| Class / Patent application number | Description | Number of patent applications / Date published |
|---|
| 530409000 | Nitrogen containing reactant | 24 |
| 20080275222 | Method for Reducing the Allergenic Protein Content of Natural Rubber Latex Articles - The present invention provides a method of reducing and/or neutralizing the allergenic protein content of natural rubber latex articles by exposing the natural rubber latex from which the article is made or the final natural rubber latex to an allergenic protein reducing compound. The allergenic protein reducing compounds for use in the present invention fall generally into two classes: (1) cationic compounds and (2) nitrogen-containing compounds. Quaternary ammonium salts are particularly preferred allergenic protein reducing compounds. | 11-06-2008 |
| 20090270598 | AMPHIPHILES FOR PROTEIN SOLUBILIZATION AND STABILIZATION - The invention provides amphiphiles for manipulating membrane proteins. The amphiphiles can feature carbohydrate-derived hydrophilic groups and branchpoints in the hydrophilic moiety and/or in a lipophilic moiety. Such amphiphiles are useful as detergents for solubilization and stabilization of membrane proteins, including photosynthetic protein superassemblies obtained from bacterial membranes. | 10-29-2009 |
| 20100249386 | DINITROXIDE-TYPE BIRADICAL COMPOUNDS OPTIMIZED FOR DYNAMIC NUCLEAR POLARIZATION (DNP) - The present invention relates to the field of organic chemistry and in particular to organic free radicals used as polarizing agents in the technique of Dynamic Nuclear Polarization (DNP), which involves transferring the polarization of electron spins to the nuclei of a compound whose Nuclear Magnetic Resonance (NMR) is being observed. It concerns dinitroxide-type biradical polarizing agents characterized by a rigid linkage between the nitroxide units that enables optimal orientation and distance to be maintained between the aminoxyl groups of said nitroxide units. This particular structure enables, at low temperatures and high fields, optimal transfer of polarization and optimal enhancement of NMR/MAS signals of the polarized nuclei of the compound studied. | 09-30-2010 |
| 20100249387 | Process for producing coelenteramide or an analog thereof - A process for producing coelenteramide or its analog in a high yield has been desired. The invention provides a process for producing di-O-methylcoelenteramide or its analog, which comprises reacting O-methylcoelenteramine or its analog with 4-methoxyphenylacetyl halide or its analog. The invention also provides a process for producing coelenteramide or its analog, which comprises demethylation of di-O-methylcoelenteramide or its analog. | 09-30-2010 |
| 20100331529 | METHODS FOR INCREASING PROTEIN POLYETHYLENE GLYCOL (PEG) CONJUGATION - The present invention relates to highly conjugated proteins and methods for making such proteins. In particular, the present invention relates to methods for linking additional sites to a protein for conjugation with activated polyethylene glycol (PEG) linkers, without denaturing the protein. The invention also relates to highly conjugated proteins with decreased immunogenicity and increased circulating half-life. | 12-30-2010 |
| 20110040077 | Protein-Responsive Translational Regulatory System Using RNA-Protein Interacting Motif - An object of the present invention is to provide a translationally regulatable mRNA which has wider application and can perform specific ON-OFF regulation, an RNA-protein complex specifically bound to the mRNA, and a translational regulatory system. The present invention provides an mRNA having an RNA-protein complex interacting motif-derived nucleotide sequence 5′ to the ribosome-binding site or within the 5′ region of the open reading frame, and an mRNA having a nucleotide sequence complementary to an RNA-protein complex interacting motif-derived nucleotide sequence 5′ to the ribosome-binding site or within the 5′ region of the open reading frame. | 02-17-2011 |
| 20110092679 | Dark Quenchers For Donor-Acceptor Energy Transfer - The present invention provides a family of dark quenchers, termed Black Hole Quenchers (“BHQs”), that are efficient quenchers of excited state energy but which are themselves substantially non-fluorescent. Also provided are methods of using the BHQs, probes incorporating the BHQs and methods of using the probes. | 04-21-2011 |
| 20110118450 | ACCELERANTS FOR THE MODIFICATION OF NON-NATURAL AMINO ACIDS AND NON-NATURAL AMINO ACID POLYPEPTIDES - Disclosed herein are accelerants for the formation of oxime-containing compounds from the reaction of a carbonyl-containing compound and a hydroxylamine-containing compound. The oxime-containing compound, the carbonyl-containing compound and the hydroxylamine-containing compound can each be a non-natural amino acid or a non-natural amino acid polypeptide. Also disclosed is the use of such accelerants to form oxime-containing compounds, the resulting oxime-containing compounds, and reaction mixtures containing such accelerants. | 05-19-2011 |
| 20110118451 | COMPOSITIONS CONTAINING, METHODS INVOLVING, AND USES OF NON-NATURAL AMINO ACIDS AND POLYPEPTIDES - Disclosed herein are non-natural amino acids and polypeptides that include at least one non-natural amino acid, and methods for making such non-natural amino acids and polypeptides. The non-natural amino acids, by themselves or as a part of a polypeptide, can include a wide range of possible functionalities, but typical have at least one oxime, carbonyl, dicarbonyl, and/or hydroxylamine group. Also disclosed herein are non-natural amino acid polypeptides that are further modified post-translationally, methods for effecting such modifications, and methods for purifying such polypeptides. Typically, the modified non-natural amino acid polypeptides include at least one oxime, carbonyl, dicarbonyl, and/or hydroxylamine group. Further disclosed are methods for using such non-natural amino acid polypeptides and modified non-natural amino acid polypeptides, including therapeutic, diagnostic, and other biotechnology uses. | 05-19-2011 |
| 20110224411 | Mutant tRNA for Introducing Unnatural Amino Acid Into Protein - It is an objective of the present invention to provide tRNA that has CUA or CCCG as an anticodon and is aminoacylated with an unnatural amino acid, such tRNA being capable of efficiently introducing an unnatural amino acid into a protein without competing with a termination factor. Such tRNA is a mutant tRNA for tryptophan which has G at the 5′ end, C as a base pairing with the G at the 5′ end, and A as a base next to the C on the 3′ side, such tRNA being a mutant tRNA which pairs with a stop codon and has CUA as an anticodon or a mutant tRNA which pairs with a stop codon or a 4-base codon has CUA or CCCG as an anticodon, into which a single base has been inserted just before the CCA sequence at the 3′ end. | 09-15-2011 |
| 20110313140 | PROCESS FOR PRODUCING COELENTERAMIDE OR AN ANALOG THEREOF - A process for producing coelenteramide or its analog in a high yield has been desired. The invention provides a process for producing di-O-methylcoelenteramide or its analog of formula (3) | 12-22-2011 |
| 20110319603 | METHOD FOR FLUORESCENTLY LABELING PROTEIN - A method for fluorescently labeling a protein is provided that can also be used for labeling a biomolecule (a protein) in vivo with fluorescence. The method for fluorescently labeling a protein includes obtaining a fusion protein of a target protein to be labeled and, for example, a photoactive yellow protein (PYP), and fluorescently labeling the target protein by reacting the fusion protein with a compound represented by Formula (I), wherein in the compound represented by Formula (I), a coumarin skeleton in Formula (A) or a benzene skeleton in Formula (B) is intramolecnlarly associated with a group X and as a result, fluorescence derived from the group X is suppressed and when in the compound of Formula (I), the coumarin skeleton in Formula (A) or the benzene skeleton in Formula (B) is bound to the PYP or the PYP-derived protein contained in the fusion protein, the coumarin skeleton in Formula (A) or the benzene skeleton in Formula (B) is intramolecnlarly dissociated from the group X, and thereby fluorescence derived from the group X can be emitted. | 12-29-2011 |
| 20120296072 | N-TERMINALLY CHEMICALLY MODIFIED PROTEIN COMPOSITIONS AND METHODS - Provided herein are methods and compositions relating to the attachment of water soluble polymers to proteins. Provided are novel methods for N-terminally modifying proteins or analogs thereof, and resultant compositions, including novel N-terminally chemically modified G-CSF compositions and related methods of preparation. Also provided is chemically modified consensus interferon. | 11-22-2012 |
| 20130012690 | METHOD FOR STABILIZATION OF PROTEINS USING NON-NATURAL AMINO ACIDS - The present invention provides a method for producing modified stable polypeptides introducing at least one non-natural amino acid into the hydrophobic region of the polypeptide. The thermal and chemical stability of such polypeptides is improved compared to those properties of its corresponding wild type proteins. | 01-10-2013 |
| 20130123475 | Non-Fluorescent Quencher Compounds and Biomolecular Assays - Bis-diazo, triaryl and aryldiazo-N-arylphenazonium quencher moieties, substituted with electron-withdrawing and electron-donating substituents which induce polarity in the delocalized aryl/diazo ring systems, are useful as labels when attached to biomolecules such as polynucleotides, nucleosides, nucleotides and polypeptides. The quencher moieties are non-fluorescent and accept energy transfer from fluorescent reporter labels by any energy-transfer mechanism, such as FRET. | 05-16-2013 |
| 20130281680 | PROCESS FOR PRODUCING COELENTERAMIDE OR AN ANALOG THEREOF - A process for producing coelenteramide or its analog in a high yield has been desired. The invention provides a process for producing di-O-methylcoelenteramide or its analog of formula (3) | 10-24-2013 |
| 20130303737 | TARGETED SCHIFF BASE COMPLEXES - The present invention provides targeted Schiff base complexes. In particular the present invention provides biopolymer targeted transition metal complexes configured to inhibit the activity of targeted proteins, methods of synthesis thereof, and pharmaceutical compositions and uses thereof. | 11-14-2013 |
| 20140128581 | DISUBSTITUTED AMINO ACIDS AND METHODS OF PREPARATION AND USE THEREOF - Provided are crystalline α, α-disubstituted amino acids and their crystalline salts containing a terminal alkene on one of their side chains, as well as optionally crystalline halogenated and deuterated analogs of the α, α-disubstituted amino acids and their salts; methods of making these, and methods of using these. | 05-08-2014 |
| 20140364594 | CYCLIC COMPOUND, METHOD FOR PRODUCING CYCLIC COMPOUND, AND METHOD FOR MODIFYING BIOLOGICAL MOLECULE - The invention aims in establishing a method for modifying biomolecules using a reaction that efficiently modifies biomolecules and is widely applicable. The invention thus provides a cyclic compound containing two triazole rings formed by adding and ligating an azide compound possessing an azido group to each of the two carbon-carbon triple bond sites of an eight-membered cyclic skeleton of a cyclic diyne compound by a double click reaction; a method for producing a cyclic compound using a double click reaction; and a method for modifying biomolecules. | 12-11-2014 |
| 20140371433 | METHOD FOR PREPARING PHYCOCYANIN - Provided is a preparation method for phycocyanin, including: adding chitosan to a suspension of cyanobacteria containing phycocyanin; and filtering the suspension. | 12-18-2014 |
| 20140378670 | Immobilized Proteins and Methods and Uses Thereof - The invention relates to the field of covalently attaching proteins to a substrate, particularly to methods of immobilizing proteins by posttranslationally modifying a cysteine residue of said protein through the addition of functional groups. The invention also relates to biological molecules used in such techniques, including proteins, and detection methods and kits that utilize such immobilized proteins, such as a microdevice or “protein chip”, a high-throughput screening device, and for the microscopy of proteins on a surface. | 12-25-2014 |
| 20150307587 | RTRAIL Mutant and Monomethyl Auristatin E Conjugate Thereof - Disclosed are an rTRAIL mutant and monomethyl auristatin E (MMAE) conjugate thereof. The amino acid sequence thereof is as represented by SEQ ID No.1. Also disclosed are a coding gene of the rTRAIL mutant and expression system, recombinant vector and expression unit containing the coding gene. Also disclosed are an rTRAIL mutant-vcMMAE conjugate and preparation and uses thereof. The conjugate of the present invention has the biological functions of both the rTRAIL mutant and the MMAE; the MMAE is directionally transferred to a tumor cell through the specific binding between the rTRAIL mutant and a death receptor on the surface of the tumor cell, and is released and takes effect in the tumor cell, thus killing the tumor cells less sensitive or even resistant to TRAIL, and reducing the toxicity generated by the separate administration of the MMAE. | 10-29-2015 |
| 20150322114 | Self-Assembling Peptides - There is provided a composition comprising a self-assembling membrane, wherein the self-assembling membrane comprises elastin-like polymers (ELPs) and peptide amphiphiles (PAs). Also provided is a method of forming a membrane and uses of the membrane. | 11-12-2015 |
| 20160146843 | DEVELOPMENT AND USE OF CYSTEINE-LABELED FLUORESCENT PROBES OF UNBOUND ANALYTES - A method for high throughput discovery of proteins fluorescently labeled at a cysteine residue and that undergo a change in fluorescence ratio at 2 wavelengths upon binding an unbound analyte is described. Probes are disclosed which are labeled at a cysteine residue and also probes labeled at both cysteine and lysine with two different fluorophores. These probes are useful for characterization and measurement of hydrophobic species in a fluid sample, particularly characterization and measurement of levels of unbound free fatty acids. A profile of unbound free fatty acids can be determined for an individual which can be used to determine the individual's relative risk for disease. | 05-26-2016 |
