32 results about "Agrin" patented technology

The invention relates to the field of protein chips, in particular to a protein chip for detecting a sugar chain abnormal IgA kidney disease. The protein chip is prepared by fixing lectin on a solid vector and using a marked second antibody to be combined with IgA in a detection sample, wherein the lectin is selected from snail lectin or vicia villosa lectin. The protein chip provided by the invention is specifically combined with special sugar chain protein by using the lectin so as to diagnose the disease, thereby providing a new way for the diagnose of the disease. The method is simple and practicable, the cost is low, the operation steps are simplified, the detection time is shortened, and the method is a novel method which is appropriate to generalize.

The invention provides a lectin chip for detecting carbohydrate chain markers based on protein in blood serum or saliva as well as a kit and application of the lectin chip, relates to the lectin chip for detecting the carbohydrate chain markers in blood serum or saliva, and particularly relates to the lectin chip for detecting the carbohydrate chain markers based on protein in blood serum and saliva as well as a kit and application of the lectin chip. The invention aims at providing a non-injury lectin chip for detecting the carbohydrate chain markers by identifying protein in saliva or blood serum and a method thereof. The lectin chip for detecting the carbohydrate chain markers based on serum carbohydrate binding protein, provided by the invention, comprises a testing lectin probe set, wherein the testing lectin probe set at least comprises PTL-I, PNA, AAL, LTL, STL, BS-I, PTL-II, SBA, ACA, UEA-I, MAL-I and PHA-E+L. The lectin chip can be used for rapidly detecting a specific carbohydrate protein chain structure in blood serum and saliva samples, and rapidly judging the specific combination of carbohydrate chains in the samples, so as to determine whether corresponding people have hepatitis or not and determine whether people are ACHBLF patients or not.

Co-incubation of an amyloid protein with sulfated macromolecules as a method for the formation of amyloid plaques. The amyloid protein may be the beta-amyloid protein or the prion protein or the like. Amyoid plaque formation in one embodiment proceeds in vitro and desireably produces amyloid plaques that stain with Congo red and demonstrate a maltese-cross pattern when viewed under polarized light. The method also produces amyloid plaques that demonstrate an "amyloid star" appearance when viewed by transmission electron microscopy. Sulfated macromolecules include a sulfated proteoglycan selected from the group consisting of perlecan, ~220 kilodalton heparan sulfate proteoglyean, glypican, cerebroglycan, aggrecan, synaptoglycan (SV2PG), syndecan, N-syndecan (also known as syndecan-3), syndecan-1, syndecan-4, neurocan, phosphacan, decorin, biglycan, versican, amphiglycan, lumican, PG-M, PG-M (3), agrin, betaglycan, claustrin, brevican, appican, epican, neuroglycan-C, and fragments thereof. Thw sulfated macromolecule may be a sulfated glycosaminoglycan selected from the group consisting of heparin, heparan sulfate, dermatan sulfate, chondroitin sulfate, keratan sulfate, and fragments thereof. An in vivo assay is also presented for selecting a candidate therapeutic agent for inhibiting or disrupting amyloid plaque deposition or persistence. The assay includes a) pre-forming congophilic maltese-cross amyloid plaques in vitro following incubation of an amyloid protein and a selected sulfated macromolecule, b) using a first cannula and osmotic pump to continuously infuse for a selected duration the pre-formed congophilic maltese-cross amyloid plaques into a tissue or organ, c) changing the first cannulae and osmotic pump with a second cannulae and osmotic pump to administer the candidate therapeutic, and d) detecting the candidate therapeutic's ability to disrupt, reduce, or eliminate congophilic maltese-cross amyloid plaque deposition / persistence in the tissue or organ.

The invention belongs to the technical field of biology, and discloses a diagnostic composition for neurotransmission disorder diseases by utilizing agrin. The diagnostic composition comprises agrin or agrin mimic epitope. The composition can be used for diagnosing neurotransmission disorder diseases, and has an excellent effect and wide market prospects.

The invention relates to amphioxus agglutinoid and expressed genes and application thereof. An expressed gene nucleotide sequence of the amphioxus agglutinoid AmphiITLN239631 is shown as SEQ ID NO.1. An amino acid sequence of the amphioxus agglutinoid AmphiITLN239631 is shown as SEQ ID NO.2. The amphioxus agglutinoid AmphiITLN239631 can be combined with polysaccharide to prepare a bacteria- polysaccharide- agglutinoid recognized chip and provides theory basis for quick identification and prevention treatment of mariculture diseases caused by bacterial infection.

The current invention involves the use of protein lectins produced by plants including the non-toxic carbohydrate binding subunits (B subunits) of plant “AB toxins” (PTB lectins) as delivery vehicles for mobilizing associated drug substances for delivery to animal and human cells. The resulting protein fusions or conjugates retain lectin carbohydrate specificity for binding to cells and cellular trafficking activity so as to deliver an associated drug compound to the site of disease manifestation. One embodiment of this invention concerns the ability of ricin toxin B subunit, as a model PTB lectin, to deliver enzyme replacement therapeutic drugs to cells of several organs of the body including the brain and central nervous system, eyes, ears, lungs, bone, heart, kidney, liver, and spleen for treating lysosomal diseases.

The invention provides a purified renaturation method of L-aspartic acid oxidase inclusion bodies. The purified renaturation method comprises the following steps that precipitates of the inclusion bodies are collected, and fully washed, denatured proteins are purified by a nickel column, the purified denatured proteins are diluted with a buffer solution D until the protein concentration is lower than 1mg / ml, and placed in a dialysis buffer solution, the dialysis temperature is kept at 4 DEG C, dialysis lasts for more than 12 hours, and supernatants are centrifugally collected. Finally, the supernatants are concentrated by an ultrafiltration tube, and then monomeric proteins and agrin are purified and separated by a molecular sieve to obtain homogeneous natural active proteins. The purified renaturation method of the L-aspartic acid oxidase inclusion bodies disclosed by the invention solves the problem of L-aspartic acid oxidase renaturation, purification and renaturation on the L-aspartic acid oxidase inclusion bodies are carried out with a convenient and fast method, the inclusion bodies are further rinsed and purified by the nickel column to obtain the denatured proteins with higher purity, denaturants are removed gradually through a one-step dialysis renaturation process, the proteins are folded to be protein molecules with activity, the renaturation efficiency of the proteins is not less than10%, and then the protein molecules are further dialyzed and purified by the molecular sieve to obtain high-purity enzymes with activity.

The invention provides a method for raising alpha galactosidase activity, which comprises the following steps: connecting an alpha galactosidase gene (Genbank number: X03102) with a N terminus of a saccharomyces cerevisiae cell wall constituents alpha lectin sequence (Genbank number:M28164), then inserting a C terminus of downstream MFalphal1 signal peptide sequence (Genbank number:M17301) of a saccharomyces cerevisiae expression vector GAL1 promotor (Genbank number:AY428072), constructing an expression cassette, wherein the expression cassette is from the N terminus to the C terminus: the GAL1 promoter, a MF alpha1 signal peptide sequence, the alpha galactosidase gene, the alpha lectin sequence; converting a cerevisiae plasmid containing the expression cassette to the saccharomyces cerevisiae cell. The invention has the advantages that the alpha galactosidase is expressed out of an external surface of the saccharomyces cerevisiae cell wall so that a total contact of enzyme and an extracellular substrate can be realized, therefore the alpha galactosidase activity can be obviously improved.

The invention discloses an application of Matriptase. The Matriptase comprises a short intracellular segment, a transmembrane region, an SEA (sea urchin sperm protein, enteropeptidase, agrin domain) region, two CUB (Cls / Clr, urchin embryonic growth factor and bone morphogenetic protein-1) regions, four low density lipoprotein acceptor domains and a C-terminal trypsin-like protease region. The Matriptase is applied to diagnosis and treatment of chronic lymphocyte leukemia. By an experiment, bone marrows and peripheral blood specimens of normal people and leukemia sufferers are collected, and the detection result shows as follows: Matriptase mRNA and protein are highly expressed in the chronic lymphocyte leukemia sufferers, the expression level of Matriptase of the surface of lymphocyte can serve as a molecular marker for diagnosis of chronic lymphocyte leukemia, and the Matriptase can serve as a novel target for diagnosis and treatment of chronic lymphocyte leukemia.

The invention relates to a TNF alpha and DC-SIGN fusion protein and an application thereof. In a traditional anti-tumor medicament or a treatment method, normal cells are easy to damage in the process of killing tumor cells. The targeting anti-tumor fusion protein provided by the invention comprises an identification functional domain and an action functional domain, as well as a connecting peptide for connecting the two functional domains. The identification functional domain is as follows: a lectin polypeptide with tumor cell surface sugar chain identification and combination functions-a DC surface specific intercellular adhesion factor 3 combined with non-integrin molecules (DC-SIGN, dendritic-cell-specific ICAM-3-grabbing nonintegrin) is positioned at a C terminal of the fusion protein; the action functional domain is as follows: a tumor necrosis factor (TNF) is positioned at an N terminal of the fusion protein; and the connecting peptide is a short peptide containing 8-25 amino acids. The fusion protein can utilize lectin and cancer cells to perform targeting combination, induce the apoptosis of the cancer cells through a ligand capable of promoting the apoptosis of the cells and simultaneously reduce the killing effect against normal tissues and cells.

An Agrin peptide which induces proliferation of cardiomyocytes for treating a heart disease is provided.

Described is a matrix to identify mother's milk missing fucosyltransferase-2 (FUT2) dependent glycans which comprise a line of a glycan binding protein such as a lectin or antibody suitable to bind 2′fucosyl-glycans and a line of a positive control to bind a mother's milk protein. For instance, this matrix is porous and allows for transport by capillary force of compounds of mother's milk such as glycoproteins. Especially, the glycan binding protein is the plant lectin from Ulex europaeus. A diagnostic kit comprising one or more of such matrices and a device suitable to receive such a matrix provided with a milk application window and a read-out window has been described as well. Finally a kit-of-parts comprising such a diagnostic kit and one or more feeding doses of 2′fucosyl-glycans has been disclosed.

Provided are methods, materials and kits for analyzing DNA samples from bovine to determine whether the animal is a recessive carrier of a genetic mutation that is associated with arthrogryposis multiplex (AM). DNA-containing samples are analyzed by genetic testing to determine whether or not a deletion mutation is present in one of the alleles that are responsible for the AM genetic mutation. In an aspect the deletion encompasses the entirety of the ISG15 ubiquitin-like modifier (ISG15) gene. In an aspect the deletion further encompasses one or both of the 5′ regulatory region of the hairy and enhancer split 4 (HES4) and of the agrin (AGRN) gene and of the first two exons of the AGRN gene.

The invention discloses an application of CHCHHD10 in promoting AChR subunit gene expression and maintaining NMJ stability. According to the invention, the regulation effect of CHCHD10 in skeletal muscle on NMJ steady state is explored through experimental technical means such as immunohistochemistry, electrophysiology, electron microscopy, behavioristics and the like; the ATP level of cells or tissues can be reduced by silencing or knocking out the CHCHD10 gene, and the generation of ATP is prompted to depend on the expression of CHCHD10; the fact that ATP can promote AChR aggregation inducedby Agrin is further proved; a chromatin immunoprecipitation experiment shows that ATP can promote the combination of a transcription factor GABP alpha and a promoter of an AChR subunit gene; the ATPis prompted to promote AChR aggregation induced by Agrin by promoting AChR subunit gene expression, so that the normal function of the NMJ is maintained; the invention suggests that targeting NMJ maybe an important means for early treatment and intervention of ALS and other neuromuscular diseases.

A method for the production of a hybridoma cell lines producing monoclonal antibodies capable to specifically binding to a human C44-fragment of agrin, comprising administering to wild-type-mice an immunizing amount of C44y≧4-fragment of agrin, isolating antibody producing cells from the immunized mice, fusing them with a myeloma cell line, growing the fused cells in a selection medium, screening the antibodies in the supernatants of hybridoma cells for binding to C44-fragment of agrin and isolating the hybridoma cells producing the desired monoclonal antibodies

A method of treating an ischemic heart disease in a subject in need thereof is provided. The method comprises administering to the subject a therapeutically effective amount of Agrin in an anterograde intracoronary manner, thereby treating the ischemic heart disease in the subject.