Significant 546 Microcystin Elisa Results

Description: Serum Amyloid A1 Protein (SAA1) is an acute phase apolipoprotein reactant that is produced predominantly by hepatocytes and is under the regulation of inflammatory cytokines. SAA is produced mainly in the liver and circulates in low levels in the blood. SAA may play a role in the immune system and facilitate the repair of injured tissues, it also acts as an antibacterial agent, and signals the migration of germ-fighting cells to sites of infection. SAA also functions as an apolipoprotein of the HDL complex. The SAA cleavage product designated amyloid protein A is deposited systemically as amyloid in vital organs such as the liver, spleen, and kidneys in chronic inflammatory diseases patients. These deposits are extremely insoluble and resistant to proteolysis; they disrupt tissue structure and compromise performance.

Description: Ephrin type-A receptor 4(EPHA4) belongs to the protein kinase superfamily and Ephrin receptor subfamily. EPHA4 contains 1 Eph LBD domain, 2 fibronectin type-III domains, 1 protein kinase domain and 1 SAM domain. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.

Description: The TIM (T cell/transmembrane, immunoglobulin and mucin) family plays a critical role in regulating immune responses, including allergy, asthma, transplant tolerance, autoimmunity and the response to viral infections. The unique structure of TIM immunoglobulin variable region domains allows highly specific recognition of phosphatidylserine (PtdSer), exposed on the surface of apoptotic cells. TIM-1 (T cell-immunoglobulinmucin; also KIM-1 and HAVcr-1) is a 100 kDa, type I transmembrane glycoprotein member of the TIM family of immunoglobulin superfamily molecules. There are two cytoplasmic alternate splice forms of TIM1. One is a long (359 aa) kidney form termed TIM-1b, and one is a short (334 aa) liver form termed TIM-1a. TIM-1, important for asthma and allergy, is preferentially expressed on T-helper 2 (Th2) cells and functions as a potent costimulatory molecule for T cell activation.

Description: The dendritic cell lysosomal-associated membrane protein (DC-LAMP)/CD208 is a type I integral transmembrane glycoprotein mostly homologous to CD68, of about 45 kDa in mouse and 90 kDa in human (glycosylation), with a bipartite C-terminal structure divided by a serine/proline rich region, a transmembrane domain and a conserved tyrosine-based lysosomal targeting motif in its cytoplasmic tail. Initially cloned as a specific marker of human mature dendritic cells (DCs), DC-LAMP has been subsequently shown to be expressed in alveolar type II pneumocytes. In both cell types, the molecule is found in the limiting membrane of intracellular multi-lamellar bodies, known as MIIC (MHC class II compartments) in human mature DCs and as lung surfactant-containing lamellar bodies in type II pneumocytes. In the latter cell type, DC-LAMP expression is also detected at the cell surface.

Description: IL3 exerts its biologic activity through its interaction with a cell surface receptor that consists of two subunits. The a subunit (CD123) specifically binds IL3, whereas the ß subunit is required for signaling and is common to the GMCSFR and IL5-R. 107D2.08 and 106C2.02 mAbs were obtained after mouse immunization with sorted human tonsillar PDC. Both clones strongly stain PDCs and basophils, weakly stain monocytes, CD34+ derived DCs and CD11c+ DC, while no staining is observed on T, B, NK cells as well as on mono-derived DCs. Staining with 107D2.08 and 106C2.02 mAbs are maintained on sorted PDC cultured in the presence of IL3 and CD40L, but lost when IL3 alone is added to the culture. The recognition of the IL3Ra chain by 107D2.08 and 106C2.02 was confirmed by transfection studies. 107D2.08 appeared to be the most appropriate clone for in situ studies. 107D2.08 allowed the first observation of IL3Ra+ cells in breast tumor microenvironment