GF003
Fibroblast Growth Factor basic Protein, Human recombinant
Synonym(s):
FGF-2, Heparin-Binding Growth Factor 2, bFGF, beta-FGF
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.77
Recommended Products
biological source
human
Quality Level
Assay
>95% (SDS-PAGE)
manufacturer/tradename
Chemicon®
technique(s)
cell culture | stem cell: suitable
impurities
<0.1 EU/μg Endotoxin level (of FGF-b)
input
sample type neural stem cell(s)
sample type mesenchymal stem cell(s)
sample type epithelial cells
NCBI accession no.
UniProt accession no.
General description
Fibroblast Growth Factor-basic (FGF-b) is a heparin binding growth factor which stimulates the proliferation of a wide variety of cells including mesenchymal, neuroectodermal and endothelial cells. FGF-b also exerts a potent angiogenic activity in vivo. Human FGF-b is a 17.2 kDa protein containing 155 amino acid residues.
Fibroblast Growth Factor-basic (bFGF) is a heparin binding growth factor which stimulates the proliferation of a wide variety of cells including mesenchymal, neuroectodermal and endothelial cells. bFGF also exerts a potent angiogenic activity in vivo. Human bFGF is a 17.2 kDa protein containing 155 amino acid residues. Xu, et al. demonstrated that bFGF synergizes with the BMP antagonist noggin to sustain undifferentiated proliferation of human embryonic stem (hES) cells under feeder-free conditions. GF003-AF was developed without animal-based ingredients and can be used for the culture of hES cells in a feeder-free, animal-free culture system.
expressed in E. coli
Application
For most in vitro applications, bFGF exerts its biological activity in the concentration range of 0.1 to 10.0 ng/mL. Responding cells are (partial list): Endothelial, mesenchymal cells. Human ES cells require concentrations in the range of 4 to 100 ng/mL, depending on the method of culture.
Optimal working dilutions must be determined by end user.
Optimal working dilutions must be determined by end user.
The Fibroblast Growth Factor-basic (FGF-b) is a heparin binding growth factor which stimulates the proliferation of a wide variety of cells including mesenchymal, neuroectodermal & endothelial cells.
Linkage
FA009-1
Physical form
Lyophilized from a 0.7 mg/mL solution in 5mM Tris, pH 7.6 with 150 mM NaCl.
Storage and Stability
Maintain the lyophilized material at -20°C until expiration date as stated on the label.
General applications:
After a quick spin, reconstitute in 0.1M phosphate buffer, pH 6.8, to a concentration of 0.1-1.0 mg/mL. Reconstituted b
General applications:
After a quick spin, reconstitute in 0.1M phosphate buffer, pH 6.8, to a concentration of 0.1-1.0 mg/mL. Reconstituted b
Analysis Note
Chemicon′s Human FGF-b is fully biologically active when compared to standards. The ED50 was determined by the dose-dependent stimulation of thymidine uptake by NIH3T3 cells expressing FGF receptors.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Alexander Brown et al.
Biomaterials, 243, 119921-119921 (2020-03-17)
In vitro tissue engineered models are poised to have significant impact on disease modeling and preclinical drug development. Reliable methods to induce microvascular networks in such microphysiological systems are needed to improve the size and physiological function of these models.
Ratchakrit Srikuea et al.
Scientific reports, 10(1), 8239-8239 (2020-05-20)
Skeletal muscle exhibits enormous plasticity throughout life, however, less is known regarding how the stages of growth regulate its local vitamin D system. Herein, we investigated serum 25(OH)D3 and Ca2+ levels along with the vitamin D system in skeletal muscle
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service