41 results about "Phosphoserine" patented technology

Cements containing certain small molecule amino acid phosphate compounds such as phosphoserine and certain multivalent metal compounds such as but not limited to calcium phosphate have been found to have improved properties and form a macromolecular network in the presence of a bioactive glass material that contain silicates, phosphates, and calcium salts which can be involved in the formation of bonding sites.

Compositions and methods of their use to adhere a variety of materials together are disclosed herein. The compositions include at least tetra calcium phosphate, an effective amount of a compound that is structurally similar to phosphoserine, and can be mixed with an aqueous solution. The compositions provide adhesive and cohesive strength in both wet and dry environments and exhibit significant bond strength upon curing.

Certain small molecule amino acid phosphate compounds such as phosphoserine and certain multivalent metal compounds such as calcium phosphate containing cements have been found to have improved properties and form an interpenetrating network in the presence of a polymer that contain either an electronegative carbonyl oxygen atom of the ester group or an electronegative nitrogen atom of the amine group as the bonding sites of the polymer surfaces to the available multivalent metal ions.

Nucleic acids encoding genes with SepRS and tRNASep activity for site specific incorporation of phosphoserine into a protein or polypeptide and methods of use thereof are described. Typically, SepRS preferentially aminoacylates tRNASep with O-phosphoserine and the tRNASep recognizes at least one codon such as a stop codon. In a preferred embodiment the nucleic acids are on vectors. In one embodiment, the vectors are expressed in cells such as bacterial cells, archeaebacterial cells, and eukaryotic cells. In an alternative embodiment, the vectors are expressed in an in vitro transcription / translation system. Proteins or polypeptides containing phosphoserine produced by the methods described herein can be used for a variety of applications such as research, antibody production, protein array manufacture and development of cell-based screens for new drug discovery.

Disclosed is an O-phosphoserine sulfhydrylase (OPSS) mutant which has a Mycobacterium smegmatis-derived amino acid sequence corresponding to that of SEQ ID NO: 1 which is devoid of three to seven C-terminal amino acid residues. Also, a nucleic acid molecule encoding the OPSS mutant, an expression vector carrying the nucleic acid molecule, and a transformant transformed with the expression vector are disclosed. In addition, a method is provided for producing cysteine in which O-phospho-L-serine (OPS) is reacted with a sulfide in the presence of the OPSS mutant. The OPSS mutant has improved enzymatic activity and can be applied to the environmentally friendly production of L-cysteine through a simple enzymatic conversion reaction.

An object of the present invention is to provide a peptide with superior immuno-enhancing activities, which comprises particular amino acid sequence, and an immuno-enhancing agent comprising such a peptide. The present invention relates to the immuno-enhancing agent comprising a peptide consisting of the following amino acid sequence (I): Q1-SerP-X-SerP-Q2 (I); wherein, SerP represents the phosphoserine residue, X represents one to three of any amino acid residues, and either of Q1 or Q2 dose not exist or neither of them exists, or Q1 and Q2 are independently at least one of any amino acid residue.

Compositions and methods of their use to adhere a variety of materials together are disclosed herein. The compositions include at least tetra calcium phosphate, an effective amount of a compound that is structurally similar to phosphoserine, and can be mixed with an aqueous solution. The compositions provide adhesive and cohesive strength in both wet and dry environments and exhibit significant bond strength upon curing.

Nucleic acids encoding mutant elongation factor proteins (EF-Sep), phosphoseryl-tRNA synthetase (SepRS), and phosphoseryl-tRNA (tRNASep) and methods of use in site specific incorporation of phosphoserine into a protein or polypeptide are described. Typically, SepRS preferentially aminoacylates tRNASep with O-phosphoserine and the tRNASep recognizes at least one codon such as a stop codon. Due to the negative charge of the phosphoserine, Sept-tRNASep does not bind elongation factor Tu (EF-Tu). However, mutant EF-Sep proteins are disclosed that bind Sep-tRNASep and protect Sep-tRNASep from deacylation. In a preferred embodiment the nucleic acids are on vectors and are expressed in cells such as bacterial cells, archeaebacterial cells, and eukaryotic cells. Proteins or polypeptides containing phosphoserine produced by the methods described herein can be used for a variety of applications such as research, antibody production, protein array manufacture and development of cell-based screens for new drug discovery.

Compositions and methods of their use to adhere a variety of materials together are disclosed herein. The compositions include at least multivalent metal compound, an effective amount of a compound that is structurally similar to phosphoserine, and can be mixed with an aqueous solution. The compositions provide adhesive and cohesive strength in both wet and dry environments which exhibit bond strength upon curing with the possible usage as bone cement for bone filler applications.

The present invention generally relates to the fields of cancer therapy and cancer prevention. More particularly, the present invention generally relates to a diagnostic marker for predicting the efficacy of topoisomerase I (topo I) inhibitors in the treatment of cancers. More specifically, the present invention relates to methods, machines, computer systems, computable readable media and kits which can be used to identify and determine the effectiveness of topoisomerase I (topo I) inhibitors in the treatment of cancers, and in some embodiments, the level of sensitivity or resistance of a tumor cell to a topoisomerase I inhibitor, such as camptothecin (CPT), or CTP analogues such as topotecan and irinotecan and derivatives thereof. More specifically, the present invention related to methods, machines, computer systems, computable readable media and kits which can be used to determine the presence of phosphorylation of topoisomerase I polypeptide, in some embodiments phosphorylation at residue serine 10 (S10) of a topoisomerase I polypeptide, wherein the presence of phosphorylation, in particular the phosphorylation at serine 10 of a topoI polypeptide indicates a cancer is likely to be unresponsive to a topo I inhibitor, whereas the absence of phosphorylation, in particular, the absence of phosphorylation at residue serine 10 (S10) identifies a cancer is likely to be responsive to a topo I inhibitor. Other aspect of the present invention relate to phospho-serine 10 topoisomerase I antibodies and other protein binding moieties, and uses thereof.

Compositions and methods for inducing immune tolerance to proteins and subsequence administration of the proteins are disclosed. Compositions comprise proteins complexed with liposomes comprising PS and PC, wherein at least part of the PS is present as lyso-PS.

The invention discloses a Parkinson's disease specific serum endogenous small molecule marker and application thereof. The marker contains 2-amino-3-(4-hydroxyl-3-methoxyphenyl) propionic acid, ferulic acid and citraconic acid, altrose, pentadecanoic acid, o-phosphoserine, 4, 6 beta-hydroxymorphine, L-thyroxine, 5[epsilon], 9[epsilon], 16[epsilon]-17-hydroxy peraluminum-19-acid, 8-(1,2,dyhydroxy-3-methylbutyl-3-ene-1-yl)-7-methoxy-2H-chromine-2-2-ketone,10-hydroxydecanoic acid, perfluoro caprylic acid, and Corchorifatty acid F. The Parkinson's disease specific serum endogenous small molecule marker provided by the invention has the characteristics of high accuracy and high sensitivity. The prediction offline prediction area AUC of some markers reaches 0.95 or above, the accuracy and sensitivity of the markers are high, and the markers can be directly used for Parkinson's disease indexes.

The object is to develop a sleep-inducing agent and an ameliorating agent for stress-induced insomnia. Disclosed is a sleep-inducing oral preparation comprising one or more members selected from serine, phosphoserine, phosphatidylserine, lysophosphatidylserine, acetylserine (which are compounds having a serine unit) and cysteine each in an L-form.

The invention relates to the field of polypeptides, in particular to casein phosphopeptide and its preparation method and application. In the invention, casein in cow's milk is used as a raw material.Casein phosphopeptide with strong calcium holding activity is prepared through trypsin and compound protease (trypsin and neutral protease) enzymolysis, enzyme inactivation, centrifugation, adjustment of isoelectric point / alcohol precipitation and impurity removal, and drying processes. The special cluster phosphoserine structure obtained by the invention has the ability of chelating calcium, andcan effectively promote the absorption and utilization of calcium. The molecular weight of the milk-derived casein phosphopeptide prepared by the invention is mainly between 1,000 and 5,000, which isbeneficial to human body absorption. The content of casein phosphopeptide is more than 85%, and its yield can reach 25%. The method is a preparation method with low cost and simple process, and is suitable for industrial production.

Nucleic acids encoding genes with SepRS and tRNASep activity for site specific incorporation of phosphoserine into a protein or polypeptide and methods of use thereof are described. Typically, SepRS preferentially aminoacylates tRNASep with O-phosphoserine and the tRNASep recognizes at least one codon such as a stop codon. In a preferred embodiment the nucleic acids are on vectors. In one embodiment, the vectors are expressed in cells such as bacterial cells, archeaebacferial cells, and eukaryotic cells. In an alternative embodiment, the vectors are expressed in an in vitro transcription / translation system. Proteins or polypeptides containing phosphoserine produced by the methods described herein can be used for a variety of applications such as research, antibody production, protein array manufacture and development of cell-based screens for new drug discovery.

The present invention relates to a microorganism, wherein the activity of a polypeptide capable of exporting O-phosphoserine (OPS) is enhanced, and a method of producing O-phosphoserine, cysteine, or a cysteine derivative using the microorganism.

The present invention relates to antibody-based probes (including single domain antibody fragment, scFv molecules, antibodies, antibody fragments, diabodies, and the epitope-binding domains thereof) that are capable of immunospecifically and selectively binding to a phospho-serine-containing epitope of Tau, such as, for example, Tau-phospho-serine 396 / 404 peptide. Such imaging ligands are useful to detect pathological Tau protein conformer if present in a biological sample, especially in conjunction with the diagnosis of Alzheimer's disease or other tauopathy, and thus provide a diagnostic for Alzheimer's disease and other Tau pathologies. The scFv molecules of the present invention have utility as diagnostic markers for, Alzheimer's disease and related tauopathies and as pharmaceutical compositions for the treatment of such conditions.

Ac-Phe-Tyr-phosphoSer-Ψ[CH═C]-Pro-Arg-NH2AND Fmoc-bis(pivaloylmethoxy)phosphoSer-Ψ[CH═C]-Pro-2-aminoethyl-(3-indole); and their Phospho-(D)-serine stereoisomers are novel compounds. Ψ refers to a pseudo amide. Such novel compounds advantageously may be used as alkene mimics.

The invention relates to an immobilized metal ion affinity chromatography material taking epoxy polymer microspheres as a matrix and application of the immobilized metal ion affinity chromatography material in enrichment of phosphorylated peptides. Specifically, firstly, allyl glycidyl ether and pentaerythritol tetraacrylate are used as raw materials, porous polymer microspheres with epoxy groups are prepared through a suspension polymerization method; the porous polymer microspheres are used as a matrix, O-phosphate-L-serine with phosphate radical functional groups is used as a modifier, a phosphoric acid functional group is introduced to the surface of the material through an epoxy-ammonia ring-opening reaction under an alkaline condition, and finally the Ti < 4 + >-IMAC material capable of being used for enriching phosphopeptides is obtained through chelating titanium ions. The obtained Ti < 4 + >-IMAC material has very high selectivity on the phosphopeptides, and can be used for high-sensitivity and high-selectivity enrichment of endogenous phosphopeptides in biological sample beta-casein enzymatic hydrolysate and human serum.

Disclosed is an O-phosphoserine sulfhydrylase (OPSS) mutant which has a Mycobacterium smegmatis-derived amino acid sequence corresponding to that of SEQ ID NO: 1 which is devoid of three to seven C-terminal amino acid residues. Also, a nucleic acid molecule encoding the OPSS mutant, an expression vector carrying the nucleic acid molecule, and a transformant transformed with the expression vector are disclosed. In addition, a method is provided for producing cysteine in which O-phospho-L-serine (OPS) is reacted with a sulfide in the presence of the OPSS mutant. The OPSS mutant has improved enzymatic activity and can be applied to the environmentally friendly production of L-cysteine through a simple enzymatic conversion reaction.

Compositions and methods for inducing immune tolerance to proteins and subsequence administration of the proteins are disclosed. Compositions comprise proteins complexed with liposomes comprising PS and PC, wherein at least part of the PS is present as lyso-PS.

The present invention relates to antibody-based probes (including single domain antibody fragment, scFv molecules, antibodies, antibody fragments, diabodies, and the epitope-binding domains thereof) that are capable of immunospecifically and selectively binding to a phospho-serine-containing epitope of Tau, such as, for example, Tau-phospho-serine 396 / 404 peptide. Such imaging ligands are useful to detect pathological Tau protein conformer if present in a biological sample, especially in conjunction with the diagnosis of Alzheimer's disease or other tauopathy, and thus provide a diagnostic for Alzheimer's disease and other Tau pathologies. The scFv molecules of the present invention have utility as diagnostic markers for, Alzheimer's disease and related tauopathies and as pharmaceutical compositions for the treatment of such conditions.

Nucleic acids encoding mutant elongation factor proteins (EF-Sep), phosphoseryl-tRNA synthetase (SepRS), and phosphoseryl-tRNA (tRNASep) and methods of use in site specific incorporation of phosphoserine into a protein or polypeptide are described. Typically, SepRS preferentially aminoacylates tRNASep with O-phosphoserine and the tRNASep recognizes at least one codon such as a stop codon. Due to the negative charge of the phosphoserine, Sept-tRNASep does not bind elongation factor Tu (EF-Tu). However, mutant EF-Sep proteins are disclosed that bind Sep-tRNASep and protect Sep-tRNASep from deacylation. In a preferred embodiment the nucleic acids are on vectors and are expressed in cells such as bacterial cells, archeaebacterial cells, and eukaryotic cells. Proteins or polypeptides containing phosphoserine produced by the methods described herein can be used for a variety of applications such as research, antibody production, protein array manufacture and development of cell-based screens for new drug discovery.

Compositions and methods for inducing immune tolerance to proteins and subsequence administration of the proteins are disclosed. Compositions comprise proteins complexed with liposomes comprising PS and PC, wherein at least part of the PS is present as lyso-PS.

The present invention relates to a microorganism, wherein the activity of a polypeptide capable of exporting O-phosphoserine (OPS) is enhanced, and a method of producing O-phosphoserine, cysteine, or a cysteine derivative using the microorganism.

The present invention relates to a method for producing cysteine or derivatives thereof using novel O-phosphoserine sulfhydrylase. According to the present invention, a method for producing cysteine by novel O-phosphoserine sulfhydrylase (OPSS) using O-phosphoserine as a substrate is provided, and this method is advantageous in that cysteine can be simply and environmental-friendly produced in a high yield.

A mutant SepRS which is suitable for a site-specific introduction of phosphoserine into a protein is prepared by analyzing the structure and functions of a phosphoseryl-tRNA synthetase (SepRS) derived from an archaebacterium. A mutant SepRS composed of an amino acid sequence depicted in SEQ ID NO:2, in which any one or more of glutamic acids at position-418 and position-420 and threonine at position-423 are substituted with other amino acid, and having enhanced binding affinity with a suppressor tRNA as compared with a wild type phosphoseryl-tRNA synthetase (SepRS) composed of an amino acid sequence depicted in SEQ ID NO:2 is provided.

The invention belongs to the technical field of milk products, and specifically relates to a preparation method of milk powder for infants. According to the milk powder for the infants, cow milk is used in replacement of breast milk. The cow milk mainly contains casein, beta-casein and [alpha]<s>-casein while the breast milk mainly contains beta-casein and no [alpha]<s>-casein; however, the cow milk is difficult for the infants to digest and absorb due to the [alpha]<s>-casein. And thus, pretreatment is performed on skimmed cow milk. The [alpha]<s>-casein comprises phosphoserine groups, so that, the [alpha]<s>-casein carries net negative charges under alkaline conditions; and thus, the [alpha]<s>-casein has high affinity for calcium ions, and is more likely to precipitate. And therefore, the content of [alpha]<s>-casein in the pretreated cow milk is further reduced so as to make the cow milk easier to digest and absorb; moreover, casein in the cow milk is modified by enzymes extractedfrom egg white so that amido bonds formed by carboxyl of hydrophobic amino acids are primarily catalyzed, and thus, peptide bonds in protein molecules are hydrolyzed so as to produce polypeptides withrelatively small molecular weight. In addition, the prepared milk powder for the infants has certain disease-preventing and disease-resisting functions; and thus, allergenicity of cow milk protein isreduced while safety of the milk powder for the infants is improved.