Recombinant Human FGF-basic/145aa (carrier-free)

Pricing & Availability
Regulatory Status
Other Names
Fibroblast Growth Factor-basic, bFGF, FGF-2, Heparin-binding growth factor
Ave. Rating
Submit a Review
Product Citations
3NIH/3T3 cell proliferation induced by human FGFb.
  • FGFb_Prolif_120108
    3NIH/3T3 cell proliferation induced by human FGFb.
Cat # Size Price Quantity Check Availability Save
571502 10 µg 62€
Check Availability

Need larger quantities of this item?
Request Bulk Quote
571504 25 µg 100€
Check Availability

Need larger quantities of this item?
Request Bulk Quote
571506 100 µg 216€
Check Availability

Need larger quantities of this item?
Request Bulk Quote
571508 500 µg 652€
Check Availability

Need larger quantities of this item?
Request Bulk Quote

FGFb is a member of the fibroblast growth factor (FGF) family which includes 23 members. FGFb is expressed in almost all tissues and play important roles 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 (2). In prostate, bladder, and renal cancers, FGFb regulates the induction of metalloproteinases (MMP) that degrade extracellular matrix proteins, thus facilitating tumor metastasis (3). FGFb binds to a family of four distinct, high affinity tyrosine kinase receptors, designated FGFR-1 to -4 (4). In addition, FGFb binds to the ECM, and heparan sulfate (HS) that 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 (5), although there is controversy regarding the exact manner by which this occurs.

Product Details
Technical data sheet

Product Details

Human FGF-basic, amino acids Ala144-Ser288 (Accession # NM_002006) was expressed in E. coli.
Molecular Mass
The 145 amino acid recombinant protein has a predicted molecular mass of 16,310 Da. The DTT-reduced and non-reduced protein migrate at approximately 18kDa by SDS-PAGE. This protein may or may not contain an N-terminal methionine.
Purity is >98%, as determined by Coomassie stained SDS-PAGE.
0.22 µm filtered protein solution is in 10mM NaH2PO4, 150mM NaCl, pH 7.2, 1mM DTT.
Endotoxin Level
Endotoxin level is <0.1 EU/µg (<0.01ng/µg) protein as determined by the LAL method.
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
ED50 = 1 - 4 ng/ml, corresponding to a specific activity of 1 - 0.25 x 106 units/mg, as determined by the dose dependent stimulation of NIH/ 3T3 cell proliferation. The bioactivity is equivalent to competitor reported values.


Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at

Application References

(PubMed link indicates BioLegend citation)
  1. Wang J, et al. 2013. Biosens Bioelectron. 41:143. PubMed
Product Citations
  1. Stoyas CA, et al. 2020. Neuron. 630:105. PubMed
  2. Revkova VA, et al. 2021. ACS Omega. 6:15264. PubMed
  3. Hubka KM, et al. 2019. Acta Biomater. 97:385. PubMed
  4. Wang J, Mountziaris T 2013. Biochem Biophys Res Commun. 41:143. PubMed
  5. Gospodinova KO, et al. 2021. Cell Mol Neurobiol. Online ahead of print. PubMed
  6. Lee EC, et al. 2020. Int J Mol Sci. 21:00. PubMed

Antigen Details


Brain, retina, pituitary, kidney, placenta, testis, corpus luteum, adrenal glands, monocytes, prostate, bone, liver, cartilage, endothelial cells, epithelial cells

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 (1).
Fibroblasts, myoblasts, osteoblasts, neuronal cells, endothelial cells, keratinocytes, chondrocytes, astrocytes, oligodendrocytes, smooth muscle
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.
FGFb is a heparin-binding growth factor that is an angiogenic agent in vivo and also a potent mitogen for a variety of cell types in vitro.
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 Current Pharm Des 13:2025-2044 2007.
2. Chaffer CL, et al. Differentiation 75(9):831-42 2007.
3. Cronauer NV, et al. Eur Urol 43:309-319 2003.
4. Shimizu A, et al. J. Biol. Chem. 276:11031-11040 2001.
5. Mahammadi M, et al. Curr Opin Struct Biol 15:506-516 2005.

Gene ID
2247 View all products for this Gene ID
View information about FGF-basic on

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 2    Revision Date: 08.19.2014

For Research Use Only. Not for diagnostic or therapeutic use.


This product is supplied subject to the terms and conditions, including the limited license, located at ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.


BioLegend, the BioLegend logo, and all other trademarks are property of BioLegend, Inc. or their respective owners, and all rights are reserved.


8999 BioLegend Way, San Diego, CA 92121
Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587


Login / Register
Remember me
Forgot your password? Reset password?
Create an Account