12 results about "THROMBIN HUMAN" patented technology

This invention provides 19 F-PDA-DNA-DTPA / Gd nanosensing probe, its preparation method, and its application in fluorine magnetic resonance imaging: This nanosensing probe consists of an MR signal source, a quencher, and a response linker. The MR signal source is a high-density fluorine perfluorocarbon nanoparticle, the quencher is Gd-DTPA, and the response linker is a DNA aptamer composed of a single-stranded DNA S1 and its complementary strand S2, with nucleotide sequences shown in SEQ ID NO.1 and SEQ ID NO.2. As a responsive nanoparticle platform, it is only visible upon activation by a specific biological trigger. Its biological application is demonstrated by targeting thrombin with the aptamer and exhibiting a strong and selective response to thrombin in live mice.

Therapeutic antibodies specific for osteopontin and methods of using them for treating osteopontin-associated disorders are provided. In particular, antibodies, or antigen-binding fragments thereof, that inhibit thrombin-cleavage of osteopontin or block the activity of thrombin cleavage fragments of osteopontin are provided. Additionally, antibody conjugates and pharmaceutical compositions or formulations comprising the antibodies or antibody conjugates as well as kits including the antibodies, conjugates, or formulations are also provided.

The application discloses a preparation device of autologous thrombin, and belongs to the technical field of biomedical engineering, which comprises an activator cylinder and a conducting pipe, a piston head of a piston of the activator cylinder is arranged in an inner container, the inner container is sleeved with an outer cylinder, and a piston seat of the piston is fixedly connected with the outer cylinder. When the outer cylinder is quantitatively moved upward relative to the inner container, the activator in the inner container is pushed by the piston to be added into a test tube through the conducting pipe, so that the activator can be quantitatively added into the test tube, and the added activator can be guaranteed not to be polluted by the outside. The preparation device of autologous thrombin is used to add the activator into centrifuged whole blood to make the whole blood be mixed uniformly, and after standing and contacting, a gel is formed in the mixture, supernatant is formed in the upper part, and the supernatant is sucked to prepare a thrombin solution. The application has the advantages of convenient operation, simple process, effective prevention of external infection, high activity of prepared autologous thrombin and fast gel formation.

The application relates to the technical field of thrombin detection, in particular to a thrombin fluorescent substrate applied to whole blood, a preparation method and application thereof. The thrombin fluorescent substrate comprises a specific recognition peptide chain D-Phe (4-MeSO2)-Pro-Gly-Arg and a fluorescent group. The thrombin fluorescent substrate has high affinity with thrombin, high catalytic efficiency and strong anti-interference capability, and can be widely applied to thrombin detection technology.

The present application belongs to the technical field of polypeptide preparation and biopharmacy, and particularly relates to eggshell membrane polypeptides with thrombin inhibitory activity and application thereof. Two polypeptides are obtained by separation and purification from eggshell membranes, which are nonapeptide YDGQHGRVS and octapeptide EVPPSPAL. It is proved by experiments that the nonapeptide YDGQHGRVS and the octapeptide EVPPSPAL have thrombin inhibitory activity equivalent to that of the positive control heparin sodium, and it is found that the nonapeptide YDGQHGRVS prolongs activated partial thromboplastin time and prothrombin time. The nonapeptide YDGQHGRVS and the octapeptide EVPPSPAL provided by the present application are derived from eggshell membranes, are natural in origin, have good thrombin inhibitory activity, high safety, and have good application prospect.

This invention discloses an earthworm protein peptide with in vitro thrombin-inhibiting activity and its preparation method, belonging to the field of functional food technology. The method first pre-treats earthworm raw materials to obtain earthworm protein; then, it uses pepsin and alkaline protease for stepwise enzymatic hydrolysis under varying temperature and pH, and ultrafiltration to collect short peptide solutions with a molecular weight below 3 kDa; the short peptide solution is specifically captured using an affinity chromatography material coupled with bovine thrombin, followed by elution, nanofiltration desalting concentration, and spray drying to obtain the final product. This invention fully releases the peptides through a dual enzymatic hydrolysis process and utilizes thrombin affinity chromatography to directionally enrich peptides with specific inhibitory activity, effectively solving the problems of low content and poor targeting of active ingredients in earthworm protein peptides in existing technologies, and significantly improving the purity and in vitro anticoagulant activity of the product.

This invention proposes a tPA delivery system based on a tetrahedral DNA origami structure, its preparation method, and its applications, relating to the biomedical field. It includes a carrier composed of a tetrahedral DNA origami structure, a thrombus-targeting peptide, and short-chain DNA. The thrombus-targeting peptide and short-chain DNA are pre-coupled to form a peptide-short-chain complex, which is grafted onto the tetrahedral DNA origami structure. tPA and short-chain DNA are pre-coupled and loaded onto the edges of the tetrahedral DNA origami structure. Using the tetrahedral DNA origami structure as the core carrier, the vertices can be precisely modified with thrombus-targeting peptides to achieve targeting of the thrombus site. The tPA molecule is loaded onto the edges of the DNA origami structure via sulfo-SMCC linkage, and its release is controlled by introducing a thrombin-responsive DNA locking mechanism. This invention overcomes the limitations of current tPA thrombolytic therapy, enabling on-demand release of tPA during treatment, achieving local thrombolysis while reducing the risk of systemic bleeding.

The present disclosure is directed to human protease activated receptor 4 (PAR4) binding proteins (e.g. antibodies). In particular, anti-PAR4 binding proteins which are antagonists of human PAR4, as well as methods and uses thereof.

This invention relates to a recombinant hirudin fusion protein with collagen affinity, its preparation method, and its applications. The fusion protein is a recombinant hirudin fusion protein incorporating a collagen-binding domain (CBD). The fusion protein of this invention possesses affinity for type I and type III collagen, and can inhibit thrombin activity to exert an anticoagulant effect. Furthermore, it can bind well to collagen-based composite materials, making it suitable for use in cardiovascular implants such as heart valves, cardiac occluders, dialysis membranes, oxygenation membranes, artificial blood vessels, and vascular stents, as well as in extracorporeal circulation and blood purification devices, enhancing anticoagulant and antithrombotic effects.

The present application relates to a kind of whole-cell biosensors of E. coli surface display, for realizing the high sensitivity detection of multiple proteases.The sensor is displayed on the surface of E. coli by synthetic biology method and includes anchor module, protease-specific cleavage peptide and fluorescent reporter module of recombinant fusion protein.When target protease exists, its specific cleavage peptide causes fluorescent reporter module to dissociate from cell surface, and fluorescence signal is weakened, and the degree of signal attenuation is positively correlated with protease concentration and activity.The detection sensitivity of the present application is high, and the detection limit of matrix metalloproteinase-2, thrombin and other proteases reaches the level of femtogram per milliliter, which is more than three orders of magnitude higher than traditional methods;It is simple to operate, only needs to be added sample-incubation-detection three steps, and the cost of single detection is less than 0.1 dollar;It can directly detect protease activity in complex biological matrix without expensive antibody, and has good clinical application and large-scale screening potential.