The present invention is related to the anti-Uroplakin II antibodies, kits, cocktails, and use of anti-Uroplakin II antibodies for detection of cancer.

The present invention relates to a CFI bioactivity assay designed to quantitatively measure (a) CFI bioactivity of plasma or other body fluids; and (b) bioactivity of CFI in plasma or other body fluids of a human patient afflicted by a disease that involves amyloid deposition in tissues, in particular Alzheimer disease, AMD, glaucoma, or beta-amyloid cataract formation.

The invention relates to an antibody molecule having specificity for antigenic determinants of IL-17, therapeutic uses of the antibody molecule and methods for producing said antibody molecule.

The invention relates to an approach for introducing one or more desired insertions and/or deletions of known sizes into one or more predefined locations in a nucleic acid (e.g., in a cell or organism genome). They developed techniques to do this either in a sequential fashion or by inserting a discrete DNA fragment of defined size into the genome precisely in a predefined location or carrying out a discrete deletion of a defined size at a precise location. The technique is based on the observation that DNA single-stranded breaks are preferentially repaired through the HDR pathway, and this reduces the chances of indels (e.g., produced by NHEJ) in the present invention and thus is more efficient than prior art techniques. The invention also provides sequential insertion and/or deletions using single- or double-stranded DNA cutting.

Herein are reported anti-PDGF-B antibodies and their use in ophthalmology.

Sharks have been thriving for over 500 million years. Sharks evolved some of the first adaptive antibodies and developed immunoglobulin M (IgM) as their primary and only class of circulating antibody. Laboratory research exposing sharks to carcinogens has failed to illicit cancers in these animals, and while reports of sharks bearing tumors exist, it is rare to find in nature.

The present invention relates to polyclonal antibodies directed against at least one non-human biological pathogen, or against at least one molecule derived from said pathogen, towards a human or a non-human animal organism, wherein the said polyclonal antibodies are devoid of an antigenic determinant selected in a group comprising (i) N-glycolneuraminic acid (Neu5Gc) and/or (ii) a-1,3-galactose, and their use as a medicament.

A method is provided for producing motif-specific, context-independent antibodies that recognize a plurality of peptides or proteins within a genome that contain the same post-translationally modified motif. The method includes the step of immunizing a host with a degenerate peptide library antigen featuring (i) a fixed target motif containing one or more invariant amino acids including at least one modified amino acid, and (ii) a plurality of degenerate amino acids flanking the motif. Motif-specific, context-independent antibodies produced by the disclosed method are also provided. The method encompasses motifs consisting of a single modified amino acid, as well as short motifs comprising multiple invariant amino acids including one or more modified amino acids, such as all or part of kinase consensus substrate motifs, protein-protein binding motifs, or other cell signaling motifs. Methods of using the antibodies, e.g. for genome-wide profiling, are also provided.

The present invention relates to the fields of molecular medicine and targeted delivery of therapeutic or diagnostic agents to cells outside the vascular system and into the parenchymal tissue of organs within the body. More specifically, the present invention relates to the methods used to identify membrane receptors or transporters capable of carrying cargo specifically targeted to the parenchymal tissue of the brain and to in vivo enrichment methods for selecting peptides that are transported across the blood-brain barrier (“BBB”), or analogously, across other membrane containing organs or structures, such as liver, spleen, kidney and tumors.

A method is described for identifying high affinity monoclonal antibody heavy and light chain pairs from high throughput screens of antibody producing cell libraries such as B-cell and hybridoma libraries. Specifically, the method relates to application of reversed immunocapture and high resolution tandem mass spectrometry for the identification of heavy and light chain pairs of binding antibodies obtained from high throughput screens of antibody producing cell libraries.