Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Additional Information | A New and Improved rh FGF-4 is Now Available! It has enhanced purity! |
Details of Functionality | Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.25-1.25 ng/mL. |
Source | E. coli-derived human FGF-4 protein Ser54-Leu206 |
Accession # | |
N-terminal Sequence | Ser54 & Leu55 |
Protein/Peptide Type | Recombinant Proteins |
Gene | FGF4 |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 17 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 16 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
FGF-4 (fibroblast growth factor-4), also known as FGF-K or K-FGF (Kaposi’s sarcoma-associated FGF), is a 25 kDa secreted, heparin-binding member of the FGF family (1, 2). The human FGF-4 cDNA encodes 206 amino acids (aa) with a 33 aa signal sequence and a 173 aa mature protein with an FGF homology domain that contains a heparin binding region near the C-terminus (2). Mature human FGF-4 (aa 71-206) shares 91%, 82%, 94% and 91% aa identity with mouse, rat, canine and bovine FGF-4, respectively. Human FGF-4 has been shown to exhibit cross species activity. Expression of FGF-4 and its receptors, FGF R1c, 2c, 3c and 4, is spatially and temporally regulated during embryonic development (1, 3). Its expression in the mouse trophoblast inner cell mass promotes expression of FGF R2, and is required for maintenance of the trophectoderm and primitive endoderm (3-5). Later in mouse development, FGF-4 works together with FGF-8 to mediate the activities of the apical ectodermal ridge, which direct the outgrowth and patterning of vertebrate limbs (3, 6-9). FGF-4 is proposed to play a physiologically relevant role in human embryonic stem cell self-renewal. It promotes stem cell proliferation, but may also aid differentiation depending on context and concentration, and is often included in embryonic stem cell media in vitro (10-12). A C-terminally truncated 15 kDa isoform that opposes full-length FGF-4 and promotes differentiation is endogenously expressed in human embryonic stem cells. FGF-4 is mitogenic for fibroblasts and endothelial cells in vitro and has autocrine transforming potential (13). It is a potent angiogenesis promoter in vivo and has been investigated as therapy for coronary artery disease (14).
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