Recombinant human / mouse FGF-8b protein (Qk057)
Fibroblast growth factor 8b (FGF-8b) is a member of the FGF family involved in the regulation of embryogenesis, cellular proliferation, differentiation, and migration.
FGF8b is commonly used for the differentiation of induced pluripotent stem cells into neural cell types and brain organoid cultures.
FGF8b is a spliced form of FGF8, a heparin-binding protein that targets mammary and non-mammary cells expressing the FGF receptors. A 22.5 kDa highly pure, bioactive recombinant protein produced in an animal-free expression system. This protein is carrier-free, tag-free and non-glycosylated to ensure a pure, homogenous protein with exceptional lot-to-lot consistency. Qk057 is suitable for enhanced reproducibility and physiologically relevant cultures.
FGF-8b activity is determined using the Promega serum response element luciferase reporter assay (*) in HEK293T cells. EC50 = 4.1 ng/ml (0.18 nM).
Cells are treated in triplicate with a serial dilution of FGF-8b for 3 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. Data from Qk057 lot #104458.
FGF-8b (Qk057) migrates as a single band at 22.5 kDa in non-reducing (NR) conditions and upon reduction.
Purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk057 batch #104458.
We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine. All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.
FGF-8b is a heparin-binding protein and an isoform of FGF-8 belonging to a family of fibroblast growth factors (FGF) . It was originally discovered as an essential growth factor for the androgen-dependent growth of mouse mammary carcinoma cells . In mouse, there are eight sliced protein isoforms of FGF8 (a-h) whereas in humans, there are four alternate spliced protein isoforms namely FGF-8a, FGF-8b, FGF-8e and FGF-8f. These four FGF8 isoforms (a, b, e and f) are highly conserved between humans and mice. Human and murine FGF-8a and FGF-8b show 100% homology  whereas there is a 98% identity with human and murine FGF8e and FGF8f .
Human FGF-8b, a monomeric protein has a molecular weight of 22.5kDa with 194 amino acid (aa) residues covering the signal sequence domain, N-terminal domain, FGF domain and proline-rich C terminal sequence. Its three-dimensional structure is composed of 12 beta strands arranged in two beta-sheet and short alpha-helices. The protein contains a conserved heparin-binding domain that is essential for its biological activity.
FGF-8, including the spliced forms, work by binding the FGF receptors (FGFR) to activate the Ras/MAPK signalling pathway, a key pathway that contributes to several cellular processes. In general, the FGF family is involved in broad cellular and biological processes including cell proliferation, differentiation, survival and apoptosis [5-8].
Functionally, FGF-8b has been shown to play a major role during prenatal development. It is widely expressed during embryogenesis and is a key player in epithelial-mesenchymal transitions . During gastrulation, it contributes to the organization and induction role and regulates the patterning of organs in the embryos. These organs include the brain, eye, ear, limb and the heart [10-12].
Although, FGF-8 isoforms work in a coordinated and concerted manner, findings have suggested that they also have distinct key roles. FGF-8b has been shown to have the strongest affinity for the receptor and oncogenic capacity. A study using transgenic mice showed FGF-8a expands the midbrain while FGF-8b showed a transformational activity by transforming the midbrain into the cerebellum .
FGF-8b and other neurotrophins have been shown to promote neural regeneration. More specifically, FGF-8b has been shown to promote neurite outgrowth in mammalian spiral ganglion neurons (SGN) in vitro . FGF-8b, in combination with Shh, a neurotrophic factor, and transcription factors Ascl1 and Nurr1, has been used to generate induced neuronal cells (pan-neuronal and dopaminergic (DA) neurons) by reprogramming embryonic mouse fibroblasts . Additionally, FGF-8b has been used to generate DA neurons from stem cells, including induced pluripotent stem cells (iPSCs) and dental pulp stem cells [16-17]. More recently, FGF-8b has been used to generate ventral midbrain organoids derived from iPSCs to provide a robust 3D in vitro platform that is suitable for comprehensive DA neuronal studies .
Whilst there is a limited expression of FGF-8 and its isoforms in the normal adult, increasing studies have shown the presence of FGF-8 in adult tissues and cells including the reproductive tract, peripheral leukocytes and hematopoietic cells [19-21]. Further functional studies are required to fully delineate the role of FGF-8 and its isoforms in the normal adult.
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