Provided are methods for lyophilization of an aqueous thrombin solution, thrombin solutions for use in such lyophilization methods, and solid thrombin compositions produced by such methods.

The present subject matter is directed to a method of manufacturing and purifying an intravenous injection of prothrombin complex concentration (PCC) from plasma Fraction III and a method of manufacturing and purifying an intravenous injection of non-PCC from plasma Fraction IV. The intravenous injection of PCC and non-PCC obtained from the method can be administered to a patient in need thereof for stopping replication, killing and preventing HIV-1 and HIV-2 in a patient.

The present disclosure describes improved SELEX methods for producing aptamers that are capable of binding to target molecules and improved photoSELEX methods for producing photoreactive aptamers that are capable of both binding and covalently crosslinking to target molecules. Specifically, the present disclosure describes methods for producing aptamers and photoaptamers having slower dissociation rate constants than are obtained using prior SELEX and photoSELEX methods. The disclosure further describes aptamers and photoaptamers having slower dissociation rate constants than those obtained using prior methods. In addition, the disclosure describes aptamer constructs that include a variety of functionalities, including a cleavable element, a detection element, and a capture or immobilization element.

An example composition that is liquid includes thrombin and a constituent that includes one or more of guanidine derivatives or one or more anticoagulants. The one or more guanidine derivative may include 1-methylguanidine, 1,1-dimethylguanidine, 1,1-diethylguanidine, or N-benzyl-N-methylguanidine. The one or more anticoagulants may include rivaroxaban, apixaban, edoxaban, betrixaban, or a factor Xa anticoagulant.

An isolated peptide of up to 6 amino acids comprising an amino acid sequence which inhibits binding of an endothelial cell protein C receptor (EPCR) ligand to the EPCR is disclosed. Also disclosed is an isolated peptide comprising an amino acid sequence which inhibits binding of an endothelial cell protein C receptor (EPCR) ligand to the EPCR, wherein the peptide comprises a modification in at least one amino acid. Also disclosed is a molecule comprising an amino acid sequence which inhibits binding of an endothelial cell protein C receptor (EPCR) ligand to the EPCR attached to a heterologous moiety. Pharmaceutical compositions and methods of treatment are also disclosed.

A hydrogel precursor formulation which is in the form of an unreacted powder. The formulation comprises an activating enzyme, preferably thrombin, a cross-linking enzyme, preferably a transglutaminase, and more preferably factor XIII transglutaminase. The cross-linking enzyme is activatable by the activating enzyme in water with or without a buffer, and at least one structural compound A. The structural compound is crosslinkable by a selective reaction mediated by the crosslinking enzyme to form a hydrogel, wherein the cross-linking enzyme is activated.

Compositions and methods for regulating the blood coagulation pathway are disclosed. More particularly, the present disclosure relates to thrombin-thrombomodulin fusion proteins and their use as blood anticoagulants and for treating sepsis.

The disclosure relates to the recombinant Gla domain proteins and their use targeting phosphatidylserine (PtdS) moieties on the surface of cells, particularly those expressing elevated levels of PtdS, such as cells undergoing apoptosis.

The present invention relates to a method for producing recombinant human prethrombin-2 protein and having human ?-thrombin activity by the plant-based expression systems.

The present invention is directed to compounds, methods for stabilizing thrombin activity with a thrombin binding oligonucleotide and to stabilized thrombin. The thrombin binding oligonucleotide is capable of inhibiting thrombin activity whereby the inhibition can be reversed with an antisense oligonucleotide.