The present invention relates to an isolated antibody, which selectively binds to CLEC14A, wherein said antibody (a) comprises at least one heavy chain variable region that comprises three CDRs and at least one light chain variable region that comprises three CDRs, wherein said heavy chain variable region comprises: (i) a variable heavy (VH) CDR1 that has the amino acid sequence of SEQ ID NO. 105, preferably of SEQ ID NO: 2 or 42; (ii) a VH CDR2 that has the amino acid sequence of SEQ ID NO. 106, preferably of SEQ ID NO: 3 or 43; and/or (iii) a VH CDR3 that has the amino acid sequence of SEQ ID NO. 107, preferably of SEQ ID NO: 4 or 44; and/or wherein said light chain variable region comprises: (iv) a variable light (VL) CDR1 that has the amino acid sequence of SEQ ID NO. 108, preferably of SEQ ID NO: 6 or 46; (v) a VL CDR2 that has the amino acid sequence of SEQ ID NO. 109, preferably of SEQ ID NO: 7 or 47; and/or (vi) a VL CDR3 that has the amino acid sequence of SEQ ID NO. 1 10, preferably of SEQ ID NO: 8 or 48; or (b) comprises at least one heavy chain variable region that comprises three CDRs and at least one light chain variable region that comprises three CDRs, wherein said heavy chain variable region comprises: (i) a variable heavy (VH) CDR1 that has the amino acid sequence of SEQ ID NO: 22; (ii) a VH CDR2 that has the amino acid sequence of SEQ ID NO: 23; and/or (iii) a VH CDR3 that has the amino acid sequence of SEQ ID NO: 24; and/or wherein said light chain variable region comprises: (iv) a variable light (VL) CDR1 that has the amino acid sequence of SEQ ID NO: 26; (v) a VL CDR2 that has the amino acid sequence of SEQ ID NO: 27; and/or (vi) a VL CDR3 that has the amino acid sequence of SEQ ID NO: 28; or (c) is an antibody which can compete with antibody (a) or (b) for binding to CLEC14A. The invention further provides chimeric antigen receptors, nucleic acid molecules encoding the antibodies of the invention or the chimeric antigen receptors, vectors, cells and methods/uses of the antibodies and chimeric antigen receptors.

A method for determining the presence of a molecule coupled to the cytoplasmic side of a cellular membrane is disclosed. The method is implemented in a microfluidic setting and is particularly suitable for determining the presence and/or the activity of a G protein or an arrestin protein in a cell.

Devices and methods for analysing extracellular vesicle glycans are described. According to an embodiment, a microfluidic device comprises an inlet portion configured to receive a fluid sample; a mixing portion fluidically coupled to the inlet portion and configured to facilitate mixing between the fluid sample and magnetic nanoparticles functionalized to bind with extracellular vesicles and aggregate to vesicle glycans in the fluid sample; a magnetic separation portion fluidically coupled to the mixing portion and configured to separate clusters of magnetic nanoparticles from the fluid sample; and a magnetic sensor configured to measure magnetic properties of the fluid sample after it has passed through the magnetic separation portion. The magnetic nanoparticles may configured to aggregate in the presence of respective lectins when bound with extracellular vesicles carrying target glycans. In a specific embodiment, the magnetic particles comprise a magnetic polycore coated with polydopamine.

Provided is an anti-CLL1 antibody and an application thereof. The variable region of the anti-CLL1 antibody includes the CDRs of SEQ ID NO: 1 to 6, SEQ ID NO: 5, and SEQ ID NO: 7 to 11 or SEQ ID NO: 12 to 17. The anti-CLL1 antibody of the present application has significant binding ability to both free and cell surface CLL1. After humanization, the affinity of the antibody to CLL1 is further improved, and it has important application prospect in the clinical diagnosis and/or treatment of tumors.

Methods are described for preparing samples including biological, environmental, and food products for microbial analysis. Microbes and microbe components in the sample can be treated with antimicrobial compounds and a matrix solution to permit fast and accurate characterization using analysis techniques such as matrix-assisted laser desorption/ionization Time-of-Flight mass spectrometry (MALDI-TOF MS).

Exemplary embodiments of the present invention relate to rapidly and easily test initial liver disease and more particularly to a monoclonal antibody for α1-acid glycoprotein, a diagnosis kit for tracking progressive chronic hepatitis and liver fibrosis in an initial phase of liver disease by measuring the concentration of asialo-α1-acid glycoprotein (AsAGP) as a hepatocyte injury marker in a sample using the antibody, and a use thereof. Further, embodiments of the present invention provide a kit for specifically determining the degree of progressive chronic hepatitis and hepatic fibrosis from a blood sample and an immunochromatography strip, comprising a HRP-RCA II (Ricinus communis agglutinin II) conjugate or a Gold-RCA II conjugate specifically binding to asialo α-1 acid glycoprotein.

The present invention provides a tumor immunotherapy target and use thereof, specifically provides use of the LSECtin expressed by infiltrating tumor-associated macrophage and BTN3A3 expressed by tumor solely or in combination as a target in tumor immunotherapy, and further provides a substance capable of inhibiting the activity of LSECtin expressed by infiltrating tumor-associated macrophage, the activity of BTN3A3 expressed by tumor, or the interaction of the LSECtin with BTN3A3, including RNA molecules, fusion protein BTN3A3-Ig, and monoclonal antibody 5E08, which can be used as an active ingredient to prepare a tumor immunotherapy drug, and is suitable for industrial applications.

A lectin-binding substance measurement method is a method for measuring a lectin-binding substance in a sample, and includes a measuring step of bringing a blocked labeled lectin including a water-soluble carrier made of a first water-soluble polymer and a labeling substance and a lectin immobilized on the water-soluble carrier into contact with the sample.

A lectin-binding substance measurement method is a method for measuring a lectin-binding substance in a sample, and includes: a capturing step of bringing a capture carrier including a water-insoluble carrier and a molecule immobilized on the water-insoluble carrier, the molecule being a molecule capable of capturing a lectin-binding substance, into contact with the sample to cause the capture carrier to capture the lectin-binding substance; a washing step of removing contaminants unbound to the capture carrier; a releasing step of releasing the lectin-binding substance from the capture carrier to obtain a prepared sample; and a measuring step of measuring the lectin-binding substance in the prepared sample by using a lectin.

The present invention includes a multivalent glycan microarray for detection of glycan-binding proteins. The multivalent glycan microarray allows a multivalent presentation of glycan on a microarray substrate, which can enhance binding of the glycan binding protein to the glycan microarray. The multivalent microarray includes a solid substrate having one or more branched polymers bonded to it via one or more silane-based linker reagents. The branched polymer in turn is bonded to a glycan, via one or more bifunctional linkers to form the multivalent glycan microarray. Nonspecific binding of glycan binding proteins to the multivalent glycan microarray can be reduced by using a blocking reagent coated on to the microarray substrate, which includes a polyethylene glycol surfactant attached to the solid substrate via a self-crosslinking azido-functionalized silane. Methods for making multivalent glycan microarrays and methods for using same to detect glycan-binding proteins are also disclosed.