Abstract: Administration of U-II to rats caused an increase in the redness or the skin temperature of the ear of the rats. The increase was inhibited by compounds that decease the biological activity of the U-II/UT receptor. Thus, the present invention provides methods of measuring the biological activity of an U-II receptor by monitoring the redness or the skin temperature of the ear of an animal, and the use of the methods to test compounds for their abilities to increase or decrease the biological activity of an U-II receptor.

Abstract: A novel human cDNA, termed PRSS11-L, was isolated which encodes a polypeptide that belongs to the S2/HtrA serine protease family. The PRSS11-L mRNA is widely expressed in several tissues throughout the body by multi-tissue Northern blotting. The full-length PRSS11-L cDNA, was cloned, expressed and purified. Proteolytic activity was demonstrated using the protein substrate casein. The isolated nucleic acid or polypeptide molecule of the invention can be used in detection assays, gene therapy, and screening assays.

Abstract: This invention relates to nucleic acid encoding guinea pig PAR 4 and to the protein encoded thereby. The guinea pig DNA and protein are useful for the development of models of human platelet aggregation. The invention further relates to an animal model to assess the role of PAR antagonists in thrombosis.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease EOS. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease EOS mRNA is expressed in platelets and leukocytes and more specifically eosinophils. Although this protease is abundantly expressed in ovary, retina and stomach, where it may perform important functions, its expression in platelets and certain cells of the immune system suggests that it may play roles in thrombosis and in the immune process.

Abstract: A novel human cDNA, termed PRSS11-L, was isolated which encodes a polypeptide that belongs to the S2/HtrA serine protease family. The PRSS11-L mRNA is widely expressed in several tissues throughout the body by multi-tissue Northern blotting. The full-length PRSS11-L cDNA, was cloned, expressed and purified. Proteolytic activity was demonstrated using the protein substrate casein. The isolated nucleic acid or polypeptide molecule of the invention can be used in detection assays, gene therapy, and screening assays.

Abstract: This invention relates to nucleic acid encoding guinea pig PAR 4 and to the protein encoded thereby. The guinea pig DNA and protein are useful for the development of models of human platelet aggregation. The invention further relates to an animal model to assess the role of PAR antagonists in thrombosis.

Abstract: Administration of U-II to rats caused an increase in the redness or the skin temperature of the ear of the rats. The increase was inhibited by compounds that decease the biological activity of the U-II/UT receptor. Thus, the present invention provides methods of measuring the biological activity of an U-II receptor by monitoring the redness or the skin temperature of the ear of an animal, and the use of the methods to test compounds for their abilities to increase or decrease the biological activity of an U-II receptor.

Abstract: A novel human nucleic acid and polypeptide, termed PRSS11-L, are disclosed. PRSS11-L, which is observed in tissues throughout the body, can be used in methods of detection, gene therapy, and screening.

Abstract: Polypeptides corresponding to a novel S1 serine protease family member, termed protease D-G, and nucleic acids encoding them are described. The materials may be used, for example, in screening assays to identify protease D-G modulators and in methods for diagnosing or treating conditions associated with aberrant protease D-G activity.

Abstract: This invention relates to nucleic acid encoding guinea pig PAR 4 and to the protein encoded thereby. The guinea pig DNA and protein are useful for the development of models of human platelet aggregation. The invention further relates to an animal model to assess the role of PAR antagonists in thrombosis.

Abstract: A novel human cDNA, termed PRSS11-L, was isolated which encodes a polypeptide that belongs to the S2/HtrA serine protease family. The PRSS11-L mRNA is widely expressed in several tissues throughout the body by multi-tissue Northern blotting. The full-length PRSS11-L cDNA, was cloned, expressed and purified. Proteolytic activity was demonstrated using the protein substrate casein. The isolated nucleic acid or polypeptide molecule of the invention can be used in detection assays, gene therapy, and screening assays.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease EOS. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease EOS mRNA is expressed in platelets and leukocytes and more specifically eosinophils. Although this protease is abundantly expressed in ovary, retina and stomach, where it may perform important functions, its expression in platelets and certain cells of the immune system suggests that it may play roles in thrombosis and in the immune process. Enzymatically active protease EOS is amenable to further biochemical analyses for the identification of physiological substrates and specific modulators.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease EOS. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease EOS mRNA is expressed in platelets and leukocytes and more specifically eosinophils. Although this protease is abundantly expressed in ovary, retina and stomach, where it may perform important functions, its expression in platelets and certain cells of the immune system suggests that it may play roles in thrombosis and in the immune process.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease EOS. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease EOS mRNA is expressed in platelets and leukocytes and more specifically eosinophils. Although this protease is abundantly expressed in ovary, retina and stomach, where it may perform important functions, its expression in platelets and certain cells of the immune system suggests that it may play roles in thrombosis and in the immune process.

Abstract: The present invention provides epitope-tagged mammalian recombinant Growth Arrest Specific Gene 6 (Gas6) proteins or polypeptides that retain their biological activity of Gas6, including a novel method of generating and purifying the aforesaid proteins or polypeptides. Such biolgically active eptitope-tagged Gas6 proteins or polypeptides can be used when the presence of Gas6 is required and/or when Gas6 antagonists and receptors need to be identified. Prior to being expressed from a mammalian cell, the recombinant Gas6 protein or polypeptide is tagged with either Flag or polyhistidine to the C-terminus. After expression, the protein or polypeptide is purified in a single step affinity purification using either anti-Flag antibody resin or nickle resin. The purified epitope-tagged mammalian recombinant Gas6 protein or polypeptide maintains its biological activity and can be used thereafter.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed D-G. The deduced amino acid sequence, and it's alignment with other well characterized serine proteases clearly indicates that it is a member of the S1 serine protease family. We have found that the protease D-G mRNA is widely expressed in several tissues throughout the body including epidermis, fibroblasts, keratinocytes, colon, small intestine, stomach, lung, kidney, bone marrow, lymph node, thymus, ovary, prostate, uterus and spinal cord. Interestingly, this protease contains a hydrophobic stretch of amino acids which is a putative transmembrane near the NH2-terminus. Thus, this serine protease is thought to be synthesized as a type II integral protein.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed D-G. The deduced amino acid sequence, and it's alignment with other well characterized serine proteases clearly indicates that it is a member of the S1 serine protease family. We have found that the protease D-G mRNA is widely expressed in several tissues throughout the body including epidermis, fibroblasts, keratinocytes, colon, small intestine, stomach, lung, kidney, bone marrow, lymph node, thymus, ovary, prostate, uterus and spinal cord. Interestingly, this protease contains a hydrophobic stretch of amino acids which is a putative transmembrane near the NH2-terminus. Thus, this serine protease is thought to be synthesized as a type II integral protein.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease EOS. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease EOS mRNA is expressed in platelets and leukocytes and more specifically eosinophils. Although this protease is abundantly expressed in ovary, retina and stomach, where it may perform important functions, its expression in platelets and certain cells of the immune system suggests that it may play roles in thrombosis and in the immune process. Enzymatically active protease EOS is amenable to further biochemical analyses for the identification of physiological substrates and specific modulators.

Abstract: A novel human cDNA, termed PRSS11-L, was isolated which encodes a polypeptide that belongs to the S2/HtrA serine protease family. The PRSS11-L mRNA is widely expressed in several tissues throughout the body by multi-tissue Northern blotting. The full-length PRSS11-L cDNA, was cloned, expressed and purified. Proteolytic activity was demonstrated using the protein substrate casein. The isolated nucleic acid or polypeptide molecule of the invention can be used in detection assays, gene therapy, and screening assays.

Abstract: Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease EOS. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease EOS mRNA is expressed in platelets and leukocytes and more specifically eosinophils. Although this protease is abundantly expressed in ovary, retina and stomach, where it may perform important functions, its expression in platelets and certain cells of the immune system suggests that it may play roles in thrombosis and in the immune process.