Abstract: Provided is the use of an effective amount of alpha-enolase (enolase-1, ENO-1) antagonist in manufacturing a medicament for treating a fibrotic disease. ENO-1 antagonist significantly attenuated body weight loss and lung weight gain as well as the fibrosis lesion and collagen deposition in lungs. Also, ENO-1 antagonist significantly reduced cell migration and secretion of collagen and TGF-? in primary mouse lung myofibroblasts.

Abstract: Provided herein are methods for treating an angiogenesis-related disease comprising administration to a subject in need thereof an effective amount of alpha-enolase (enolase-1. ENO-1) antagonist.

Abstract: An immunoconjugate includes an anti-ENO-1 antibody, or a binding fragment thereof, and a therapeutic agent or a label, having the formula: Ab-(L-D)m, wherein Ab is the anti-ENO-1 antibody or the binding fragment thereof, L is a linker or a direct bond, D is the therapeutic agent or the label, and m is an integer from 1 to 12. The antibody may be a monoclonal antibody, which may be a humanized antibody or fully human antibody. A method for treating an inflammatory disease, immune disorder, or cancer includes administering to a subject in need of such treatment a pharmaceutically effective amount of an immunoconjugate containing an antibody against ENO-1, or a binding fragment thereof, and a therapeutic agent covalently conjugated with the antibody.

Abstract: An antibody, or an antigen-binding fragment there, binding human ENO1 (GenBank: AAH506421.1) is provided. Methods for treating an ENO1 protein-related disease or disorder, inhibiting cancer invasion and diagnosis of cancer are also provided.

Abstract: A detoxified recombinant E. coli heat-labile enterotoxin mutant, LTS61K, is employed as a carrier protein to conjugate polysaccharide. The LTS61K contains a mutated mature sub-unit A (LTA) that includes lysine at amino acid position 61 and a wild-type mature sub-unit B (LTB). Various types of bacterial capsular polysaccharide antigens were chemically conjugated with the LTS61K protein by a reductive amination reaction. The conjugated polysaccharide-LTS61K products were physically, chemically and biochemically identified as soluble form. Rabbits were immunized intramuscularly to determine the immunogenicity of conjugated vaccines by ELISA to detect anti-polysaccharide antigen IgG titers and serum bactericidal assay thereby determining the functional activity of the antibodies. Study results show that conjugated polysaccharide-LTS61K vaccines induce higher polysaccharide-specific IgG titers and greater bactericidal activity in sera than that of polysaccharide alone or polysaccharide mixed with LTS61K.

Abstract: An antibody, or an antigen-binding fragment there, binding human ENO1 (GenBank: AAH506421.1) is provided. Methods for treating an ENO1 protein-related disease or disorder, inhibiting cancer invasion and diagnosis of cancer are also provided.

Abstract: A method for specific linkage to a glycoprotein includes obtaining a glycoprotein having a monoglycan or diglycan attached thereto; producing a reactive functional group on a sugar unit on the glycoprotein; and coupling a linker or a payload to the reactive functional group on the glycoprotein.

Abstract: A method for treating an inflammatory disease or an immune disorder includes administering to a subject in need of such treatment an antagonist against ENO1. The antagonist binds ENO1 and inhibits ENO1 plasminogen receptor activity. The antagonist may be an anti-human ENO1 antibody, or an scFv, Fab, or F(ab)2 fragment thereof, that specifically binds to human ENO1 (GenBank: AAH50642.1) for the treatment of an inflammatory disease or an immune disorder, which may be multiple sclerosis, rheumatoid arthritis, Crohn's disease, ulcerative colitis, systemic Lupus erythematosus, chronic obstructive pulmonary disease (COPD), asthma, allergy, psoriasis, type 1 diabetes mellitus, artherosclerosis or osteoporosis.

Abstract: A humanized antibody, or a binding fragment thereof, wherein the humanized antibody binds human ENO1 (GenBank: AAH50642.1), wherein the antibody comprises a light chain variable region (VL) domain comprising a CDR1 having the amino acid sequence LCDR1 (RASENIYSYLT; SEQ ID NO: 6) and a CDR2 having the amino acid sequence LCDR2 (NAKTLPE; SEQ ID NO: 7) and a CDR3 having the amino acid sequence LCDR3 (QHHYGTPYT; SEQ ID NO: 8) and an antibody heavy chain variable region (VH) domain comprising a CDR1 having the amino acid sequence HCDR1 (GYTFTSCVMN; SEQ ID NO: 3), a CDR2 having the amino acid sequence HCDR2 (YINPYNDGTKYNEKFKG; SEQ ID NO: 4) and a CDR3 having the amino acid sequence HCDR3 (EGFYYGNFDN; SEQ ID NO: 5), wherein framework regions in the light chain variable region (VL) domain and the heavy chain variable region (VH) domain comprise amino acid sequences from a human immunoglobulin.

Abstract: The present invention discloses an anti-human alpha-enolase (ENO1) antibody, which can bind the peptides, comprising amino-acid sequence 296FD Q D D W G A W Q K F TA309 (SEQ ID: #9) and/or 326K R I A K A V N EK S336 (SEQ ID: #10) of human ENO1 protein (GenBank: AAH50642.1), has a favorable binding activity (the binding affinity is around 2.19×10-10 mol/L) and a remarkable capability to inhibit the cell invasion and tumor metastasis of a varied of tumors. The recognized peptides and antibody of the invention are useful for diagnosis, prognosis, and treatment of cancers that have been reported to express cell-surface ENO1 such as including lung, breast, pancreas, liver, colorectal, prostate cancers and solid tumors.

Abstract: A humanized antibody, or a binding fragment thereof, wherein the humanized antibody binds human ENO1 (GenBank: AAH50642.1), wherein the antibody comprises a light chain variable region (VL) domain comprising a CDR1 having the amino acid sequence LCDR1 (RASENIYSYLT; SEQ ID NO: 6) and a CDR2 having the amino acid sequence LCDR2 (NAKTLPE; SEQ ID NO: 7) and a CDR3 having the amino acid sequence LCDR3 (QHHYGTPYT; SEQ ID NO: 8) and an antibody heavy chain variable region (VH) domain comprising a CDR1 having the amino acid sequence HCDR1 (GYTFTSCVMN; SEQ ID NO: 3), a CDR2 having the amino acid sequence HCDR2 (YINPYNDGTKYNEKFKG; SEQ ID NO: 4) and a CDR3 having the amino acid sequence HCDR3 (EGFYYGNFDN; SEQ ID NO: 5), wherein framework regions in the light chain variable region (VL) domain and the heavy chain variable region (VH) domain comprise amino acid sequences from a human immunoglobulin.

Abstract: The present invention discloses an anti-human alpha-enolase (ENO1) antibody, which can bind the peptides, comprising amino-acid sequence 296FD Q D D W G A W Q K F TA309 (SEQ ID: #9) and/or 326K R I A K A V N EK S336 (SEQ ID: #10) of human ENO1 protein (GenBank: AAH50642.1), has a favorable binding activity (the binding affinity is around 2.19×10-10 mol/L) and a remarkable capability to inhibit the cell invasion and tumor metastasis of a varied of tumors. The recognized peptides and antibody of the invention are useful for diagnosis, prognosis, and treatment of cancers that have been reported to express cell-surface ENO1 such as including lung, breast, pancreas, liver, colorectal, prostate cancers and solid tumors.

Abstract: A method for treating an inflammatory disease or an immune disorder includes administering to a subject in need of such treatment an antagonist against ENO1. The antagonist binds ENO1 and inhibits ENO1 plasminogen receptor activity. The antagonist may be an anti-human ENO1 antibody, or an scFv, Fab, or F(ab)2 fragment thereof, that specifically binds to human ENO1 (GenBank: AAH50642.1) for the treatment of an inflammatory disease or an immune disorder, which may be multiple sclerosis, rheumatoid arthritis, Crohn's disease, ulcerative colitis, systemic Lupus erythematosus, chronic obstructive pulmonary disease (COPD), asthma, allergy, psoriasis, type 1 diabetes mellitus, artherosclerosis or osteoporosis.

Abstract: This invention relates to bispecific antibodies having combinations of linker and hinge sequences to create linker-hinge interface domains with biological significance. Such linker-hinge interface domains covalently join two molecules, maintain the biological activities of linked molecules (target binding), stabilize the biological characteristics of new molecule (solubility and 4° C. stability), maintain the chemical, biochemical and physical properties (cytotoxicity) of the linked molecules, and modulate the biological characteristics of the linked molecules (activating T-lymphocytes without significant sign of proliferations). Both linker (GGGGS) and hinge (CPPCP) sequences are required to establish functional linker-hinge interface domains as deletion of any of the component resulted in significant lost of T-lymphocyte mediated activity.

Abstract: This invention relates to a mutant E. coli heat-labile enterotoxin (LT) subunit A that can be used as an adjuvant. This subunit A mutant contains an amino acid substitution at a position corresponding to position 61 of a wild-type LT. An LT containing this mutated subunit A exhibits reduced toxicity compared to its wild type counterpart.

Abstract: This invention relates to a mutant E. coli heat-labile enterotoxin (LT) subunit A that can be used as an adjuvant. This subunit A mutant contains an amino acid substitution at a position corresponding to position 61 of a wild-type LT. An LT containing this mutated subunit A exhibits reduced toxicity compared to its wild type counterpart.

Abstract: A detoxified recombinant E. coli heat-labile enterotoxin mutant, LTS61K, is employed as a carrier protein to conjugate polysaccharide. The LTS61K contains a mutated mature sub-unit A (LTA) that includes lysine at amino acid position 61 and a wild-type mature sub-unit B (LTB). Various types of bacterial capsular polysaccharide antigens were chemically conjugated with the LTS61K protein by a reductive amination reaction. The conjugated polysaccharide-LTS61K products were physically, chemically and biochemically identified as soluble form. Rabbits were immunized intramuscularly to determine the immunogenicity of conjugated vaccines by ELISA to detect anti-polysaccharide antigen IgG titers and serum bactericidal assay thereby determining the functional activity of the antibodies. Study results show that conjugated polysaccharide-LTS61K vaccines induce higher polysaccharide-specific IgG titers and greater bactericidal activity in sera than that of polysaccharide alone or polysaccharide mixed with LTS61K.

Abstract: This invention relates to protein-polymer conjugates described in the specification. Also disclosed are a method for preparing a protein-polymer conjugate and using such a conjugate in treating various immune disorders.

Abstract: This invention relates to a mutant E. coli heat-labile enterotoxin (LT) subunit A that can be used as an adjuvant. This subunit A mutant contains an amino acid substitution at a position corresponding to position 61 of a wild-type LT. An LT containing this mutated subunit A exhibits reduced toxicity compared to its wild type counterpart.

Abstract: This invention relates to a mutant E. coli heat-labile enterotoxin (LT) subunit A that can be used as an adjuvant. This subunit A mutant contains an amino acid substitution at a position corresponding to position 61 of a wild-type LT. An LT containing this mutated subunit A exhibits reduced toxicity compared to its wild type counterpart.