34 results about "Protein Sa" patented technology

Production of a lipidated protein in an E. coli strain adapted to membrane protein expression.

A protein which inhibits osteoclast differentiation and / or maturation and a method of production of the protein. The protein is produced by human embryonic lung fibroblasts and has molecular weight of about 60 kD and about 120 kD under non-reducing conditions and about 60 kD under reducing conditions on SDS-polyacrylamide gel electrophoresis, respectively. The protein can be isolated and purified from culture medium of the said fibroblasts. Furthermore, the protein can be produced by gene engineering. The present invention includes cDNA for producing the protein by gene engineering, antibodies having specific affinity to the protein or a method for determination of the protein concentration using the antibodies.

A fast and sensitive method and device for protein sequencing are disclosed. The method uses a combination of Edman degradation chemistry and mass spectrometry to sequence proteins and polypeptides. A peptide degradation reaction is performed on a polypeptide or protein ion reactant in the gas phase. The reaction yields a first ion product corresponding to a first amino acid residue of the polypeptide or protein reactant and a polypeptide or protein fragment ion. The mass-to-charge ratio for the first ion product, or the polypeptide or protein fragment ion, or both, is then determined. The first amino acid residue of the polypeptide or protein reactant is then identified from the mass-to-charge ratio so determined.

The present invention provides screening methods for agonists or antagonists of Sema6C using Plexin-A1, and tools for the screening and the like. It evaluates a case of making a recombinant protein having an extracellular domain of Semaphorin 6C contact a protein having an extracellular domain of Plexin-A1 by comparing it with a case of contacting a recombinant protein and a target substance having an extracellular domain of Semaphorin 6C, or the target substance with a protein having an extracellular domain of Plexin-A1. The evaluation will be carried out by the connectivity of a protein having an extracellular domain of Semaphorin 6C, a growth cone collapse activity of Plexin-A1 expressing cell, or a contractile activity of Plexin-A1 expressing cell.

The invention relates to a recombinant protein fabricated in a baculovirus system, of which the essential constitutive polypeptide sequence is that of a C-terminal fragment of 19 kilodalton (p19) of the surface protein 1 (protein MSP-1) of the merozoite parasite of the Plasmodium type, particularly Plasmodium falciparum, which is infectious for humans, said C-terminal fragment remaining normally anchored at the surface of the parasite at the end of its penetration phase into human erythrocytes, in the occurrence of an infectious cycle. Said recombinant protein is applicable to the production of vaccines against malaria.

The invention relates to an L-glutamate oxidase gene from Afghanistan streptomyces and an application thereof and in particular relates to a recombinant bacterium which is obtained by screening Afghanistan streptomyces capable of generating L-glutamate oxidase from soil, cloning and coding the L-glutamate oxidase gene from the bacterium by a homological cloning method and artificially synthesizing the gene and recombining the gene in an escherichia coli and has the activity of L-glutamate oxidase. The nucleotide sequence of the L-glutamate oxidase gene is SEQ ID No 1, the full length of the L-glutamate oxidase gene is 2073bp, and a coding protein sequence of the L-glutamate oxidase gene is SEQ ID No 2. L-glutamate oxidase coded by the gene can be used for specifically catalyzing L-glutamic acid, can serve as an enzyme for detecting the content of L-glutamic acid and is applied to the fields of the food industry and clinical biochemical detection.

Described herein are methods for increasing the amount of protein secreted by a cell. In one case, a cell is provided which contains a heterologous nucleic acid encoding a protein having unfolded protein response modulating activity and a heterologous nucleic acid encoding a protein of interest to be secreted. In one case, the protein having unfolded protein response modulating activity is selected from the proteins selected from the group consisting of HAC1, PTC2 and IRE1. The protein of interest can be any secreted protein such as a therapeutic or an industrial enzyme. For example the protein can be selected from the group consisting of lipase, cellulase, endo-glucosidase H, protease, carbohydrase, reductase, oxidase, isomerase, transferase, kinase, phosphatase, alpha-amylase, glucoamylase, lignocellulose hemicellulase, pectinase and ligninase.

The invention discloses a malus xiaojinensis Cheng et Jiang MxHA5 protein, and a coding gene and application thereof. The protein provided by the invention is protein (a) or protein (b), wherein the protein (a) has amino acid sequences shown as a sequence 1 in a sequence table; and the protein (b) has an amino acid residue sequence which is derived from the sequence 1 by substituting and / or losing and / or adding one or more amino acid residues and is related with the P type H<+>-ATPase enzymatic activity in plant. The MxHA5 protein provided by the invention has an important effect of adjusting ion-deficient stressed plant, and the invention further provides good theoretical basis for the research on the ion-deficiency resistance of malus xiaojinensis Cheng et Jiang, and has significance to cultivation of stress-tolerant plant.

The invention discloses a lonicera japonica thunb phenylalanine ammonia-lyase (LJPAL) gene as well as a protease coded by the same and application of the gene. The LJPAL gene has nucleotide sequences shown in SEQ ID NO.1 or homologous sequences obtained through addition, substitution, insertion or deletion of one or a plurality of nucleotides or nucleotide sequences derived from alleles of the gene and the gene. A protein coded by the gene has amino acid sequences shown in SEQ ID NO.2 or homologous sequences obtained through addition, substitution, insertion or deletion of one or a plurality of amino acids.

The present invention discloses an earthnut acetyl coenzyme A carboxylase carboxyltransferase beta subunit gene and an encoding protein and a cloning method thereof. The gene sequence is composed of a nucleotide sequence from 92th to 1570th bits of SEQ ID No.1; the protein encoded by the gene has an amino acid sequence represented by the SEQ ID No.2 in a sequence table. The nucleotide sequence of the earthnut acetyl coenzyme A carboxylase carboxyltransferase beta subunit (AhCT beta) gene and the encoding protein sequence and the gene cloning method of the invention may be used for improving the earthnut quality and the earthnut cultivation widely, especially a field where the earthnut is used for developing and using oil crops.

A method for determining an optimized nucleotide sequence encoding a predetermined amino acid sequence, wherein the nucleotide sequence is optimized for expression in a host cell, and wherein the method comprises the steps of: (a) generating a plurality of candidate nucleotide sequences encoding the predetermined amino acid sequence; (b) obtaining a sequence score based on a scoring function based on a plurality of sequence features that influence protein expression in the host cell using a statistical machine learning algorithm, wherein the plurality of sequence features comprises one or more sequence features selected from the group consisting of protein per time, average elongation rate and accuracy for each of the plurality of candidate nucleotide sequences of step (a); and (c) determining the candidate nucleotide sequence with optimized protein expression in the host cell as the optimized nucleotide sequence.

Described herein are viral amplicon-based protein expression systems and methods useful for producing heterologous proteins, such as enzymes, by agroinfiltration. The methods involve producing an Agrobacterium with a Ti plasmid encoding a heterologous protein, infecting plant cells with the Agrobacterium, allowing expression of the heterologous protein, and recovering the heterologous protein from the plant cells. In one embodiment, the protein produced is an endoglucanase.

The invention relates to a high-vitality cellulose endonuclease artificially synthetic gene shown in a nucleotide sequence in SEQ ID NO.1 in a sequence table or a sequence which has 90% homology or above and coding the same biological functional protein with the nucleotide sequence shown in the SEQ ID NO.1. The nucleotide sequence shown in the SEQ ID NO.1 in the sequence table can use pichia pastoris constitutive expression plasma pGAPZaA as a vector and realize high-level recombination expression of target protein in pichia pastoris host bacteria X33. Meanwhile, a screened high-level expression transformant can realize high-level secretion of recombinant protein by use of inorganic salt high-density fermentation, and by simple nickel affinity chromatography purification, a novel recombinant cellulose endonuclease protein pure product with high vitality can be obtained. The recombinant protein has very high capacity for hydrolyzing cellulose substances and producing glucose and has important application value in biological energy source, feed and food industries.

The invention discloses a prokaryotic expression vector pET28a-PADH for efficiently expressing Pseudomonas putida glutathione-independent formaldehyde dehydrogenase protein. The vector is a prokaryotic expression vector containing a Pseudomonas putida glutathione-independent formaldehyde dehydrogenase gene (PADH). In the invention, the PADH gene is cloned from Pseudomonas putida, and the expression of the PADH gene in colon bacillus is controlled by using a T7 promoter; 40 percent of expressed recombinant protein exists in a supernate in a soluble mode (accounting for 30 percent of soluble total protein of the colon bacillus), and 60 percent of expressed recombinant protein exists in an inclusion body; the high-purity PADH recombinant protein can be easily obtained from the upper inclusion body through tapping and purification and can be used as an antigen used for preparing a PADH specific antibody. The PADH recombinant protein with activity can be easily purified from the soluble total protein of the colon bacillus by affinity chromatography and is used for the production and the physiological-biochemical characteristic analysis of PADH enzyme preparations.

The invention relates to endo-glucanase with immune-enhancing activity and nucleotide sequences of genes coding the endo-glucanase, and belongs to the technical field of biology. The invention provides a beta-1,3 endo-glucanase protein sequence and nucleotide sequences of genes of beta-1,3 endo-glucanase. Beta-1,3 endo-glucanase is one of key enzymes in a glucan hydrolytic enzyme system. The beta-1,3 endo-glucanase is from Arca inflata Reeve, 333 amino acids are included, the total length of corresponding coding gene nucleotide is 999 bp, the content of (G+C) is 39.34%, and a novel glucan hydrolytic enzyme resource is achieved. Engineered strains constructed by using the enzyme gene nucleotide can high-efficiently express the beta-1,3 endo-glucanase, a Kd value of the beta-1,3 endo-glucanase is 13.09 muM when laminarin is used as a substrate, produced enzymic preparations can be used for food industry, medicine industry, fodder industry, washing industry and other industries, the problem of recycling of biomass waste being rich in glucan can be solved, and rich glucosyl-oligosaccharides can be obtained to generate considerable economic benefits.

The present invention provides nucleic acid sequences encoding a modified leukotoxin protein, wherein the modification comprises the removal of nucleic acid sequences encoding amino acids within hydrophobic transmembrane domains of full length leukotoxin protein, preferably from Mannheimia haemolytica. The modified leukotoxin proteins are useful in vaccine compositions effective against Mannheimia haemolytica in animals.

The present invention relates to sperm specific surface proteins, nucleic acid sequences encoding those proteins and antibodies raised against those proteins. Compositions comprising the sperm specific proteins or inhibitors of said proteins can be used in contraceptive applications.

The invention belongs to the technical field of biology, particularly belongs to the field of genetic engineering, and more particularly relates to UGD gene in kelp, protein thereof and application. the UGD gene is from the kelp and is named as SjaUGD gene, and a nucleotide sequence of the SjaUGD gene is a sequence shown as SEQ ID NO:1. The invention further provides GDP-mannose-6-dehydrogenase which is coded by the SjaUGD gene, an amino acid sequence of GDP-mannose-6-dehydrogenase is a sequence shown as SEQ ID NO:2 while specific activity of the same is 7.99nanokatals.mg-1, and GDP-mannose-6-dehydrogenase has wider optimum reaction temperature range and higher thermostability. Excellent gene resources and enzyme resources are provided for biological preparation of algin.

The invention discloses application of protein AxMan113A as beta-mannase. The protein AxMan113A provided by the invention is protein with an amino acid sequence shown as a sequence 2 in a sequence table or protein with an amino acid sequence shown as a sequence 4 in the sequence table. Proved by experiments, the protein AxMan113A has the activity of the beta-mannase, so that vegetable gum, such aslocust bean gum and konjac powder, with rich mannan can be hydrolyzed in a high-efficiency manner; meanwhile, the protein AxMan113A has good acid resistance, heat resistance and hydrolysis characteristic, and is obviously different from the existing beta-mannase. The protein AxMan113A and an encoding gene of the protein AxMan113A have important economic value and practical significance in the industries of foods, feed and the like.

A recombinant microorganism having improved productivity for a protein or a polypeptide, and a method for producing a protein or a polypeptide using the recombinant microorganism, are provided. A recombinant microorganism obtained by transfecting a gene for encoding a desired protein or polypeptide into a microorganism strain which is obtained by genetically constructing to overexpress secY gene of Bacillus subtilis or a gene corresponding to the secY gene, and deleting or inactivating one or more genes selected from sporulation-associated genes and genes corresponding to the sporulation-associated genes from the genome.

The invention discloses dermatophagoides farina allergen Der f9 gene recombinant protein and application thereof. The amino acid sequence of the recombinant protein is shown in SEQ ID No:2. The invention further discloses a preparation method and application of the recombinant protein. The dermatophagoides farina allergen Der f9 gene recombinant protein and the preparation method and application thereof have the advantages that a dermatophagoides farina allergen Der f9 full-length gene sequence is obtained, the recombinant protein is prepared according to the gene sequence, and the coded recombinant protein is high in purity, good in specificity and high in yield. The dermatophagoides farina allergen Der f9 gene recombinant protein can be applied to diagnosing whether a patient suffers from allergic diseases caused by a dermatophagoides farina allergen ninth component.

The present invention relates to one method of detecting serum protein fingerprint of esophagus cancer. The serum protein fingerprint is obtained through collecting human serum, combining human serum with weak cationic affinity protein chip, reading serum protein map in mass spectrograph and analyzing the map data with protein fingerprint analyzing software. The serum protein fingerprint of esophagus cancer consists of 12 proteins with different mass-to-charge ratios. The serum protein fingerprint of esophagus cancer the present invention provides may be used in the early detection of esophagus cancer and has sensitivity and specificity over 80 %.

A general method and recombinant nucleic acid sequences, by means which the method selects a recombinant protein containing an FHA domain for binding a target molecule from a library proteins with a high-throughput method of creating protein variations within the FHA domain in non-conserved or non-structural sequences of the FHA scaffold, and the library may also be in the form of a phagemid or phage library wherein the ALP nucleic acid sequence is inserted into a vector capable of allowing the vector and expressed ALP protein from being virally packaged, and the recombinant nucleic acid sequences which are randomly mutated at varying non-conserved or non-structural FHA domain sequences.

Alpha 1-antitrypsin is prepared by growing in a fermentor methylotropic yeast transformants containing in their genome at least one copy of DNA encoding alpha 1-antitrypsin, in operational linkage with DNA encoding a signal sequence, which is effective for directing secretion of proteins from the host cells, DNA constructs and recombinant yeast strains used for the expression and secretion of alpha 1-antritrypsin are also provided. The fermentation medium requires a pH of 6.5 to 7.5. The fermentation is at a pH between 5 and 6.8.