Human FBLN2 Recombinant Protein (His tag)

Background: Fibulin 2 is the second largest member of the seven-member fibulin family of extracellular membrane (ECM) glycoproteins. Fibulin-2 consists of 1184 amino acids (aa) with a predicted molecular weight of ~125 kDa. The overall structure is common to fibulins: 3 Anaphylatoxin (AT)-like domains, 11 Epidermal Growth Factor (EGF)?like domains, and a Fibulin-type carboxy-terminal (FC) domain. Fibulin 2 is considered a Class I fibulin because the 400-residue N-terminus is divided into the Na and Nb sections, with the Na section containing 150-residues and 12 cysteines while the remaining Nb section is cysteine-free. The protein is known to form disulfide-linked homodimers, but it can also be secreted as an oligomer. Fibulin 2 is highly conserved across species, with the human protein sharing 82% amino acid identity compared to both mouse and rat. Fibulin 2 is considered a multifunctional binding protein due to its association with numerous ECM components, but its specific interactions have yet to be determined. Fibulin 2 is localized at the interface between microfibrils and the elastin core and its known interactions include nidogen-1, perlecan, laminin, aggrecan, endostatins, versican, collagen, and tropoelastin. It is down-regulated in numerous forms of cancer including breast, colorectal, lung, esophageal, and squamous cell carcinoma, but over-expression has been shown with solid tumors. There is also evidence that suggests that Fibulin 2 may play an indirect role in the neurogenesis of adult neural stem cells via interaction with integrins and TGF-beta 1.