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5605808 Oncoprotein protein kinase
PATENT ABSTRACTS
invention makes it possible to assay an endotoxin originating from gram-negative bacteria contained in a biological sample such as blood, urine and cerebrospinal fluid at an extremely high sensitivity without being affected by (1 right arrow 3)- beta-D-glucan.
5605807 PROCESS FOR SCREENING FOR MALIGNANT TUMORS BY DETERMINING THE AMOUNT OF GLCNAC TRANSFERASE ACTIVITY
745
5605808 ONCOPROTEIN PROTEIN KINASE Karin Michae; Hibi Masahik; Lin Arming San Diego, CA, UNITED STATES Assigned to The Regents of the University of California An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD as determined by reducing SDS-PAGE, having serine and threonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences and method of detection of JNK are provided herein. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites.
V
Dennis James W Etobicoke, CANADA Assigned to Mount Sinai Hospital Corporation
5605809 A process is provided for screening for a malignant tumor. The process comprises the steps of detemtining the amount of GIcNAc transferase V activity in a tumor sample by reacting the GicNAc transferase V in a tumor sample with an aceeptor substrate and a sugar nucleotide donor to produce a detectable change, and detecting the change. The acceptor substrate is an oligosaccharide, a glycopeptide or a glycoprotein having the structure GIcNAc betal-2Man alphal-6Man-R1. R1 is GIcNAc betal-4GlcNAc with or without fucose or a synthetic linker. The sugar nucleotide donor is uridine diphospho-N-acetylglycosamine. The amount of GlcNAc transferase V activity in the sample is thereby determined. A determination of the malignancy of the tumor is made by comparing the amount of GIcNAc transferase V activity in the sample with an amount of GIcNAc transferase V associated with normal tissues or with known malignant tumors. A diagnostic kit for screening for a malignant tumor is provided. The kit comprises an acceptor substrate and a sugar nucleotide donor to interact with GIcNAc transferase V in a tumor sample to produce a detectable change, and means for detecting the change.
COMPOSITIONS DETECTION BIOLOGICAL METHODS
FOR
THE
OF PROTEASES SAMPLES
IN
AND
OF USE THEREOF
Komoriya Akira; Packard Beverly RockviUe, MD, UNITED STATES Assigned to Oncoimmunin Inc The present invention provides for novel reagents whose fluorescence increases in the presence of particular proteases. The reagents comprise a characteristically folded peptide backbone each end of which is conjugated to a fluorophore. When the folded peptide is cleaved, as by digestion with a protease, the fluorophores provide a high intensity fluorescent signal at a visible wavelength. Because of their high fluorescence signal in the visible wavelengths, these protease indicators are particularly well suited for detection of protease activity in biological samples, in particular in frozen tissue sections. Thus this invention also provides for methods of detecting protease activity in situ in frozen sections.
invention makes it possible to assay an endotoxin originating from gram-negative bacteria contained in a biological sample such as blood, urine and cerebrospinal fluid at an extremely high sensitivity without being affected by (1 right arrow 3)- beta-D-glucan.
5605807 PROCESS FOR SCREENING FOR MALIGNANT TUMORS BY DETERMINING THE AMOUNT OF GLCNAC TRANSFERASE ACTIVITY
745
5605808 ONCOPROTEIN PROTEIN KINASE Karin Michae; Hibi Masahik; Lin Arming San Diego, CA, UNITED STATES Assigned to The Regents of the University of California An isolated polypeptide (JNK) characterized by having a molecular weight of 46 kD as determined by reducing SDS-PAGE, having serine and threonine kinase activity, phosphorylating the c-Jun N-terminal activation domain and polynucleotide sequences and method of detection of JNK are provided herein. JNK phosphorylates c-Jun N-terminal activation domain which affects gene expression from AP-1 sites.
V
Dennis James W Etobicoke, CANADA Assigned to Mount Sinai Hospital Corporation
5605809 A process is provided for screening for a malignant tumor. The process comprises the steps of detemtining the amount of GIcNAc transferase V activity in a tumor sample by reacting the GicNAc transferase V in a tumor sample with an aceeptor substrate and a sugar nucleotide donor to produce a detectable change, and detecting the change. The acceptor substrate is an oligosaccharide, a glycopeptide or a glycoprotein having the structure GIcNAc betal-2Man alphal-6Man-R1. R1 is GIcNAc betal-4GlcNAc with or without fucose or a synthetic linker. The sugar nucleotide donor is uridine diphospho-N-acetylglycosamine. The amount of GlcNAc transferase V activity in the sample is thereby determined. A determination of the malignancy of the tumor is made by comparing the amount of GIcNAc transferase V activity in the sample with an amount of GIcNAc transferase V associated with normal tissues or with known malignant tumors. A diagnostic kit for screening for a malignant tumor is provided. The kit comprises an acceptor substrate and a sugar nucleotide donor to interact with GIcNAc transferase V in a tumor sample to produce a detectable change, and means for detecting the change.
COMPOSITIONS DETECTION BIOLOGICAL METHODS
FOR
THE
OF PROTEASES SAMPLES
IN
AND
OF USE THEREOF
Komoriya Akira; Packard Beverly RockviUe, MD, UNITED STATES Assigned to Oncoimmunin Inc The present invention provides for novel reagents whose fluorescence increases in the presence of particular proteases. The reagents comprise a characteristically folded peptide backbone each end of which is conjugated to a fluorophore. When the folded peptide is cleaved, as by digestion with a protease, the fluorophores provide a high intensity fluorescent signal at a visible wavelength. Because of their high fluorescence signal in the visible wavelengths, these protease indicators are particularly well suited for detection of protease activity in biological samples, in particular in frozen tissue sections. Thus this invention also provides for methods of detecting protease activity in situ in frozen sections.