32 results about "Factor XIII" patented technology

A method for treating inflammatory bowel disease by administering interferon beta in conjunction with factor XIII to a mammal afflicted with the disease. The IBD may either be ulcerative colitis or Crohn's disease. The factor XIII used may be recombinant or nonrecombinant. The interferon beta used can be naturally occurring interferon beta, interferon beta-1a or interferon beta-1b.

The invention is related to a process for separating proteins fibrinogen, Factor XIII and biological glue from a solubilized plasma fraction and for preparing freeze-dried concentrates of said proteins comprising the steps of:chromatographic purification comprising the steps of loading an anion exchanger of weak base type with the said solubilized fraction, previously equilibrated with a buffer of a predetermined ionic strength of an alkaline pH, which allows to retain the biological glue, elution of the biological glue by increasing the ionic strength of the said buffer, andseparation of FXIII from fibrinogen by addition to at least one part of the biological glue eluate of at least one chemical agent precipitating the FXIII, and recovery of the resulting purified fibrinogen containing supernatant solution, anddiafiltration of the fibrinogen, biological glue and resolubilized FXIII solutions, followed by a freeze-drying of said solutions.

A method for preparing a highly concentrated fibrinogen solution includes adding amino acid or amino acid derivatives, and / or salts to a lowly concentrated fibrinogen solution, followed by a ultra-filtration concentration. Factor XIII can be added either before or after the ultra-filtration to give a fibrin sealant component 1 containing the highly concentrated fibrinogen solution. The fibrin sealant component 1 could be preserved for a long time at room temperature and be used without a reconstitution. Fibrin sealant component 2 is a solution containing thrombin and calcium. A fibrin sealant product may be provided in a vial type in which the fibrin sealant components 1 and 2 are each filled in separate vials or in a re-filled syringe type wherein the fibrin sealant components 1 and 2 are each filled in separate syringes connected with each other to be instantly used.

The present disclosure provides compositions and methods that are useful for normalizing the amount of signal detected in an assay, such as an immunoassay. The compositions and methods are useful for improving the accuracy of immunoassays, such as immunoassays that detect whether a subject is infected with a retrovirus such as HIV.

Plants have emerged as an alternative expression system and are increasingly being used byindustry and academia for producing target proteins. However, the ability of plants to glycosylate proteins can be a significant limitation for those proteins, which do not require N-glycosylation. For example, Plasmodium falciparum proteins, or A chain of human factor XIII do not carry N-linked glycans, or the protective antigen (PA) of Bacillus anthracisis not a glycoprotein; however, these proteins contain potential N-linked glycosylation sites that can be aberrantly glycosylated during expression in yeast, mammalian, or plant systems, potentially leading to reduced functionality and immunogenicity because of incorrect / altered folding and / or masking of epitopes. To overcome this problem we have recently developed a strategy of enzymatic deglycosylation of proteins in vivo by co-expressing with bacterial PNGase F (Peptide: N-glycosidase F) using transient expression in plants (WIPO Patent Application WO / 2012 / 170678), which allowed production of malaria vaccine candidate Pfs48 / 45, which can provide a high transmission blocking (TB) activity (Mamedov et al., 2012). In addition, other deglycosylated antigens induced significantly higher levels of toxin-neutralizing antibody responses in mice than compared with glycosylated forms (Mamedov et al, manuscript has been submitted). Although a PNGase F treatment (in vivodeglycosylation) removes the oligosaccharide intact, but causes amino acid change in the deglycosylated protein due to deamidation of the asparagine (N) in the NxS / T site (sequence) into an aspartate (D). In this study, a strategy was developed for production of target proteins in plants in non-N-glycosylated form, but with no amino acid change in the NxS / T site of the resulting deglycosylated proteins, which can provide production of non-N-glycosylated recombinant proteins in plants or other eukaryotic system with a native-like fold. Thus, materials and methods for in vivo de-glycosylation of recombinant N-glycosylated proteins by co-expression with Endo-β-N-acetylglucosaminidase H (Endo H) in plants, using a transient expression system are described in this invention. A method of expressing active Endo Hin plants is also provided.

A method for determining whether an individual is at an increased risk for myocardial infarction, comprising screening for the presence of Factor II and Factor XIII alleles associated with myocardial infarction. Also provided are kits and primers that specifically hybridize adjacent to the allele-specific regions of the Factor II and Factor XIII genes.

The invention provides an immunoaffinity chromatography column filler, an immunoaffinity chromatography column, a method for separating and purifying blood coagulation factor XIII and applications thereof, and relates to the technical field of preparation of functional blood coagulation factors. The immunoaffinity chromatography column filler is mainly obtained by coupling an anticoagulation factor XIII monoclonal antibody with an affinity chromatography medium. According to the principle of high-specificity selection of antigen and antibody, during the purification process of coagulation factor XIII on the immunoaffinity chromatography column containing this filler, the monoclonal antibody against coagulation factor XIII can specifically adsorb coagulation factor XIII, thus effectively The purity and extraction efficiency of the blood coagulation factor XIII are improved, and the purity of the prepared blood coagulation factor XIII is as high as 95%, which can be widely used in the preparation of viscoelastic coagulation analysis and detection reagents.

The disclosed apparatus, systems and methods relate to ATPA technology that provides a method for the real-time assessment of the polymerization of a sample, e.g., whole blood or blood plasma coagulation, by a non-contact acoustic tweezing device. The acoustic tweezing technology integrates photo-optical tests used in plasma coagulation assays with mechanical (viscoelastic) tests used in whole blood analysis. Its key disruptive features are the increased reliability and accuracy due to non-contact measurement, low sample volume requirement, relatively short procedure time (less than 10 minutes), and the ability to assess the level of Factor XIII function from measurements of the fibrin network formation time.

Use of factor XIII for inhibiting the formation of seromas by administering factor XIII. The factor XIII can be administered locally at the site of a wound or surgery or administered systemically. If the factor XIII is administered locally, it can be activated or non-activated and may be administered in conjunction with activated thrombin.

The disclosed apparatus, systems and methods relate to ATPA technology that provides a method for the real-time assessment of the polymerization of a sample, e.g., whole blood or blood plasma coagulation, by a non-contact acoustic tweezing device. The acoustic tweezing technology integrates photo-optical tests used in plasma coagulation assays with mechanical (viscoelastic) tests used in whole blood analysis. Its key disruptive features are the increased reliability and accuracy due to non-contact measurement, low sample volume requirement, relatively short procedure time (less than 10 minutes), and the ability to assess the level of Factor XIII function from measurements of the fibrin network formation time.

The invention relates to a method of quality control testing a Factor XIII (FXIII) containing sample which comprises the step of detecting the presence of and / or measuring the concentration of pre-activated FXIII (FXIIIao) in said sample and to a quality control kit for determining the quality of a Factor XIII (FXIII) containing sample. Preferably, an anion-exchange chromatographic column is used, as well as the fluorescent substrate Abz-NE (Cad-Dnp) EQVS PLTLLK-OH.

Analyses of serum samples for the presence and amount of either of the two subunits of human Factor XIII protein are used as a means of eliminating a significant source of error that arises in the testing of serum and plasma. For serum samples, a negative result of an analysis for the presence of subunit a is a means of verifying that a sample is indeed serum, while a negative or positive result for subunit a serves to distinguish serum (negative) from plasma (positive). A positive result for the presence of subunit b is a means of verifying that the sample is either serum or plasma and not any other biological fluid. A quantitative analysis of subunit b is a means of verifying that the sample is of the intended volume rather than having been reduced in volume due to improper sampling. A quantitative analysis of subunit b is also a means of verifying the dilution of a sample of either serum or plasma.