180 results about "Chaperonin" patented technology

The present invention is based on the discovery that three proteins, Cystatin B, Chaperonin 10, and Profilin are present in the urine of patients with bladder cancer, a cancer of epithelial origin. Accordingly, the present invention is directed to methods for prognostic evaluation of cancers of epithelial origin and to methods for facilitating diagnosis of cancers of epithelial origin by monitoring the presence of these markers in biological samples. The invention is also directed to markers for therapeutic efficacy.

Engineered binding proteins are provided. In some cases, the parent protein corresponding to the engineered protein has a three-layer swiveling beta/beta/alpha domain. In other cases, the parent protein corresponding to the engineered protein has a rubredoxin-like fold. At least one portion of the primary sequence of the engineered protein is determined by an engineering scheme. In some case, the engineered protein is characterized by an ability to bind to a compound that the parent protein does not bind. In some cases, the parent protein is derived from a domain of a chaperonin or a rubredoxin. One form of engineering scheme used is a randomization scheme. A method for making libraries of engineered proteins, all based on a single parent protein is provided. Methods to identify proteins that bind to compounds of interest in libraries of engineered libraries is provided. An array of engineered proteins immobilized on a support is provided. Each engineered protein in the array is a chaperonin domain or a rubredoxin that has been subjected to an engineering scheme.

Introducing blocks of foreign genes in a single operon would avoid complications such as position effect and gene silencing inherent in putting one gene at a time into random locations in the nuclear genome. Cloning several genes into a single T-DNA does not avoid the compounded variable expression problem encountered in nuclear transgenic plants. This disclosure shows that a bacterial operon can be expressed in a single integration event as opposed to multiple events requiring several years to accomplish. Expression of multiple genes via a single transformation event opens the possibility of expressing foreign pathways or pharmaceutical proteins involving multiple genes. Expressing the Cry2aA2 operon, including a putative chaperonin to aid in protein folding, in the chloroplast via a single transformation event leads to production of crystalized insecticidal proteins. Expressing the Mer operon via a single transformation event leads to a phytoremediation system.

The present invention relates conotoxin peptides that are analogs of the α-contoxin peptide RgIA. These conotoxin peptides block the α9α10 subtype of the nicotinic acetylcholine receptor (nAChR) and can be used for treating pain, such as neuropathic pain and inflammatory pain, inflammatory disorders, such as rheumatic diseases, and in the treatment of breast cancer.

The invention relates to a method for biosynthesis preparation of human glucagon-like peptide-1 (GLP-1) and an analogue thereof. With adopting of a gene engineering technology, a recombinant escherichia coli expressed GLP-1 fusion protein is constructed, and a protein enzyme digestion site is designed in the fusion protein; a fusion gene has a gene sequence with a form of A-B-C structure, wherein A is a chaperonin gene, B is a nucleotide sequence encoding a connection peptide containing the enzyme digestion site, and C is a gene encoding the GLP-1 or the analogue thereof. After recombinant engineering bacteria is subjected to induced expression, the fusion protein is purified and subjected to enzyme digestion, and then the GLP-1 and the analogue thereof are obtained and are detected to have biological activity. The preparation method of the GLP-1 and the analogue thereof provided by the invention is simple and quick, the production conditions are mild, the product is convenient to separate and extract, the process is simple, and the industrialization prospect is good.

Focused acoustic treatment of samples including a target biomolecule, such as cfDNA, may aid in the recovery of the biomolecule from a sample. cfDNA in a sample, whether chemically stabilized or not, may be linked or otherwise bound to histones or other proteins, e.g., by hydrogen bonds of histones or chaperone proteins to DNA and/or covalent crosslinks of such proteins to the DNA. Focused acoustic energy may remove or disrupt such links, aiding in isolation of the cfDNA from the sample.

The present invention provides a chaperonin-target protein complex and a method of producing the same, and a method of stabilizing the target protein, a method of immobilizing the target protein, a method of analyzing the structure of the target protein, a sustained-release formulation, and a method of producing an antibody against the target protein. The chaperonin-target protein complex in the present invention includes a fusion protein having a chaperonin subunit and an affinity tag linked to the chaperonin subunit via a peptide bond and a target protein for which the affinity tag shows a specific affinity, wherein the target protein is bound to the affinity tag by means of the specific affinity, thereby forming a chaperonin ring structure consisting of a plurality of chaperonin subunits. The chaperonin-target protein in the present invention stabilizes the target protein and surely immobilize on a carrier without causing any change in its stereostructure.

Desirable fusion proteins can be produced in and purified from the milk of transgenic animals. The peptides are made as fusion proteins with a suitable fusion partner such as human alpha-fetoprotein. The fusion partner protein acts to promote and increase the half-life of the overall molecule as well as having therapeutic effects on its own. The fusion protein is typically produced through the use of transgenic animals and can be purified away from the now the milk or other bodily fluid of such an animal by an affinity purification method. A particular advantage of producing peptides via this route, in addition to the obvious advantages of high yield and biocompatibility, is that specific post-translational modifications, such as carboxy terminal amidation, can be performed in the mammary gland. Biologically active polypeptides comprising a therapeutically active polypeptide fused to human alpha-fetoprotein fragment or a variant thereof, methods for the preparation thereof, nucleotide sequences encoding such fusion polypeptides, expression cassettes comprising such nucleotide sequences, self-replicating plasmids containing such expression cassettes, and pharmaceutical compositions containing said fusion polypeptides.

Protein antigens are provided. The protein antigens typically include a peptide antigen conjugated or fused to a chaperone protein to form a “chaperone-antigen” that increases lymph node uptake; improves an immune response; or a combination thereof relative to the peptide antigen alone. The immune response can be, for example, increased antigen-specific proliferation, enhanced cytokine production, stimulation of differentiation and/or effector functions, promotion of survival, rescue from exhaustion and/or anergy of T cells, or a combination thereof. Chaperon-antigens can also be used to induce tolerance and increase immune suppressive responses. In the most preferred embodiments, the peptide antigen is fused to the chaperone protein to form a fusion protein. The “chaperone-antigen” can be combined with an adjuvant to form a vaccine and administered to a subject to modulate an immune response to the antigen. Methods of increasing immune responses, treating cancer and infectious and inducing tolerance are also provided.

The present invention provides methods for efficient and concomitant recovery of multiple chaperone proteins and/or chaperone protein complexes from a limited sample source. Disclosed are methods involving the use of Free Solution Iso-Electric Focusing (FS-IEF) which can enrich samples containing chaperone proteins and/or chaperone protein complexes from a given sample. The chaperone proteins can be, but are not restricted to calreticulin, gp96, hsp86, hsp84, hsp70, hsp60 and hsp40. The invention also provides methods of recovering chaperone protein complexes for the preparation of vaccines containing chaperone complexes.

The invention provides a method for soluble expression of recombinant protein of a human brain natriuretic peptide (Human Brain Natriuretic Peptide, hBNP). The method comprises the following steps: 1) obtaining a recombinant gene, namely obtaining the recombinant gene His-DsbAmut-BNP of expressing the recombinant protein of the human brain natriuretic peptide, wherein the sequence of the recombinant gene comprises a purified tag gene sequence, a molecular chaperone protein gene sequence, a protease recognition site sequence and a human brain natriuretic peptide sequence, which are sequentially arranged along the direction from 5' to 3'; 2) obtaining recombinant plasmids, namely inserting the recombinant gene obtained in the previous step into a carrier vector, so as to obtain the recombinant plasmids containing the recombinant gene; 3) obtaining genetically engineered bacterium, transferring the recombinant plasmids obtained in the previous step into host cells to obtain the genetically engineered bacterium; 4) expressing exogenous genes, fermenting the genetically engineered bacterium, and expressing fusion protein containing the human brain natriuretic peptide; 5) purifying target protein, splitting thallus, collecting fusion protein, removing molecular chaperone and carrying out chromatographic purification by protease digestion, so as to obtain the recombinant protein of the human brain natriuretic peptide.

A recombinant genome comprising polynucleotides encoding at least two additional molecular chaperones and a protein of interest, recombinant baculovirus vectors providing molecular chaperones and a method for producing a foreign protein using said genomes and vectors.

The present invention relates to a method for increased production of a secreted, recombinant protein product through the introduction of molecular chaperones in a mammalian host cell. The present invention also relates to a mammalian host cell with enhanced expression of a secreted recombinant protein product by coexpressing at least one chaperone protein.

The invention relates to an application of chaperonin CCTgamma in preparation of a tumour diagnosis reagent and in particular relates to a new application of the chaperonin CCTgamma in preparation of an osteosarcoma diagnosis reagent. The inventor adopts bioinformatics method analysis for carrying out gene screening based on high-throughput sequencing results, a candidate gene CCTgamma is picked out, and further molecular cell biology experiments prove that CCTgamma has a good correlation with osteosarcoma, can be used for preparing an auxiliary osteosarcoma diagnosis and treatment preparation and has important clinical application value.

This invention provides a means for high-level secretory production of a protein, and, in particular, a protein having a complicated structure such as an antibody, in a host cell such as a yeast cell. This invention provides a method for high-level secretory production of a foreign protein with the use of a transformed host cell having one or more types of chaperone protein genes and via suppression of O sugar chain inherent to a host cell such as a yeast cell.

The present invention relates to polypeptides capable of binding chaperone receptors, composition and methods for protecting, restoring, or improving the physiological properties of sperm cells. More particularly, the invention relates to protection of the motility, survival, fertility capability, resistance to cooling, freezing, and thawing of sperm cells put in contact with chaperone polypeptides.

The invention provides a polygene coexpression system which comprises an expression vector of disulfide-bond target protein coding genes, and one or more than one expression vector of coding genes of an enzyme and/or chaperonin which has the effect of promoting the functionalization of disulfide-bond target protein; the coding genes of the enzyme and/or chaperonin are constructed in one reading frame of the expression vector in a form of fusion genes, or two or more than two of the coding genes of the enzyme and/or chaperonin are respectively constructed in different reading frames of the expression vector; the coding genes of the target protein are constructed in an expression vector which contains different resistant genes from the expression vector of the enzyme and/or chaperonin. The invention also provides a preparation method of the polygene coexpression system, and a method for preparing soluble functional target protein by using the preparation method. The polygene coexpression system of the invention enables the expressed disulfide bond-containing protein to form correct disulfide bonds, to fold into correct spatial conformation, and thus to dissolve in a cracking supernatant with maintained corresponding biological functions or activity.

The present invention provides a method for producing heterologous protein comprising: (a) providing a host cell comprising a 2 μm-family plasmid, the plasmid comprising a gene encoding a protein comprising the sequence of a chaperone protein and a gene encoding a heterologous protein; (b) culturing the host cell in a culture medium under conditions that allow the expression of the gene encoding the chaperone protein and the gene encoding a heterologous protein; (c) purifying the thus expressed heterologous protein from the cultured host cell or the culture medium.