ELISA

Transforming growth factor beta 3(TGF-beta 3) is a type of protein, known as a cytokine, which is involved in cell differentiation, embryogenesis and development. It belongs to a large family of cytokines called the Transforming growth factor beta superfamily. TGF-beta 3 is believed to regulate molecules involved in cellular adhesion and extracellular matrix(ECM) formation during the process of palate development. Without TGF-beta 3, mammals develop a deformity known as acleft palate. This is caused by failure of epithelial cells in both sides of the developing palate to fuse. TGF-beta 3 also plays an essential role in controlling the development of lungs in mammals, by also regulating cell adhesion and ECM formation in this tissue, and controls wound healing by regulating the movements of epidermal and dermal cells in injured skin. TGF-beta 3 activated Lef1 in the absence of beta-catenin(CTNNB1) via nuclear phospho-Smad2 and Smad4.

Transforming growth factor beta 3(TGF-beta 3) is a type of protein, known as a cytokine, which is involved in cell differentiation, embryogenesis and development. It belongs to a large family of cytokines called the Transforming growth factor beta superfamily. TGF-beta 3 is believed to regulate molecules involved in cellular adhesion and extracellular matrix(ECM) formation during the process of palate development. Without TGF-beta 3, mammals develop a deformity known as acleft palate. This is caused by failure of epithelial cells in both sides of the developing palate to fuse. TGF-beta 3 also plays an essential role in controlling the development of lungs in mammals, by also regulating cell adhesion and ECM formation in this tissue, and controls wound healing by regulating the movements of epidermal and dermal cells in injured skin. TGF-beta 3 activated Lef1 in the absence of beta-catenin(CTNNB1) via nuclear phospho-Smad2 and Smad4.

Transforming growth factor beta 3(TGF-beta 3) is a type of protein, known as a cytokine, which is involved in cell differentiation, embryogenesis and development. It belongs to a large family of cytokines called the Transforming growth factor beta superfamily. TGF-beta 3 is believed to regulate molecules involved in cellular adhesion and extracellular matrix(ECM) formation during the process of palate development. Without TGF-beta 3, mammals develop a deformity known as acleft palate. This is caused by failure of epithelial cells in both sides of the developing palate to fuse. TGF-beta 3 also plays an essential role in controlling the development of lungs in mammals, by also regulating cell adhesion and ECM formation in this tissue, and controls wound healing by regulating the movements of epidermal and dermal cells in injured skin. TGF-beta 3 activated Lef1 in the absence of beta-catenin(CTNNB1) via nuclear phospho-Smad2 and Smad4.

Tumor necrosis factor receptor superfamily, member4, also known as ACT35 or CD134 is a cell surface glycoprotein that was discovered through the production of a monoclonal antibody raised against the HUT-102 cell line. It belongs to the tumor necrosis factor receptor superfamily. CD134 was mapped to 1p36 by fluorescence in situ hybridization. CD134 is the primary receptor for feline immunodeficiency virus. CD134 expression can promote viral binding and renders cells permissive for viral entry, productive infection, and syncytium formation. Stimulating the receptor can improve the response to a powerful virus vector and may be useful in vaccine development.

Cystatin C or cystatin 3(formerly gamma trace, post-gamma-globulin or neuroendocrine basic polypeptide), a protein encoded by the CST3 gene, was originally described as a constituent of normal cerebrospinal fluid(CSF) and of urine from patients with renal failure. Cystatin 3 has a low molecular weight(approximately 13.3 kilodaltons), and it is removed from the bloodstream by glomerular filtration in the kidneys. In mouses, all cells with a nucleus(cell core containing the DNA) produce cystatin C as a chain of 120 amino acids. It is found in virtually all tissues and bodily fluids. Cystatin C, which belongs to the type II cystatin gene family, is a potent inhibitor of lysosomal proteinases(enzymes from a special subunit of the cell that break down proteins) and probably one of the most important extracellular inhibitors of cysteine proteases(it prevents the breakdown of proteins outside the cell by a specific type of protein degrading enzymes). Moreover, cystatin C is involved in networ

FAS Ligand (FASL) is a 40 kDa type II membrane protein belonging to the tumor necrosis factor family, which induces apoptosis by binding to its receptor, Fas. The human FasL gene consists of approximately 8.0 kb and is split into four exons. This gene consists of 281 amino acids with a calculated M(r) of 31,759 and was mapped on chromosome 1q23. It has an identity of 76.9% at the amino acid sequence level with mouse FasL. The FAS and FASL system plays a key role in regulating apoptotic cell death and corruption of this signaling pathway has been shown to participate in immune escape and tumor genesis. FAS and FASL triggered apoptosis pathway plays an important role in human carcinogenesis. This system may also play a role in modulating the genetic susceptibility of mouse strains to develop T-cell lymphoblastic lymphomas.

Galectin-9, also called HUAT or LGALS9A is a protein that in humans is encoded by the LGALS9 gene. This gene is mapped to 17q11.2. The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. The protein encoded by this gene is an S-type lectin. It is overexpressed in Hodgkin's disease tissue and might participate in the interaction between the H&RS cells with their surrounding cells and might thus play a role in the pathogenesis of this disease and/or its associated immunodeficiency. The protein has N- and C- terminal carbohydrate-binding domains connected by a link peptide.

Granzyme B is a serine protease that in humans is encoded by the GZMB gene. Granzyme B is expressed by cytotoxic T lymphocytes(CTL) and natural killer(NK) cells. CTL and NK cells share the remarkable ability to recognize specific infected target cells. They are thought to protect their host by inducing apoptosis of cells that bear on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein encoded by this gene is crucial for the rapid induction of target cell apoptosis by CTL in cell-mediated immune response.

Interleukin 1 receptor-like 1, also known as IL1RL1 or ST2, is a protein that in humans is encoded by the IL1RL1 gene. The protein encoded by this gene is a member of the interleukin 1 receptor family. Studies of the similar gene in mouse suggested that this receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells. TL1RL1 is necessary for endotoxin tolerance and, by inhibiting TLR responses, enhances Th2 responses. This gene, interleukin 1 receptor, type I(IL1R1), interleukin 1 receptor, type II(IL1R2) and interleukin 1 receptor-like 2(IL1RL2) form a cytokine receptor gene cluster in a region mapped to chromosome 2q12.