Improved anti-CD154 antibodies are provided herein which have ablated FcR binding and/or complement binding/activation. The use of these antibodies for inducing tolerance and treating immune diseases including autoimmunity, inflammation and allergic disorders is disclosed herein.

The present disclosure relates to antibodies or fragments thereof that target at least one conformational epitope of a Notch 3 or mutant Notch 3 receptor; and compositions and methods of use thereof.

The present disclosure relates to antibodies or fragments thereof that target at least one conformational epitope of a Notch 3 or mutant Notch 3 receptor; and compositions and methods of use thereof.

The present invention relates to Chimeric Antigen Receptors (CAR) that are recombinant chimeric proteins able to redirect immune cell specificity and reactivity toward CLL1 positive cells. The engineered immune cells endowed with such CARs are particularly suited for immunotherapy for treating cancer, in particular leukemia.

The disclosure provides antibodies that are useful for, among other things, inhibiting terminal complement (e.g., the assembly and/or activity of the C5b-9 TCC) and C5a anaphylatoxin-mediated inflammation and, thus, treating complement-associated disorders. The antibodies have a number of improved properties relative to eculizumab, including, e.g., increased serum half-life in a human.

The invention provides anti-CLL-1 antibodies and immunoconjugates and methods of using the same.

The present invention provides nucleic acids, vectors, host cells, methods and compositions to confer and/or augment immune responses mediated by cellular immunotherapy, such as by adoptively transferring CD8+ central memory T cells or combinations of central memory T cells with CD4+ T cells that are genetically modified to express a chimeric receptor. In some alternatives the genetically modified host cell comprises a nucleic acid comprising a polynucleotide coding for a ligand binding domain, a poly nucleotide comprising a customized spacer region, a polynucleotide comprising a transmembrane domain, and a polynucleotide comprising an intracellular signaling domain. In some alternatives, the ligand binding domains binds to CD171.

There is provided inter alia a polypeptide comprising an immunoglobulin chain variable domain comprising three complementarity determining regions (CDR1-CDR3) and four framework regions, wherein: (a) at least one lysine residue in CDR1, CDR2 and/or CDR3 has been substituted with at least one histidine residue, and/or (b) at least one arginine residue in CDR1, CDR2 and/or CDR3 has been substituted with at least one histidine residue; wherein the polypeptide has increased intestinal stability relative to a corresponding polypeptide not having said histidine substitutions.

The invention relates to methods to evaluate in one single assay the biocompatibility of materials based on the simultaneous determination of the phagocytosis, cell activation and cell death produced by said materials, preferably, in peripheral blood or other human cells and proximal fluids. The invention also relates to a kit to perform the method of the invention.

The invention relates to methods to evaluate in one single assay the biocompatibility of materials based on the simultaneous determination of the phagocytosis, cell activation and cell death produced by said materials, preferably, in peripheral blood or other human cells and proximal fluids. The invention also relates to a kit to perform the method of the invention.