Recombinant Human FGF-basic (154 aa) (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
FGF-2, HBGF-2, BFGF, FGFB, Fibroblast Growth Factor 2, Basic Fibroblast Growth Factor
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publications
Human_FGF-basic_CF_RECOM_1_030520
Recombinant human FGF-basic (154 aa) induces the proliferation of NIH/3T3 cells in a dose-dependent manner. The ED50 for this effect is 0.02 - 0.1 ng/mL.
  • Human_FGF-basic_CF_RECOM_1_030520
    Recombinant human FGF-basic (154 aa) induces the proliferation of NIH/3T3 cells in a dose-dependent manner. The ED50 for this effect is 0.02 - 0.1 ng/mL.
  • Human_FGF-basic_CF_RECOM_2_030520
    Stability Testing for Recombinant human FGF-basic (154 aa). Recombinant human FGF-basic was aliquoted in PBS, pH 7 at 0.2 mg/mL. One aliquot was frozen and thawed four times (4x Freeze/Thaw) and compared to the control that was kept at 4°C (Control). The samples were tested for their ability to induce the proliferation of NIH/3T3 cells in a dose-dependent manner. The ED50 for this effect is 0.02 - 0.1 ng/mL.
Cat # Size Price Save
788402 10 µg ¥12,600
788404 25 µg ¥19,800
Description

FGF-basic also known as FGF-2, is a member of the fibroblast growth factor (FGF) family, which includes 23 members. FGF-2 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. FGF-2 is mitogenic for many cell types, both epithelial and mesenchymal. It shows potent angiogenic activity and has been implicated in tumor angiogenesis. FGF-2 significantly promotes the proliferation of adipose-derived mesenchymal cells (AMC) and enhances chondrogenesis in three-dimensional micromass culture. FGF-2 binds to a family of four distinct, high affinity tyrosine kinase receptors, designated FGFR-1 to FGFR-4. In addition, FGF-2 binds to the extracellular matrix (ECM) and heparan sulfate (HS), and 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 heparin sulfate 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. FGF-2, αvβ3 integrin, and FGFR-1, form a trimolecular complex required for ERK1/2 activation. MT1-MMP (MMP-14) downregulates the amount of FGF-2 bound to the cell surface and therefore, reduces FGF-2 signaling.

Product Details
Technical data sheet

Product Details

Source
Human FGF-basic (154 aa), amino acid Ala135-Ser288 (Accession # P09038) was expressed in E.coli. The amino terminal contains Met.
Molecular Mass
The 155 amino acid recombinant protein has a predicted molecular mass of approximately 17.2 kD. The DTT-reduced and non-reduced protein migrate at approximately 18 kD by SDS-PAGE. The predicted N-terminal amino acid is Met.
Purity
>98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS pH 7.2.
Endotoxin Level
Less than 0.1 EU per µg protein as determined by the LAL method.
Concentration
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg and larger sizes are lot-specific and bottled at the concentration indicated on the vial (please contact technical support for concentration, or use our Lookup tool if you have a lot number.)
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for six months, or at -70°C untill expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C to -70°C. 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 to -70°C for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
Recombinant human FGF-basic (154 aa) induces the proliferation of NIH/3T3 cells in a dose-dependent manner. The ED50 for this effect is 0.02 - 0.1 ng/mL.
Application

Bioassay

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 tech@biolegend.com.

Antigen Details

Structure
Monomer
Distribution

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

Function
Possess broad mitogenic and potent angiogenic activity, plays a key role in physiological and pathological conditions, including embryonic development, wound repair, inflammation, and tumor growth. MT1-MMP downregulates fibroblast growth factor-2 (FGF-2) signaling.
Interaction
FGF-basic (154 aa) binds to αvβ3 integrin. Fibroblasts, myoblasts, osteoblasts, neuronal cells, endothelial cells, keratinocytes, chondrocytes, astrocytes, oligodendrocytes, and smooth muscle cells.
Ligand/Receptor
FGFR1, FGFR2, FGFR3 and FGFR4. Low affinity coreceptor heparan sulfate (HS) and heparan sulfate proteoglycans (HSPG) required for full activity.
Bioactivity
Recombinant human FGF-basic (154 aa) induces the proliferation of NIH/3T3 cells.
Cell Type
Astrocytes, Embryonic Stem Cells, Endothelial cells, Epithelial cells, Fibroblasts, Hematopoietic stem and progenitors, Mesenchymal cells, Mesenchymal Stem Cells, Neural Stem Cells, Osteoblasts, Osteoclasts
Biology Area
Angiogenesis, Cancer Biomarkers, Cardiovascular Biology, Cell Proliferation and Viability, Stem Cells
Molecular Family
Growth Factors
Antigen References
  1. Schlessinger J, et al. 2000. Mol Cell. 6:743-50.
  2. Ibrahimi OA, et al. 2001. Proc Natl Acad Sci U S A. 98:7182-7.
  3. Beenken A & Mohammadi M. 2009. Nat Rev Drug Discov. 8:235-53.
  4. Tassone E, et al. 2015. J Cell Physiol. 230:366-77.
  5. Chien SY, et al. 2016. Clin Sci (Lond). 130:667-81.
Gene ID
2247 View all products for this Gene ID
UniProt
View information about FGF-basic on UniProt.org

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) = 10e6/ ED50 (ng/mL)
Go To Top Version: 1    Revision Date: 03/05/2020

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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

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