Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein

Carrier Free

Catalog # Availability Size / Price Qty
234-FSE-025/CF

With Carrier

Catalog # Availability Size / Price Qty
234-FSE-025
Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein Bioactivity
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Product Details
Citations (14)
FAQs
Reviews (1)

Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.5‑2.5 ng/mL.
Source
E. coli-derived human FGF basic/FGF2/bFGF protein
Gly132-Ser288
Accession #
N-terminal Sequence
Analysis
Gly132
Predicted Molecular Mass
17.4 kDa

Product Datasheets

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234-FSE (with carrier)

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234-FSE/CF (carrier free)

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

234-FSE

Formulation Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

234-FSE/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

Bioactivity Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein Bioactivity View Larger

Recombinant Human FGF basic/FGF2/bFGF (157 aa) (Catalog # 234-FSE) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 0.5-2.5 ng/mL.

SDS-PAGE Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein SDS-PAGE View Larger

1 μg/lane of Recombinant Human FGF basic/FGF2/bFGF (157 aa) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 19 kDa.

Background: FGF basic/FGF2/bFGF

FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum, and placenta. This factor contains four cysteine residues, but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. A variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. Binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF basic stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates embryonic development and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may participate in the production of a variety of pathological conditions resulting from excessive cell proliferation and excessive angiogenesis.

References
  1. Coulier, F. et al. 1997, J. Mol. Evol. 44:43.
  2. Chen, C.H. et al. 2004, Curr. Vasc. Pharmacol. 2:33.
  3. Mohammadi, M. et al. 2005, Curr. Opin. Struct. Biol. 15:506.
  4. Fernig, D. et al. 1994, Prog. Growth Factor Res. 5:353.
Long Name
Fibroblast Growth Factor basic
Entrez Gene IDs
2247 (Human); 14173 (Mouse); 281161 (Bovine); 403857 (Canine); 100033955 (Equine)
Alternate Names
basic fibroblast growth factor bFGF; Basic fibroblast growth factor; bFGF; FGF basic; FGF2; FGF-2; FGFBprostatropin; fibroblast growth factor 2 (basic); HBGF-2; heparin-binding growth factor 2; Prostatropin

Citations for Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

14 Citations: Showing 1 - 10
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  1. Betaglycan sustains HGF/Met signaling in lung cancer and endothelial cells promoting cell migration and tumor growth
    Authors: Cervantes-Villagrana, RD;Mendoza, V;Hinck, CS;de la Fuente-León, RL;Hinck, AP;Reyes-Cruz, G;Vázquez-Prado, J;López-Casillas, F;
    Heliyon
    Species: Mouse, Porcine
    Sample Types: Whole Cells
    Applications: Bioassay
  2. The temporal balance between self-renewal and differentiation of human neural stem cells requires the amyloid precursor protein
    Authors: Shabani, K;Pigeon, J;Benaissa Touil Zariouh, M;Liu, T;Saffarian, A;Komatsu, J;Liu, E;Danda, N;Becmeur-Lefebvre, M;Limame, R;Bohl, D;Parras, C;Hassan, BA;
    Science advances
    Species: Human
    Sample Types: Organoids
    Applications: Bioassay
  3. Organoids from mouse molar and incisor as new tools to study tooth-specific biology and development
    Authors: F Hermans, L Hemeryck, C Bueds, M Torres Per, S Hasevoets, H Kobayashi, D Lambrechts, I Lambrichts, A Bronckaers, H Vankelecom
    Stem Cell Reports, 2023-04-20;18(5):1166-1181.
    Species: Mouse
    Sample Types: Whole Cell
    Applications: Bioassay
  4. Thymosin &beta4-Enhancing Therapeutic Efficacy of Human Adipose-Derived Stem Cells in Mouse Ischemic Hindlimb Model
    Authors: JH Kim, IR Lim, CY Park, HJ Joo, JM Noh, SC Choi, SJ Hong, DS Lim
    Int J Mol Sci, 2020-03-21;21(6):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Sorsby Fundus Dystrophy Mutation in Tissue Inhibitor of Metalloproteinase 3 (TIMP3) promotes Choroidal Neovascularization via a Fibroblast Growth Factor-dependent Mechanism
    Authors: JH Qi, B Bell, R Singh, J Batoki, A Wolk, A Cutler, N Prayson, M Ali, H Stoehr, B Anand-Apte
    Sci Rep, 2019-11-22;9(1):17429.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Anti-CD160, Alone or in Combination With Bevacizumab, Is a Potent Inhibitor of Ocular Neovascularization in Rabbit and Monkey Models
    Authors: T Menguy, A Briaux, E Jeunesse, J Giustinian, A Calcei, T Guyon, J Mizrahi, H Haegel, V Duong, V Soler, P Brousset, A Bensussan, I Raymond Le, P Le Bouteil
    Invest. Ophthalmol. Vis. Sci., 2018-06-01;59(7):2687-2698.
    Species: Human
    Sample Types:
    Applications: In Vivo
  7. Ythdf2-mediated m6A mRNA clearance modulates neural development in mice
    Authors: M Li, X Zhao, W Wang, H Shi, Q Pan, Z Lu, SP Perez, R Suganthan, C He, M Bjørås, A Klungland
    Genome Biol., 2018-05-31;19(1):69.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  8. A Combination of Culture Conditions and Gene Expression Analysis Can Be Used to Investigate and Predict hES Cell Differentiation Potential towards Male Gonadal Cells.
    Authors: Kjartansdottir K, Reda A, Panula S, Day K, Hultenby K, Soder O, Hovatta O, Stukenborg J
    PLoS ONE, 2015-12-02;10(12):e0144029.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Antifibrotic and anti-inflammatory activity of the tyrosine kinase inhibitor nintedanib in experimental models of lung fibrosis.
    Authors: Wollin L, Maillet I, Quesniaux V, Holweg A, Ryffel B
    J Pharmacol Exp Ther, 2014-02-20;349(2):209-20.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J
    Nature, 2012-07-26;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Interactions between important regulatory proteins and human alphaB crystallin.
    Authors: Ghosh JG, Shenoy AK, Clark JI
    Biochemistry, 2007-05-08;46(21):6308-17.
    Species: Human
    Sample Types: Peptide
    Applications: ELISA-Based Protein Pin Array
  12. Neuritogenic activity of chondroitin/dermatan sulfate hybrid chains of embryonic pig brain and their mimicry from shark liver. Involvement of the pleiotrophin and hepatocyte growth factor signaling pathways.
    Authors: Li F, Shetty AK, Sugahara K
    J. Biol. Chem., 2006-12-04;282(5):2956-66.
    Species: Fish - Prionace glauca (Blue Shark)
    Sample Types: Peptide
    Applications: Bioassay
  13. Placenta growth factor in diabetic wound healing: altered expression and therapeutic potential.
    Authors: Cianfarani F, Zambruno G, Brogelli L, Sera F, Lacal PM, Pesce M, Capogrossi MC, Failla CM, Napolitano M, Odorisio T
    Am. J. Pathol., 2006-10-01;169(4):1167-82.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  14. Platelet-derived LIGHT induces inflammatory responses in endothelial cells and monocytes.
    Authors: Otterdal K, Smith C, Oie E, Pedersen TM, Yndestad A, Stang E, Endresen K, Solum NO, Aukrust P, Damas JK
    Blood, 2006-08-01;108(3):928-35.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

FAQs

  1. What receptors does FGF basic bind?

  2. Does human FGF basic show activity on mouse cells?
    • Yes, it does. The bioassay uses NR-6 mouse fibroblast cells.  There is 95% homology between the human and mouse protein and 98% homology between the human and mouse receptor.

View all Proteins and Enzyme FAQs

Reviews for Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein

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Recombinant Human FGF basic/FGF2/bFGF (157 aa) Protein
By Anonymous on 12/05/2021
Application: CellProlif
Reason for Rating: ECs were treated with FGF to test its effect on proliferation.