34 results about "Protein Sa" patented technology

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.

A recombinant protein is prepared comprising a polypeptide of interest and a starch binding domain (SBD). The said SBD is obtainable from glucoamylase of fungi genus Rhizopus. The said recombinant protein comprising the said SBD can be purified by contacting with an affinity matrix such as starch, the SBD binds to the affinity matrix to isolate the recombinant protein. The recombinant protein can be purified by separating the association between the SBD and the affinity matrix by acid, alkaline, salt, or sugar. The polypeptide of interest may be an antibody, an antigen, a therapeutic compound, an enzyme, or a protein and may apply in pathogen destruction, vaccine producing, and oral care product manufacturing. The SBD further provides as a tool to screen or identify polysacchrides.

It is intended to provide a host microorganism capable of increasing productivity of a protein or a polypeptide; a recombinant microorganism obtained by introducing a gene encoding a protein or a polypeptide into the host microorganism; and a process for producing a protein or a polypeptide using the recombinant microorganism. The recombinant microorganism is prepared by using a microorganism, in which aprX gene of Bacillus subtilis or a gene corresponding to the gene has been deleted or inactivated, as a host and introducing a gene encoding a heterologous protein or polypeptide into the host. The recombinant microorganism is used in the process for producing a protein or a polypeptide.

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.

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.

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.

A recombinant microorganism is provided that has increased productivity of a protein or polypeptide of interest. A method for producing a protein of interest using the microorganism is also provided. The microorganism is prepared by inserting, in its genome, a transcription initiation regulatory region or both a transcription initiation regulatory region and a ribosome-binding site, upstream of a Bacillus subtilis prsA gene and by deleting or inactivating one or more of the abrB gene, dltA gene, dltB gene, dltC gene, dltD gene, dltE gene, or a gene (genes) corresponding thereto.

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 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 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.

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.

The invention relates to the field of biotechnology, and in particular relates to a cDNA (Complementary Deoxyribose Nucleic Acid) nucleotide of monascus ruber GAD (Glutamic Acid Decarboxylase) gene and a synthetic method thereof, and a corresponding protein. The base sequence of the nucleotide at the coding region of monascus ruber glutamic acid decarboxylase gene is shown as SEQ ID NO: 1. According to the cDNA nucleotide of monascus ruber GAD gene and the synthetic method thereof and the corresponding protein, the complete nucleotide sequence at the cDNA coding region of monascus ruber GAD (Glutamic Acid Decarboxylase) gene is cloned, the nucleotide can be applied to the immune prediction and early diagnosis of Type 1 Diabetes Mellitus, and GABA (Gamma-Aminobutyric Acid) can be prepared by using the biocatalysis of the nucleotide, thus having multiple applications and wide application prospect.