Recombinant Human Fibrillin-1/Asprosin (N-8His)

Source: Human Cells. MW :17kD. Recombinant Human Asprosin is produced by our Mammalian expression system and the target gene encoding Ser2732-His2871 is expressed with a 8His tag at the N-terminus. Asprosin is a protein hormone that is produced by white adipose tissue in mammals (and potentially by other tissues), which is then transported to the liver and stimulates it to release glucose into the blood stream. In the liver asprosin activates rapid glucose release by a cAMP-dependent pathway. The glucose release by the liver into the blood stream is vital for brain function and survival during fasting. People with neonatal progeroid syndrome lack asprosin, while people with insulin resistance have it in abundance. In animal tests asprosin showed potential for treating type 2 diabetes. When antibodies targeting asprosin were injected into diabetic mice, blood glucose and insulin levels improved. Protein function: Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1- containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell- surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively. Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca2+ signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). [The UniProt Consortium]