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Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF

Catalog #: 3718-FB
12 Citations 1 Review Datasheet / COA / SDS
GMP Version Available: 3718-GMP
GMP
Catalog # Availability Size / Price Qty
3718-FB-01M
3718-FB-025
3718-FB-100
3718-FB-010
Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein Bioactivity
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Product Details
Citations (12)
FAQs
Supplemental Products
Reviews (1)
Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.01 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 0.1-0.6 ng/mL.
Source
E. coli-derived human FGF basic/FGF2/bFGF protein
Ala144-Ser288
Accession #
NP_001997
N-terminal Sequence
Analysis
Ala144
Predicted Molecular Mass
16 kDa

Product Datasheets

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3718-FB

Product Datasheet
COA
SDS

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.

3718-FB

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 with polar packs. 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 (145 aa) Protein Bioactivity View Larger

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 0.1-0.6 ng/mL.

Bioactivity View Larger

iPSC-derived cerebral organoids (day 45) were cultured using Cultrex UltiMatrix RGF Basement Membrane Extract (Catalog # BME001-05) and brain organoid culture medium, which includes Recombinant Human FGF-basic (Catalog # 3718-FB) and Recombinant Human Noggin (Catalog # 6057-NG), along with the other reagents listed in the brain organoid culture recipe. Cerebral organoids were stained for Syto6 (blue), Pax6 (red), and Vimentin (green). (A) Image taken at 4x magnification. (B) An enlarged view of the area shown within the white box in part A of the figure. (C) Image taken at 15x magnification. Images courtesy of LifeCanvas Technologies.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: FGF basic/FGF2/bFGF

FGF basic (also known as FGF-2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3). Superfamily members are characterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF-1) and FGF basic (FGF-2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which utilize atypical CUG codons, and one that initiates at an AUG start site (4-6). The four CUG start sites generate high molecular weight (HMW) FGF basic. There is a 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation, and possess one or more nuclear localization signals (NLS) (7-9). The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss). It is, however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10). In place of a ss, there is purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11). Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, an effect attributed to the presence of acid proteases (12). The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117 (13). There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7). Human 146 aa FGF basic is 97% aa identical to mouse FGF basic (14).

References
  1. Sorenson, V. et al. (2006) BioEssays 28:504.
  2. Kardami, E. et al. (2004) Cardiovasc. Res. 63:458.
  3. Nugent, M.A. and R.V. Lozzo (2000) Int. J. Biochem. Cell Biol. 32:115.
  4. Abraham, J.A. et al. (1986) EMBO J. 5:2523.
  5. Prats, H. et al. (1989) Proc. Natl. Acad. Sci. USA 86:1836.
  6. Arnaud, E. et al. (1999) Mol. Cell. Biol. 19:505.
  7. Foletti, A. et al. (2003) Cell. Mol. Life Sci. 60:2254.
  8. Arese, M. et al. (1999) Mol. Biol. Cell 10:1429.
  9. Pintucci, G. et al. (1996) Mol. Biol. Cell 7:1249.
  10. Nickel, W. (2005) Traffic 6:607.
  11. SwissProt # P09038.
  12. Klagsbrun, M. et al. (1987) Proc. Natl. Acad. Sci. USA 84:1839.
  13. Bailly, K. et al. (2000) FASEB J. 14:333.
  14. Hebert, J.M. et al. (1990) Dev. Biol. 138:454.
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 (145 aa) Protein, CF

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.

12 Citations: Showing 1 - 10
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  1. The Role of Interstitial Fluid Pressure in Cerebral Porous Biomaterial Integration
    Authors: F Bonini, S Mosser, FM Mor, A Boutabla, P Burch, A Béduer, A Roux, T Braschler
    Brain sciences, 2022;12(4):.
    Species: Human
    Sample Types: Organoid
    Applications: Bioassay
  2. A common transcriptional mechanism involving R-loop and RNA abasic site regulates an enhancer RNA of APOE
    Authors: JA Watts, C Grunseich, Y Rodriguez, Y Liu, D Li, JT Burdick, A Bruzel, RJ Crouch, RW Mahley, SH Wilson, VG Cheung
    Nucleic Acids Research, 2022;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. A novel antibody for the detection of alternatively spliced secreted KLOTHO isoform in human plasma
    Authors: S Jadhav, S Tripathi, A Chandrekar, SS Waikar, LL Hsiao
    PLoS ONE, 2021;16(1):e0245614.
    Species: Human
    Sample Types: Protein
    Applications: ELISA Capture
  4. Coactivation of GSK3beta and IGF-1 Attenuates Amyotrophic Lateral Sclerosis Nerve Fiber Cytopathies in SOD1 Mutant Patient-Derived Motor Neurons
    Authors: HC Ting, HI Yang, HJ Harn, IM Chiu, HL Su, X Li, MF Chen, TJ Ho, CA Liu, YJ Tsai, TW Chiou, SZ Lin, CY Chang
    Cells, 2021;10(10):.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Bioassay
  5. The Use of Human Serum Samples to Study Malignant Transformation: A Pilot Study
    Authors: AN Holowatyj, B Gigic, CA Warby, J Ose, T Lin, P Schrotz-Ki, CM Ulrich, JJ Bernard
    Cells, 2021;10(10):.
    Species: Human
    Sample Types: Serum
    Applications: Bioassay
  6. Regulation of prefrontal patterning and connectivity by retinoic acid
    Authors: M Shibata, K Pattabiram, B Lorente-Ga, D Andrijevic, SK Kim, N Kaur, SK Muchnik, X Xing, G Santpere, AMM Sousa, N Sestan
    Nature, 2021;0(0):.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Cell Culture
  7. Low dose amiodarone reduces tumor growth and angiogenesis
    Authors: E Steinberg, A Fluksman, C Zemmour, K Tischenko, A Karsch-Blu, Y Brill-Karn, AE Birsner, RJ D'Amato, O Benny
    Sci Rep, 2020;10(1):18034.
    Species: Mouse
    Sample Types: In Vivo
    Applications: Bioassay
  8. Physical and functional interactome atlas of human receptor tyrosine kinases.
    Authors: Salokas K, Liu X, Ohman T, Chowdhury I, Gawriyski L, Keskitalo S, Varjosalo M
    EMBO Rep, 0;23(6):e54041.
    Species: Human
    Sample Types: Transfected Whole Cells
    Applications: Bioassay
  9. Generating Patient-Derived Gliomas within Cerebral Organoids.
    Authors: Linkous A, Fine H
    STAR Protoc, 0;1(1):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. A Stage-Specific OTX2 Regulatory Network and Maturation-Associated Gene Programs Are Inherent Barriers to RPE Neural Competency.
    Authors: Tangeman J, Perez-Estrada J, Van Zeeland E, Liu L, Danciutiu A, Grajales-Esquivel E, Smucker B, Liang C, Del Rio-Tsonis K
    Front Cell Dev Biol, 0;10(0):875155.
    Species: Chicken
    Sample Types: Whole Tissue
    Applications: Bioassay
  11. CD44 promotes angiogenesis in myocardial infarction through regulating plasma exosome uptake and further enhancing FGFR2 signaling transduction.
    Authors: Zhang Q, Chen L, Huang L, Cheng H, Wang L, Xu L, Hu D, He C, Fu C, Wei Q
    Mol Med, 0;28(1):145.
    Species: Human
    Sample Types: Transfected Whole Cells
    Applications: Bioassay
  12. Glioblastoma patient-derived cell-based phenotypic drug screening and identification of possible action mechanisms through proteomic analysis.
    Authors: Kim Y, Kim H, Jung D, Kang D, Nam D, Nam H, Cho H
    STAR Protoc, 0;2(4):100849.
    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.

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Reconstitution Buffers

Reconstitution Buffer 1 (PBS)

RB01
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Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF
By Anonymous on 07/31/2020
Application: Stem/Immune cell maintenance or differentiation

Supplementing media for growing iPS-derived cortical spheroids

Stem/Immune cell maintenance or differentiation Recombinant Human FGF basic/FGF2/bFGF (145 aa) Protein, CF 3718-FB