388 results about "Human proteins" patented technology

The invention provides human protein modification and maintenance molecules (PMMM) and polynucleotides which identify and encode PMMM. The invention also provides expression vectors, host cells, antibodies, agonists, and antagonists. The invention also provides methods for diagnosing, treating, or preventing disorders associated with aberrant expression of PMMM.

Multiplexed lateral flow assays, related methods, and devices are disclosed which are capable of simultaneously detecting multiple analytes. The assays are preferably immunoassays and can be multiplexed spatially, spectrally, and both spatially and spectrally. Multiplexed assays are disclosed employing quantum dots for applications including the detection of human proteins and the monitoring of microorganisms relevant to water contamination. The multiplexed assays can employ one or more species of Surface Enhanced Raman Scattering nanoparticles, with one or more species having a unique Raman shift spectrum. The invention is widely adaptable to a variety of analytes such as biowarfare agents, human clinical markers, and other substances.

The present disclosure relates to compounds effective as human protein tyrosine phosphatase beta (HPTP-β) inhibitors thereby regulating angiogenesis. The present disclosure further relates to compositions comprising said human protein tyrosine phosphatase beta (HPTP-β) inhibitors, and to methods for regulating angiogenesis.

The current invention involves a series of fully recombinant multimerized forms of immunoglobulin Fc which thereby present polyvalent immunoglobulin Fc to immune cell receptors. The fusion proteins exist as both homodimeric and highly ordered multimeric fractions, termed stradomers. In comparison to the homodimeric fraction, purified multimeric stradomers have higher affinity and avidity for Fc Rs with slower dissociation and are useful in the treatment and prevention of disease. The current invention demonstrates that directly linking IgG1 Fc regions to multimerization domains leads to enhanced multimerization and biological activity.

The transmembrane human protein thrombomodulin (TM), as a critical regulator of the protein C pathway, represents the major anticoagulant mechanism that is operative in both normal and injured blood vessels under physiologic conditions in vivo. Compositions and methods are disclosed relating to thrombomodulin derivatives and conjugates, including methods for site-specific pegylation and compositions of a truncated thrombomodulin derivative.

Transgenic chloroplast technology could provide a viable solution to the production of Insulin-like Growth Factor I (IGF-I), Human Serum Albumin (HSA), or interferons (IFN) because of hyper-expression capabilities, ability to fold and process eukaryotic proteins with disulfide bridges (thereby eliminating the need for expensive post-purification processing). Tobacco is an ideal choice because of its large biomass, ease of scale-up (million seeds per plant), genetic manipulation and impending need to explore alternate uses for this hazardous crop. Therefore, all three human proteins will be expressed as follows: a) Develop recombinant DNA vectors for enhanced expression via tobacco chloroplast genomes b) generate transgenic plants c) characterize transgenic expression of proteins or fusion proteins using molecular and biochemical methods d) large scale purification of therapeutic proteins from transgenic tobacco and comparison of current purification/processing methods in E. coli or yeast e) Characterization and comparison of therapeutic proteins (yield, purity, functionality) produced in yeast or E. coli with transgenic tobacco f) animal testing and pre-clinical trials for effectiveness of the therapeutic proteins. Mass production of affordable vaccines can be achieved by genetically engineering plants to produce recombinant proteins that are candidate vaccine antigens. The B subunits of Enteroxigenic E. coli (LTB) and cholera toxin of Vibrio cholerae (CTB) are examples of such antigens. When the native LTB gene was expressed via the tobacco nuclear genome, LTB accumulated at levels less than 0.01% of the total soluble leaf protein. Production of effective levels of LTB in plants, required extensive codon modification. Amplification of an unmodified CTB coding sequence in chloroplasts, up to 10,000 copies per cell, resulted in the accumulation of up to 4.1% of total soluble tobacco leaf protein as oligomers (about 410 fold higher expression levels than that of the unmodified LTB gene). PCR and Southern blot analyses confirmed stable integration of the CTB gene into the chloroplast genome. Western blot analysis showed that chloroplast synthesized CTB assembled into oligomers and was antigenically identical to purified native CTB. Also, GM1,-ganglioside binding assays confirmed that chloroplast synthesized CTB binds to the intestinal membrane receptor of cholera toxin, indicating correct folding and disulfide bond formation within the chloroplast. In contrast to stunted nuclear transgenic plants, chloroplast transgenic plants were morphologically indistinguishable from untransformed plants, when CTB was constitutively expressed. The introduced gene was stably inherited in the subsequent generation as confirmed by PCR and Southern blot analyses. Incrased production of an efficient transmucosal carrier molecule and delivery system, like CTB, in transgenic chloroplasts makes plant based oral vaccines and fusion proteins with CTB needing oral administration a much more practical approach.

The present disclosure relates to compounds effective as human protein tyrosine phosphatase beta (HPTP-β) inhibitors thereby regulating angiogenesis. The present disclosure further relates to compositions comprising said human protein tyrosine phosphatase beta (HPTP-β) inhibitors, and to methods for regulating angiogenesis.

The present invention provides methods for efficiently generating and screening protein libraries for optimal proteins with desired biological functions, such as improved binding affinity for biologically and/or therapeutically important target molecules. The method is performed in silico in a high-throughput fashion by mining the ever-expanding database of protein sequences in all living things, especially humans. In one embodiment, a method of constructing a designer protein library comprises the steps of: providing an amino acid sequence derived from a lead protein, referred to as a lead sequence; comparing the lead sequence with a plurality of test protein sequences; Select at least two peptide fragments having at least 15% sequence identity with the leader sequence from each test protein sequence, and the selected peptide fragments form a selection library; a library of designed proteins is formed by replacing the leader sequence with the selection library. Libraries of designed proteins can be expressed in vitro or in vivo to generate libraries of recombinant proteins that can be screened for new or improved functions relative to lead proteins, such as antibodies against a therapeutically important target.

Antibodies and antigen binding fragments thereof that bind to human protein tyrosine phosphatase beta (HPTPβ), and uses thereof.

The present disclosure relates to compounds effective as human protein tyrosine phosphatase beta (HPTP-β) inhibitors thereby regulating angiogenesis. The present disclosure further relates to compositions comprising said human protein tyrosine phosphatase beta (HPTP-β) inhibitors, and to methods for regulating angiogenesis.

The invention relates to a method and a system for predicting a protein interaction target point of a drug. The method comprises: 1) collecting a human protein interaction network and single protein target point data of the drug, and constructing an interactive protein target point data set of the drug; 2) obtaining description data of the drug and proteins; 3) constructing a bigraph for representing an interactive relationship between the drug and a protein pair, constructing a similar matrix for representing drug similarity and protein pair similarity, establishing a kernel function for correlating the similar matrix of the drug and the protein pair, and establishing a prediction model through a machine learning algorithm; and 4) performing independent set testing by utilizing unknown drug and interactive protein pair, and predicting a possibly existent unknown drug protein interaction target point, and verifying a prediction result through database and document retrieval. According to the method and the system, the search space of the drug target point can be expanded and the more specific drug protein interaction target point with the best classification performance can be obtained.

The present invention provides humanized viral vectors and methods of use thereof for delivery of transgenes or therapeutic nucleic acids to human subjects. Humanized viral vectors are modified from known viral vectors such as those based on AAV by coating their surface with a human protein such as human serum albumin and optionally a lipid coating or formulation, so that the foreign or non-human nature of the vector is masked. The coating is performed in a manner that reduces or prevents binding of antibodies to the vector surface, thereby reducing or preventing antibody-mediated clearance of vector, but still allowing the vector to transduce target cells and achieve therapeutic gene transfer. Such humanized vectors therefore evade pre-existing immune surveillance, reduce immune responses, and achieve therapeutic gene transfer in the presence of pre-existing antibodies to the viral vector.