Recombinant Human FGF-basic (146 aa) (Animal-Free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Fibroblast growth factor 2 (Fgf-2), Fgfb, bFGF
Cat # Size Price Quantity Check Availability
713304 50 µg $253.00
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Description

FGF-basic, also known as FGFb and FGF-2, is a member of the fibroblast growth factor (FGF) family which includes 23 members. FGFb is expressed in almost all tissues and plays an important role in a variety of normal and pathological processes, including development, wound healing, and neoplastic transformation. FGFb is mitogenic for many cell types, both epithelial and mesenchymal. FGFb shows potent angiogenic activity and has been implicated in tumor angiogenesis. In prostate, bladder, and renal cancers, FGFb regulates the induction of metalloproteinases (MMP) that degrade extracellular matrix proteins, thus facilitating tumor metastasis. FGFb binds to a family of four distinct, high affinity tyrosine kinase receptors, designated FGFR-1 to -4. In addition, FGFb binds to the ECM, and heparan sulfate (HS) is an essential and dynamic regulator of fibroblast growth factor (FGF) signaling. Two fundamentally different crystallographic models have been proposed to explain, at the molecular level, how HS/heparin enables FGF and FGF receptor (FGFR) to assemble into a functional dimer on the cell surface, although there is controversy regarding the exact manner by which this occurs.

Technical data sheet

Product Details

Source
Human FGF-basic, amino acids Pro143-Ser288 (Accession# NM_002006) was expressed in E. coli.
Molecular Mass
The 146 amino acid recombinant protein has a predicted molecular mass of approximately 16.4 kD. The predicted N-terminal amino acid is Pro.
Purity
>98%, as determined by Coomassie stained SDS-PAGE and HPLC analysis.
Formulation
Lyophilized, carrier-free.
Endotoxin Level
Less than 0.1 ng per µg of protein.
Storage & Handling
Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. It is recommended to further dilute in a buffer, such as 5% Trehalose, and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
Activity
ED50 ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 107 units/mg as determined by a cell proliferation assay using BALB/c 3T3 cells.
Application

Bioassay

Application Notes

This product is reactive with human and mouse.

Product Citations
  1. Li L, et al. 2023. PLoS Pathog. e1011856:19. PubMed
  2. Liu M, et al. 2021. Dev Cell. 56:2765. PubMed

Antigen Details

Distribution
Brain, retina, pituitary, kidney, placenta, testis, corpus luteum, adrenal glands, monocytes, prostate, bone, liver, cartilage, endothelial cells, and epithelial cells
Function
FGFb is a potent angiogenic factor, and plays a key role in various physiological and pathological conditions, including embryonic development, wound repair, inflammation, and tumor growth.
Interaction
Fibroblasts, myoblasts, osteoblasts, neuronal cells, endothelial cells, keratinocytes, chondrocytes, astrocytes, oligodendrocytes, and smooth muscle cells.
Ligand/Receptor
FGFR-1 (flg), FGFR-2 (bek, K-sam), FGFR3, and FGFR-4 (flg-2); low affinity coreceptor heparin sulfate and heparin sulfate proteoglycans required for full activity.
Bioactivity
Stimulation of 3T3 cell proliferation.
Cell Type
Neural Stem Cells, Mesenchymal Stem Cells, Hematopoietic stem and progenitors, Embryonic Stem Cells
Biology Area
Cell Biology, Neuroscience, Stem Cells, Synaptic Biology
Molecular Family
Growth Factors, Cytokines/Chemokines
Antigen References

1. Rusnati M and Presta M. 2007. Current Pharm. Des. 13:2025.
2. Chaffer CL, et al. 2007. Differentiation 75:831.
3. Cronauer NV, et al. 2003. Eur. Urol. 43:309.
4. Shimizu A, et al. 2001. J. Biol. Chem. 276:11031.
5. Mahammadi M, et al. 2005. Curr. Opin. Struct. Biol. 15:506.
6. Chiou M and Xu Y. 2006. Longaker MT Biochem. Biophys. Res. Commun. 343:644.

Gene ID
2247 View all products for this Gene ID
UniProt
View information about FGF-basic on UniProt.org
Go To Top Version: 3    Revision Date: 05/06/2014

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