Provided herein is a thermolabile proteinase and methods of using the same. In some embodiments, the thermolabile proteinase may comprise an amino acid sequence that is at least 90% identical to any of SEQ ID NOs:1-11 and at least one amino acid substitution in helix 3. The thermolabile proteinase is active at a temperature in the range of 4° C.-40° C. and is inactivated by raising the temperature to above 50° C., where the proteinase is substantially inactive at 65° C.

An object of the present invention is to provide a method for enhancing a sensitivity of a current endotoxin measuring reagent employing a recombinant protein to the endotoxin of Helicobacter pylori. The present invention provides a method for enhancing the sensitivity of an endotoxin measuring reagent to the endotoxin of Helicobacter pylori, the endotoxin measuring reagent containing a recombinant protein of horseshoe crab factor C, the method including increasing a content of the recombinant protein of factor C at the time of endotoxin measurement to an amount that is sufficient for enhancing the sensitivity.

A method of detecting a metal ion in a protein-containing sample includes adding a protein degrading enzyme to the protein-containing sample to form an enzyme degradation product, adding an acid to the enzyme degradation product to provide a mixture, filtering the mixture to provide a supernatant, extracting the supernatant with an organic solvent to remove organic solvent soluble byproducts to provide a washed aqueous layer, and detecting the metal ion in the washed aqueous layer. The method is amenable to the detection of heavy metal ions in complex products such as milk. A kit includes reagents for performing the method.

Isolated bioactive priming peptides and bioactive priming compostions comprising bioactive priming polypeptides and/or inducer compounds are provided that are useful when applied to plants in agricultural formulations. Methods of using the isolated bioactive priming peptides and/or compositions are also provided which are applied exogenously to the surface of a plant or a plant cell membrane or endogenously to the interior of a plant or to a plant cell. The isolated bioactive priming peptides and/or bioactive priming compositions when applied to a plant, a plant part, or a plant growth medium or a rhizosphere in an area surrounding the plant or the plant part increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or protect the plant or the plant part from disease, and/or increase the innate immune response of the plant or the plant part and/or improve the quality and/or quantity of juice obtained from a plant or plant part.

Provided herein is a thermolabile proteinase and methods of using the same. In some embodiments, the thermolabile proteinase may comprise an amino acid sequence that is at least 90% identical to any of SEQ ID NOs:1-11 and at least one amino acid substitution in helix 3. The thermolabile proteinase is active at a temperature in the range of 4 C.-40 C. and is inactivated by raising the temperature to above 50 C., where the proteinase is substantially inactive at 65 C.

In one aspect, the invention provides methods of inhibiting the effects of MASP-2-dependent complement activation in a living subject. The methods comprise the step of administering, to a subject in need thereof, an amount of a MASP-2 inhibitory agent effective to inhibit MASP-2-dependent complement activation. In some embodiments, the MASP-2 inhibitory agent inhibits cellular injury associated with MASP-2-mediated alternative complement pathway activation, while leaving the classical (C1q-dependent) pathway component of the immune system intact. In another aspect, the invention provides compositions for inhibiting the effects of lectin-dependent complement activation, comprising a therapeutically effective amount of a MASP-2 inhibitory agent and a pharmaceutically acceptable carrier.

The present invention generally relates to the field of fermentation technology and microorganisms useful for such fermentations. The invention also relates to materials including nucleic acids and proteins useful for altering fermentation characteristics of microorganisms, and to microorganisms comprising such nucleic acids and/or proteins. In particular, the invention relates to materials for conferring, modifying or reducing microbial stress resistance.

The present invention relates to a method for the recombinant production of a serine protease comprising (a) culturing a host cell comprising one or more vectors, wherein the one or more vectors encode in expressible form the serine protease and a proteinaceous inhibitor of the serine protease, wherein the proteinaceous inhibitor of the serine protease is heterologous with respect to the serine protease, under conditions wherein the serine protease and the proteinaceous inhibitor of the serine protease are expressed; or (a) culturing a host cell the genome of which encodes in expressible form the serine protease and a proteinaceous inhibitor of the serine protease, wherein the proteinaceous inhibitor of the serine protease is heterologous with respect to the serine protease, and wherein the coding sequences of the serine protease and/or the proteinaceous inhibitor have been introduced into the host cell genome by applying a CRISPR technology, under conditions wherein the serine protease and the proteinaceous inhibitor of the serine protease are expressed; and (b) isolating the serine protease expressed in step (a) or (a) from the host cell. The present invention also relates to a host cell comprising one or more vectors, wherein the one or more vectors encode in expressible form a serine protease and a proteinaceous inhibitor of the serine protease.

Provided herein is a thermolabile proteinase and methods of using the same. In some embodiments, the thermolabile proteinase may comprise an amino acid sequence that is at least 90% identical to any of SEQ ID NOs:1-11 and at least one amino acid substitution in helix 3. The thermolabile proteinase is active at a temperature in the range of 4 C.-40 C. and is inactivated by raising the temperature to above 50 C., where the proteinase is substantially inactive at 65 C.

The present invention provides antibodies and antigen-binding molecules thereof which specifically bind the and/or subunits of the non-active form of the GPIIb/IIIIa receptor. The antibodies and antigen-binding molecules can be genetically fused and/or conjugated to heterologous moieties and used, for example, as targeting moieties. The invention also includes methods for screening for these antibodies, as well as methods of making and methods of using chimeric molecules derived from the antibodies.