85-1546-06　Fibrinogen, Rabbit 25mg　F4215-37

特徴

• Rabbit Fibrinogen is prepared from fresh rabbit plasma using several chromatographic steps. Plasminogen depleted by lysine affinity chromatography.
• Molecular Weight: 330kD
• Fibronectin is a high-molecular weight (~440kD) extracellular matrix glycoprotein that binds to membrane-spanning receptor proteins called integrins.[1] In addition to integrins, fibronectin also binds extracellular matrix components such as collagen, fibrin and heparan sulfate proteoglycans (e.g. syndecans). Fibronectin exists as a dimer, consisting of two nearly identical monomers linked by a pair of disulfide bonds.[1] The fibronectin protein is produced from a single gene, but alternative splicing of its pre-mRNA leads to the creation of several isoforms.
• Two types of fibronectin are present in vertebrates:[1] soluble plasma fibronectin (formerly called "cold-insoluble globulin", or CIg) is a major protein component of blood plasma (300ug/ml) and is produced in the liver by hepatocytes. Insoluble cellular fibronectin is a major component of the extracellular matrix. It is secreted by various cells, primarily fibroblasts, as a soluble dimer and is then assembled into an insoluble matrix in a complex cell-mediated process.
• Fibronectin plays a major role in cell adhesion, growth, migration and differentiation, and it is important for processes such as wound healing and embryonic development.[1] Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer and fibrosis.[2]
• Fibronectin exists as a dimer, consisting of two nearly identical polypeptide chains linked by a pair of C-terminal disulfide bonds.[3] Each fibronectin monomer has a molecular weight of 230-250kD and contains three types of modules: type I, II, and III. All three modules are composed of two anti-parallel β-sheets; however, type I and type II are stabilized by intra-chain disulfide bonds, while type III modules do not contain any disulfide bridges. The absence of disulfide bonds in type III modules allows them to partially unfold under applied force.[4]Three regions of variable splicing occur along the length of the fibronectin monomer.[3] One or both of the "extra" type III modules (EIIIA and EIIIB) may be present in cellular fibronectin, but they are never present in plasma fibronectin. A "variable" V-region exists between III14-15 (the 14th and 15th type III module). The V-region structure is different from the type I, II, and III modules, and its presence and length may vary. The V-region contains the binding site for α4β1 integrins. It is present in most cellular fibronectin, but only one of the two subunits in a plasma fibronectin dimer contains a V-region sequence.