Bovine FGF

Description

Fibroblast growth factor 1 (FGF1), also known as acidic FGF (AFGF), is a signaling polypeptide and member of the FGF family with roles in cell growth, proliferation, development, and survival, as well as osteogenesis and adipogenesis.1,2 Unlike other FGFs, FGF1 lacks an N-terminal signaling peptide and is secreted via a non-canonical pathway as part of a multi-protein complex.1 FGF1 binds to FGF receptors at the cell surface to stimulate intracellular signaling pathways such as PKC/PLCγ, PI3K/Akt/mTOR, and ERK/MAPK, but can also be translocated across the cell membrane to localize in both the cytosol and nucleus. FGF1 induces osteogenic differentiation of bone marrow mesenchymal stem cells and increases the number of osteoblasts in early stages of bone repair. Exogenous administration of FGF1 normalizes blood glucose levels in diabetic ob/ob and db/db mice and a mouse model of diet-induced obesity.3 Cayman’s FGF1 (human, recombinant) protein can be used for cell-based assays. This protein consists of 141 amino acids and has a calculated molecular weight of 16 kDa.WARNING This product is not for human or veterinary use.

Description

Fibroblast Growth Factor-acidic Human Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.
The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli

Background

Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis.
Three alternatively spliced variants encoding different isoforms have been described.
The hep-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.