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Recombinant Human FGF2

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Product Source Size Cat. No. Price
Recombinant Human FGF2 E. coli50 µg Z101455 $40.00
100 µg Z101456 $60.00
500 µg Z101457 $190.00
1.0 mg Z101459 $504.00
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Data Sheet
Print Version
Alternative Names bFGF, Fibroblast growth factor 2, FGF-2, Heparin-binding growth factor 2, HBGF-2
Recombinant Human Basic Fibroblast Growth Factor (FGF2)
Description Basic Fibroblast Growth Factor is found in almost all tissues of mesodermal and neuroectodermal origin and also in tumors derived from these tissues. Endothelial cells produce large amounts of this factor. Some bFGF is associated with the extracellular matrix of the subendothelial cells. Many cells express bFGF only transiently and store it in a biologically inactive form. The mechanism by which the factor is released by the cells is not known. It is released after tissue injuries and during inflammatory processes. FGF receptors are encoded by a gene family consisting of at least four receptor tyrosine kinases that transduce signals important in a variety of developmental and physiological processes related to cell growth and differentiation. bFGF stimulates the growth of fibroblasts, myoblasts, osteoblasts, neuronal cells, endothelial cells, keratinocytes, chondrocytes, and many other cell types.
Gene Symbol FGF2
Gene ID 2247
Accession No. P09038
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 17.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method
Purity >95% as determined by SDS-PAGE
Gel Image Click To Enlarge
Bioactivity The bioactivity was determined in a NIH/3T3 cell proliferation assay. The ED50 was in the range of 0.05 - 0.5 ng/ml.
Bioactivity Data Click To Enlarge
Formulation Lyophilized from a 0.2 μm filtered solution in PBS
Reconstitution A quick spin of the vial followed by reconstitution in sterile distilled water to a concentration not less than 0.1 mg/mL is recommended. Please note, filter sterilization is a must following reconstitution. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
FAQs
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How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.

· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).

· For recombinant proteins: EU is reported per microgram of protein.

· One EU = 0.1-0.2 ng endotoxin/µg of protein.

· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.