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250 results about "Lysine residue" patented technology

Methods of modulating bromodomains

InactiveUS20120028912A1Inhibit binding/formationInhibit bindingBiocideDispersion deliveryDiseaseBromodomain
Owner:THE J DAVID GLADSTONE INST A TESTAMENTARY TRUST ESTABLISHED UNDER THE WILL OF J DAVID GLADS +1

Protein appropriate for orientation-controlled immobilization and immobilization carrier on which the proteins are immobilized

An object of the present invention is to provide a novel protein having the following amino acid sequence altered for specifically and efficiently binding a protein to an immobilization carrier via the carboxy terminus. The protein is used for immobilizing a portion represented by R1-R2 on an immobilization carrier, comprising the amino acid sequence represented by the general formula R1-R2-R3-R4-R5 [wherein:the sequences are oriented from the amino terminal side to the carboxy terminal side;the sequence of the R1 portion is the sequence of a subject protein to be immobilized and contains neither a lysine residue nor a cysteine residue;the sequence of the R2 portion may be absent, but when the sequence of the R2 portion is present, the sequence of the R2 portion is a spacer sequence composed of amino acid residues other than lysine and cysteine residues;the sequence of the R3 portion is composed of two residues of amino acid represented by cysteine-X (where X denotes an amino acid residue other than lysine or cysteine);the sequence of the R4 portion may be absent, but when the sequence of the R4 portion is present, the sequence of the R4 portion contains neither a lysine residue nor a cysteine residue, but contains an acidic amino acid residue capable of acidifying the isoelectric point of the entire protein comprising the amino acid sequence represented by the general formula R1-R2-R3-R4-R5; andthe sequence of an R5 portion is an affinity tag sequence for protein purification.
Owner:NAT INST OF ADVANCED IND SCI & TECH

Synthesis and application of exenatide joined with polyethylene glycol

The invention relates to exenatide joined with polyethylene glycol. The structural general formula of exenatide is (I), mPEG represents residue of methoxy polyethylene glycol, the selected value of n is 0-3, R represents an exenatide molecule from which an amino is removed, the amino is of lysine residue or of N-end histidine residue in the exenatide molecule, and the molecular weight of the exenatide joined with polyethylene glycol is 9,800-110,000. The invention further relates to a preparation method of the compound and application of the compound in preparing medicines for curing type 2 diabetes mellitus. The exenatide joined with polyethylene glycol has the advantages of being long in half-life period and good in stability and hypoglycemic effect.
Owner:CHEMFUTURE PHARMATECH JIANGSU

Laying hen feed

ActiveCN103099064AEgg shell quality advantageFeed-to-egg ratio advantageAnimal feeding stuffTrace elementFodder
The invention discloses laying hen feed. The laying hen feed consists of the following components in parts by weight: 10-50 parts of calcium hydrogen phosphate, 30-70 parts of stone powder, 20-30 parts of salt, 10-20 parts of sodium sulfate, 6-10 parts of choline, 18-20 parts of compound trace elements, 4-5 parts of compound vitamin, 10-25 parts of lysine, 10-15 parts of methionine, 100-150 parts of bone meal, 350-400 parts of cottonseed meal, 50-100 parts of blood cell protein powder, 100-200 parts of corn protein powder, 50-100 parts of lysine residue and 10-15 parts of additive. In application, complete feed can be prepared by mixing the laying hen feed with conventional basal feed. The invention relates to the laying hen feed which is applicable to laying hens in an egg producing period to meet the needs for exact effect, lasting egg production peak and high feed-gain ratio of the laying hen feed.
Owner:南通和美华科技饲料有限公司

Method for the linkage of bifunctional chelating agents and (radioactive) transition metal complexes to proteins and peptides

InactiveUS20070184537A1Avoiding misfolding and denaturationIn-vivo radioactive preparationsFermentationPeptideLysine residue
The present invention relates to a method for radioactive labeling of a protein or peptide, by providing a protein or peptide having at least one glutamine or lysine residue; adding a metal chelating agent having at least one lysine or glutamine residue, respectively, which metal chelating agent is optionally complexed with a radioactive or paramagnetic metal; reacting the protein or peptide and metal chelating agent in the presence of a transglutaminase to obtain a protein or peptide with a metal chelating group covalently bound thereto, and optionally complexing the metal chelating group with a radioactive or paramagnetic metal. The invention also relates to proteins and peptides thus labeled and to proteins and peptides that have been coupled to a metal chelating agent but not yet labeled.
Owner:PAUL SCHERRER INSTITUT

Immobilized protein that is immobilized only at its amino terminus in orientation-controlled manner

This invention provides an immobilized protein bound to an immobilization carrier at a protein amino terminus via the sole α-amino group of the protein comprising an amino acid sequence containing neither lysine residues nor cysteine residues represented by the general formula S1-R1-R2, wherein: the sequences are oriented from the amino terminal side to the carboxy terminal side; the sequence of the S1 portion may be absent, but when the sequence of the S1 portion is present, the sequence of the S1 portion is a spacer sequence composed of amino acid residues other than lysine and cysteine residues; the sequence of the R1 portion is the sequence of a subject protein to be immobilized and contains neither lysine residues nor cysteine residues; and the sequence of the R2 portion may be absent, but when the sequence of the R2 portion is present, the sequence of the R2 portion is a spacer sequence composed of amino acid residues other than lysine and cysteine residues.
Owner:NAT INST OF ADVANCED IND SCI & TECH

Protein analysis

A method of forming an array of proteins selected from antigens or antibodies; said method comprising the steps of (i) expressing in a recombinant cell, a fusion protein which comprises either (a) an antigen or (b) an antibody binding protein, fused to a peptide having up to 50 amino acids, which peptide comprises amino acid sequence of SEQ ID NO 1 LX1X2IX3X4X5X6KX7X8X9X10 (SEQ ID NO 1) where X1 is a naturally occurring amino acid, X2 is any naturally occurring amino acid other than leucine, valine, isoleucine, tryptophan, phenylalanine or tyrosine, X3 is phenylalanine or leucine, X4 is glutamine or asparagine, X5 is alanine, glycine, serine or threonine, X6 is glycine or methionine, X7 is isoleucine, methionine or valine, X8 is glutamine, leucine, valine, tyrosine or isoleucine, X9 is tryptophan, tyrosine, valine, phenylalanine, leucine or isoleucine and X10 is any naturally occurring amino acid other than asparagine or glutamine; where said peptide is capable of being biotinylated by a biotin ligase at the lysine residue adjacent to X6; (ii) biotinylating said peptide of the fusion protein at the lysine residue adjacent X6; (iii) isolating the biotinylated fusion protein; (iv) applying the biotinylated fusion protein to an avidin or streptavidin coated non-porous support; (v) forming an array of at least three different proteins on the support by either (a) where the fusion protein comprises an antigen, carrying out steps (i) to (iv) the desired number of times to form an antigen array; or (b) where the fusion protein comprises an antibody binding protein, applying to said protein, either prior to or after step (iv) a plurality of different antibodies or binding fragments thereof.
Owner:NEXTGEN SCI

Methylated Peptides Derived from Tau Protein and Their Antibodies for Diagnosis and Therapy of Alzheimer's Disease

In sporadic Alzheimer's disease, neurofibrillary lesion formation is preceded by extensive post-translational modification of the microtubule associated protein tau. Immunoassays have been developed recently that detect tau in biological specimens, thus providing a means for pre-mortem diagnosis of Alzheimer's disease, which has remained elusive. These assays have been improved by the analysis of relevant post-translational modifications, such as phosphorylation, however opportunity for improvement remains. The present invention addresses this issue by disclosing synthetic methylated peptides derived from the tau protein of paired helical filaments and non-diseased control brain. Alzheimer's disease specificity is provided by the presence or absence of methyl moieties on lysine residues and differences between mono-, di-, and tri-methylation. The methylated peptide is useful as an antigen and a binding partner for identifying compounds that interact with the peptide and the methylated tau protein, including antibodies that can distinguish non-diseased brain from that affected by Alzheimer's disease. The resulting antibodies are useful diagnostically and therapeutically. The compounds that specifically bind to methylated tau proteins are useful for eliminating abnormally methylated tau.
Owner:UNIV OF MARYLAND BALTIMORE +1

Method of covalently modifying proteins with organic molecules to prevent aggregation

A system and method for preventing protein aggregation is developed by covalent modification of proteins with organic molecules that can preserve the native protein folding. Proteins are covalently modified with sugar alcohols or cyclodextrins (organic Kosmotropes) or other small molecule drugs by water-driven bioorganic reactions in water. In the water-driven bioorganic reactions, the reagent is stable in water and can modify lysine residues or cysteine residue of a protein at physiological conditions with high yield and fast rate. Proteins and antibodies will be modified by non-natural sugar alcohols. As a result, the efficacy of protein drugs (reduction in aggregation and enzymatic degradation, and increase in blood stream life time) may be improved.
Owner:SYRACUSE UNIVERSITY

Copolymer containing lysine residue on side chain and preparation method thereof as well as fibrinolytic functional material

The invention relates to a copolymer containing a lysine residue on a side chain, a preparation method of the copolymer, and a fibrinolytic functional material prepared on the basis of the copolymer. The preparation method comprises the following steps of: synthesizing a lysine functional monomer; on the presence of an initiator, preparing the copolymer containing the lysine residue at the side chain by carrying out free radical polymerization on the functional monomer and a vinyl monomer; and blending the prepared copolymer with other commercially available medical polymer materials, and processing and molding to prepare a biological medical functional polymer material of which the surface has a fibrinolytic function. When the obtained material contacts with blood, the fibrinolytic system of a human body can be simulated and nascent thrombus on the surface of a material can be dissolved. The copolymer can be adjusted and controlled directly by changing the charging ratio of the lysine functional monomer to a comonomer, so that the process is simple; the copolymer containing the lysine residue on the side chain can be conveniently blended with various commercially available medical polymer materials, and can be subjected to various processing for molding, so that the construction of a fibrinolytic system on the surface of a material is realized while a biological material in a certain shape is prepared, and the universality is strong.
Owner:JIANGSU BIOSURF BIOTECH CO LTD

Novel compounds, use thereof in cosmetic and cosmeceutic applications, and compositions comprising same

ActiveUS20100311667A1Increase productionPreventing, reducing, delaying or treating a skin conditionCosmetic preparationsToilet preparationsGlycineHydrogen
A compound of the formula I: R-A-Gly-His-B (I) wherein: A and B are independently of each other a L-lysine residue, a D-lysine residue, or a L- or D-lysine residue in which the NH2 group of the side chain comprises a modification, where-in said modification is (i) a replacement with a hydrogen, (ii) an acetylation, (iii) a benzoylation, or (iv) a palmitoylation; GIy is a glycine residue; His is a L- or D-histidine residue; R is CH3—(CH2)n—CO—, wherein n=2, 3, 4, 5, 6, 7 or 8; R′ is a group of formula (II): N(Z)(Z′) (II) wherein: Z and Z′ is hydrogen, a methyl group, an ethyl group, a phenyl group, an hexyl group, a decyl group or an hexadecyl group; or a racemate, an enantiomer or a diastereomer thereof, or mixtures thereof, or a salt thereof.
Owner:LUCAS MEYER COSMETICS CANADA

Chemical treatment of in vivo tissue to alter charge and net charge density characteristics

A method for treating animal tissue with acylation agents to alter the net charge and net charge density of the treated tissue for therapeutic applications is provided. The method involves applying an alkaline solution to the exposed tissue surface area. This results in deprotonation of ε-amino groups of lysine residues on the exposed tissue proteins so that the tissue proteins have a net charge. Then, an acylating agent is applied and the acylating agent reacts with the tissue protein to form a protein complex having an altered net charge. Acylating agents such as sulfonic acids, sulfonyl chlorides, and acid chlorides can be used. The method can be used to treat a wide variety of human tissues including the human cornea for correcting myopia. The method can also be used to treat skin tissue, so that there is an increase in dermal thickness and pliability. The method can be further used to treat articular cartilage.
Owner:DEVORE DALE PAUL +1
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