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Fragment crystallizable region

Index Fragment crystallizable region

The fragment crystallizable region (Fc region) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. [1]

29 relations: Antibody, Antibody opsonization, Antigen, Basophil, Bispecific monoclonal antibody, Complement system, Degranulation, Eosinophil, Fc receptor, Fcab, Fragment antigen-binding, Fucose, Glycosidic bond, Glycosylation, Immune system, Immunoglobulin A, Immunoglobulin D, Immunoglobulin E, Immunoglobulin G, Immunoglobulin M, Isotype (immunology), Lysis, Mast cell, Peptide, Physiology, Protein domain, Protein tag, Receptor (biochemistry), Sialic acid.

Antibody

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses.

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Antibody opsonization

Antibody opsonization is the process by which the pathogen is marked for ingestion and eliminated by the phagocytes.

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Antigen

In immunology, an antigen is a molecule capable of inducing an immune response (to produce an antibody) in the host organism.

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Basophil

Basophils are a type of white blood cells.

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Bispecific monoclonal antibody

A bispecific monoclonal antibody (BsMAb, BsAb) is an artificial protein that can simultaneously bind to two different types of antigen.

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Complement system

The complement system is a part of the immune system that enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promotes inflammation, and attacks the pathogen's cell membrane.

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Degranulation

Degranulation is a cellular process that releases antimicrobial cytotoxic or other molecules from secretory vesicles called granules found inside some cells.

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Eosinophil

Eosinophils sometimes called eosinophiles or, less commonly, acidophils, are a variety of white blood cells and one of the immune system components responsible for combating multicellular parasites and certain infections in vertebrates. Along with mast cells and basophils, they also control mechanisms associated with allergy and asthma. They are granulocytes that develop during hematopoiesis in the bone marrow before migrating into blood, after which they are terminally differentiated and do not multiply. These cells are eosinophilic or "acid-loving" due to their large acidophilic cytoplasmic granules, which show their affinity for acids by their affinity to coal tar dyes: Normally transparent, it is this affinity that causes them to appear brick-red after staining with eosin, a red dye, using the Romanowsky method. The staining is concentrated in small granules within the cellular cytoplasm, which contain many chemical mediators, such as eosinophil peroxidase, ribonuclease (RNase), deoxyribonucleases (DNase), lipase, plasminogen, and major basic protein. These mediators are released by a process called degranulation following activation of the eosinophil, and are toxic to both parasite and host tissues. In normal individuals, eosinophils make up about 1–3% of white blood cells, and are about 12–17 micrometres in size with bilobed nuclei. While they are released into the bloodstream as neutrophils are, eosinophils reside in tissue They are found in the medulla and the junction between the cortex and medulla of the thymus, and, in the lower gastrointestinal tract, ovary, uterus, spleen, and lymph nodes, but not in the lung, skin, esophagus, or some other internal organs under normal conditions. The presence of eosinophils in these latter organs is associated with disease. For instance, patients with eosinophilic asthma have high levels of eosinophils that lead to inflammation and tissue damage, making it more difficult for patients to breathe. Eosinophils persist in the circulation for 8–12 hours, and can survive in tissue for an additional 8–12 days in the absence of stimulation. Pioneering work in the 1980s elucidated that eosinophils were unique granulocytes, having the capacity to survive for extended periods of time after their maturation as demonstrated by ex-vivo culture experiments.

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Fc receptor

An Fc receptor is a protein found on the surface of certain cells – including, among others, B lymphocytes, follicular dendritic cells, natural killer cells, macrophages, neutrophils, eosinophils, basophils, human platelets, and mast cells – that contribute to the protective functions of the immune system.

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Fcab

Fcabs are antibodies fragments engineered from the constant region of an antibody (Fc).

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Fragment antigen-binding

The antigen-binding (Fab) fragment is a region on an antibody that binds to antigens.

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Fucose

Fucose is a hexose deoxy sugar with the chemical formula C6H12O5.

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Glycosidic bond

In chemistry, a glycosidic bond or glycosidic linkage is a type of covalent bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate.

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Glycosylation

Glycosylation (see also chemical glycosylation) is the reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor).

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Immune system

The immune system is a host defense system comprising many biological structures and processes within an organism that protects against disease.

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Immunoglobulin A

Immunoglobulin A (IgA, also referred to as sIgA in its secretory form) is an antibody that plays a crucial role in the immune function of mucous membranes.

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Immunoglobulin D

Immunoglobulin D (IgD) is an antibody isotype that makes up about 1% of proteins in the plasma membranes of immature B-lymphocytes where it is usually coexpressed with another cell surface antibody called IgM.

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Immunoglobulin E

Immunoglobulin E (IgE) is a type of antibody (or immunoglobulin (Ig) "isotype") that has only been found in mammals.

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Immunoglobulin G

Immunoglobulin G (IgG) is a type of antibody.

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Immunoglobulin M

Immunoglobulin M (IgM) is one of several forms of antibody that are produced by vertebrates.

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Isotype (immunology)

In immunology, the immunoglobulin (Ig) isotype (class) is encoded by the constant region segments of the immunoglobulin gene which form the Fc portion of an antibody.

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Lysis

Lysis (Greek λύσις lýsis, "a loosing" from λύειν lýein, "to unbind") refers to the breaking down of the membrane of a cell, often by viral, enzymic, or osmotic (that is, "lytic") mechanisms that compromise its integrity.

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Mast cell

A mast cell (also known as a mastocyte or a labrocyte) is a type of white blood cell.

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Peptide

Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.

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Physiology

Physiology is the scientific study of normal mechanisms, and their interactions, which work within a living system.

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Protein domain

A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain.

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Protein tag

Protein tags are peptide sequences genetically grafted onto a recombinant protein.

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Receptor (biochemistry)

In biochemistry and pharmacology, a receptor is a protein molecule that receives chemical signals from outside a cell.

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Sialic acid

Sialic acid is a generic term for the N- or O-substituted derivatives of neuraminic acid, a monosaccharide with a nine-carbon backbone.

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Crystallizable fragment, FC fragment, FC region, Fc fragment, Fc region, Fc regions, Fc segment, Fc-domain, Fragment crystallizable, Immunoglobulin fc fragments, PFc fragment, PFc region.

References

[1] https://en.wikipedia.org/wiki/Fragment_crystallizable_region

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