RNA to bind to the ion exchanger; collecting the flow-through which contains unbound proteins; eluting RNA from the ion exchanger; and eluting DNA from the ion exchanger. For the purification of any two of the cellular components, one of the components is not collected. The invention also provides reagent kits for carrying out the methods.

Secreted proteins as detection markers for insect vector and graft transmitted citrus disease are described. Method and kits for detecting the secreted proteins are provided.

Human colon specific gene polypeptides and DNA (RNA) encoding such polypeptides and a procedure for producing such polypeptides by recombinant techniques is disclosed. Also disclosed are methods for utilizing such polynucleotides or polypeptides as a diagnostic marker for colon cancer and as an agent to determine if colon cancer has metastasized. Also disclosed are antibodies specific to the colon specific gene polypeptides which may be used to target cancer cells and be used as part of a colon cancer vaccine. Methods of screening for agonists and antagonists for the polypeptide and therapeutic uses of the antagonists are also disclosed.

The invention belongs to the field of protein purification and relates to a purification method for a recombinant human epidermal growth factor (rhEGF). According to the purification method for the recombinant human epidermal growth factor (rhEGF), high-activity high-purity rhEGF protein is obtained through Ni Sepharose affinity chromatography, Source 15RPC reversed phase chromatography and Source 30Q ion-exchange chromatography of centrifugation supernatant containing the rhEGF in sequence. According to the purification method for the recombinant human epidermal growth factor (rhEGF), the Ni Sepharose affinity chromatography is adopted for purifying a natural structure recombinant human epidermal growth factor without containing an HIS purification tag, and the purification method for the recombinant human epidermal growth factor (rhEGF) has the advantages that the technology is simple, the activity yield is high, and the purification method for the recombinant human epidermal growth factor (rhEGF) is easy for large-scale production.

The invention provides isolated nucleic acids encoding a variety of proteins having diagnostic, preventive, therapeutic, and other uses. These nucleic and proteins are useful for diagnosis, prevention, and therapy of a number of human and other animal disorders. The invention also provides antisense nucleic acid molecules, expression vectors containing the nucleic acid molecules of the invention, host cells into which the expression vectors have been introduced, and non-human transgenic animals in which a nucleic acid molecule of the invention has been introduced or disrupted. The invention still further provides isolated polypeptides, fusion polypeptides, antigenic peptides and antibodies. Diagnostic, screening, and therapeutic methods using compositions of the invention are also provided. The nucleic acids and polypeptides of the present invention are useful as modulating agents in regulating a variety of cellular processes.

The present invention relates to methods of determining colorectal cancer status in a subject. The invention further relates to kits for determining colorectal cancer status in a subject. The invention further related to methods of identifying biomarker for determining colorectal cancer status in a subject.

The invention relates to chemical modification of proteins, and discloses a continuous pegylation reaction method for recombinant human erythropoietin (EPO). The method comprises the following steps of: performing a primary pegylation reaction on EPO molecules in a first buffer solution; and further adding PEG into a reaction liquid obtained in the primary pegylation reaction in a second buffer solution which is different from the first buffer solution for performing a secondary pegylation reaction to obtain a final reaction liquid. A reaction method of multiple buffering systems is applied, so that continuous pegylation reaction of EPO is realized, and a pegylation reaction method with high mono-substitution rate and low multi-substitution rate is established.

The present invention relates to use of an Anaplasma phagocytophilum protein APH1384 as diagnostic antigen for granulocytic anaplasmosis. The protein can remedy the drawback of missed detection of an existing diagnostic antigen P44 for granulocytic anaplasmosis, improve sensitivity of detection for granulocytic anaplasmosis, and facilitate rapid and accurate clinical diagnosis of granulocytic anaplasmosis.