Abstract: Proteins that are electrophoretically separated in a gel are derivatized to produce fluorescent emissions by incorporating halo-substituted organic compounds into one or both of the electrode buffer solutions at the two ends of the gel. The halo-substituted compounds used are ones that bear an electric charge at the pH of the buffer solutions and gel, and the polarity of the charge on the compounds is such that the compounds migrate from the electrode buffer into the gel under the electrophoretic influence concurrently with the migration of the proteins into the gel. Once the proteins are separated and distributed within the gel and the gel is fully penetrated with the halo-substituted compounds, the gel is irradiated with ultraviolet light to induce a reaction between the halo-substituted compounds and the proteins through the tryptophan residues on the proteins, producing fluorescent reaction products.

Abstract: Proteins that are electrophoretically separated in a gel are derivatized to produce fluorescent emissions by incorporating halo-substituted organic compounds into one or both of the electrode buffer solutions at the two ends of the gel. The halo-substituted compounds used are ones that bear an electric charge at the pH of the buffer solutions and gel, and the polarity of the charge on the compounds is such that the compounds migrate from the electrode buffer into the gel under the electrophoretic influence concurrently with the migration of the proteins into the gel. Once the proteins are separated and distributed within the gel and the gel is fully penetrated with the halo-substituted compounds, the gel is irradiated with ultraviolet light to induce a reaction between the halo-substituted compounds and the proteins through the tryptophan residues on the proteins, producing fluorescent reaction products.

Abstract: Disclosed herein is a method of preparing a protein sample for mass spectroscopy. The method includes separating proteins of the sample on an electrophoresis gel; contacting the proteins with a halo-substituted organic compound; exposing the gel to UV light; detecting fluorescence emitted from the electrophoresis gel; excising at least one portion of the electrophoresis gel based upon the detected fluorescence, wherein said at least one portion contains proteins of the protein sample; and subjecting proteins from the at least one portion to mass spectroscopy. Using this method, more proteins can be identified by GeLC-MS than when the electrophoresis gel is treated with a protein stain or subjected to the gel handling steps accompanying such treatment.

Abstract: Hand cast gels, and solutions for their preparation, are described.

Abstract: A method is provided for detecting a protein using a cyclodextrin covalently linked to at least one label. The cyclodextrin can associate with the protein by sequestering an aromatic amino acid side-chain of the protein in its hydrophobic cavity. After contacting the protein with the cyclodextrin, the label can be detected directly or can undergo a chemical interaction with a reagent to form a detectable product. The label can include an indole moiety, which can react with a halo-substituted organic compound upon exposure to UV light and thereby be rendered fluorescent. Alternatively, the label can include a biotin moiety, which can bind to a binding partner such as avidin, or variants thereof, to form a detectable molecular complex. A labeled cyclodextrin can be used in the present methods to detect a protein of interest in an electrophoresis gel or on a blotting membrane.

Abstract: Hand cast gels, and solutions for their preparation, are described.

Abstract: Hand cast gels, and solutions for their preparation, are described.

Abstract: Proteins that are electrophoretically separated in a gel are derivatized to produce fluorescent emissions by incorporating halo-substituted organic compounds into one or both of the electrode buffer solutions at the two ends of the gel. The halo-substituted compounds used are ones that bear an electric charge at the pH of the buffer solutions and gel, and the polarity of the charge on the compounds is such that the compounds migrate from the electrode buffer into the gel under the electrophoretic influence concurrently with the migration of the proteins into the gel. Once the proteins are separated and distributed within the gel and the gel is fully penetrated with the halo-substituted compounds, the gel is irradiated with ultraviolet light to induce a reaction between the halo-substituted compounds and the proteins through the tryptophan residues on the proteins, producing fluorescent reaction products.

Abstract: Colloidal formulation for staining proteins and methods of their use are provided.

Abstract: Proteins that are electrophoretically separated in a gel are derivatized to produce fluorescent emissions by incorporating halo-substituted organic compounds into one or both of the electrode buffer solutions at the two ends of the gel. The halo-substituted compounds used are ones that bear an electric charge at the pH of the buffer solutions and gel, and the polarity of the charge on the compounds is such that the compounds migrate from the electrode buffer into the gel under the electrophoretic influence concurrently with the migration of the proteins into the gel. Once the proteins are separated and distributed within the gel and the gel is fully penetrated with the halo-substituted compounds, the gel is irradiated with ultraviolet light to induce a reaction between the halo-substituted compounds and the proteins through the tryptophan residues on the proteins, producing fluorescent reaction products.

Abstract: A method is provided for detecting a protein using a cyclodextrin covalently linked to at least one label. The cyclodextrin can associate with the protein by sequestering an aromatic amino acid side-chain of the protein in its hydrophobic cavity. After contacting the protein with the cyclodextrin, the label can be detected directly or can undergo a chemical interaction with a reagent to form a detectable product. The label can include an indole moiety, which can react with a halo-substituted organic compound upon exposure to UV light and thereby be rendered fluorescent. Alternatively, the label can include a biotin moiety, which can bind to a binding partner such as avidin, or variants thereof, to form a detectable molecular complex. A labeled cyclodextrin can be used in the present methods to detect a protein of interest in an electrophoresis gel or on a blotting membrane.

Abstract: Colloidal formulation for staining proteins and methods of their use are provided.

Abstract: Hand cast gels, and solutions for their preparation, are described.

Abstract: Proteins that are electrophoretically separated in a gel are derivatized to produce fluorescent emissions by incorporating halo-substituted organic compounds into one or both of the electrode buffer solutions at the two ends of the gel. The halo-substituted compounds used are ones that bear an electric charge at the pH of the buffer solutions and gel, and the polarity of the charge on the compounds is such that the compounds migrate from the electrode buffer into the gel under the electrophoretic influence concurrently with the migration of the proteins into the gel. Once the proteins are separated and distributed within the gel and the gel is fully penetrated with the halo-substituted compounds, the gel is irradiated with ultraviolet light to induce a reaction between the halo-substituted compounds and the proteins through the tryptophan residues on the proteins, producing fluorescent reaction products.

Abstract: Disclosed herein is a method of preparing a protein sample for mass spectroscopy. The method includes separating proteins of the sample on an electrophoresis gel; contacting the proteins with a halo-substituted organic compound; exposing the gel to UV light; detecting fluorescence emitted from the electrophoresis gel; excising at least one portion of the electrophoresis gel based upon the detected fluorescence, wherein said at least one portion contains proteins of the protein sample; and subjecting proteins from the at least one portion to mass spectroscopy. Using this method, more proteins can be identified by GeLC-MS than when the electrophoresis gel is treated with a protein stain or subjected to the gel handling steps accompanying such treatment.

Abstract: A directory and members are allocated to store a data set, wherein the directory stores pointers to the members to allow data stored in the members to be accessed. The directory is expanded to accommodate an expansion of the data set, causing the directory to be stored in non-contiguous pages and becoming fragmented. A computational device determines that a threshold that measures a level of fragmentation of the directory relative to an amount of storage allocated for the data set has been exceeded. The computational device reorganizes the fragmented directory, into a reorganized directory that is stored in contiguous pages at the end of the data set, in response to determining that the threshold has been exceeded.

Abstract: A directory and members are allocated to store a data set, wherein the directory stores pointers to the members to allow data stored in the members to be accessed. The directory is expanded to accommodate an expansion of the data set, causing the directory to be stored in non-contiguous pages and becoming fragmented. A computational device determines that a threshold that measures a level of fragmentation of the directory relative to an amount of storage allocated for the data set has been exceeded. The computational device reorganizes the fragmented directory, into a reorganized directory that is stored in contiguous pages at the end of the data set, in response to determining that the threshold has been exceeded.

Abstract: A directory and members are allocated to store a data set, wherein the directory stores pointers to the members to allow data stored in the members to be accessed. The directory is expanded to accommodate an expansion of the data set, causing the directory to be stored in non-contiguous pages and becoming fragmented. A computational device determines that a threshold that measures a level of fragmentation of the directory relative to an amount of storage allocated for the data set has been exceeded. The computational device reorganizes the fragmented directory, into a reorganized directory that is stored in contiguous pages at the end of the data set, in response to determining that the threshold has been exceeded.

Abstract: A directory and members are allocated to store a data set, wherein the directory stores pointers to the members to allow data stored in the members to be accessed. The directory is expanded to accommodate an expansion of the data set, causing the directory to be stored in non-contiguous pages and becoming fragmented. A computational device determines that a threshold that measures a level of fragmentation of the directory relative to an amount of storage allocated for the data set has been exceeded. The computational device reorganizes the fragmented directory, into a reorganized directory that is stored in contiguous pages at the end of the data set, in response to determining that the threshold has been exceeded.

Abstract: This invention pertains to the general field of chemical and biological assays which employ electrochemiluminescence (ECL), also referred to as electrogenerated chemiliminescence. More particularly, the present invention pertains to certain classes of chemical moieties which strongly quench ECL, and the use of these ECL quenchers in combination with ECL labels, for example, in ECL assay methods which employ an ECL quencher and an ECL label. One class of such quenching moieties are those which comprise at least one benzene moiety. Sub-classes of such quenching moieties are those which comprise at least one phenol moiety, quinone moiety, benzene carboxylic acid, and/or benzene carboxylate moiety.