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Recombinant Human FGF acidic/FGF1 (aa 2-155) Protein

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Recombinant Human FGF acidic/FGF1 (aa 2-155) (Catalog # 231-BC) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 0.015-0.15 ng/mL in the presence of 10 μg/mL of heparin.
Recombinant Human FGF acidic/FGF1 (aa 2-155) (Catalog # 231-BC) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 0.015-0.15 ng/mL in the presence of 10 μg/mL of ...read more
1 μg/lane of Recombinant Human FGF acidic/FGF1 (aa 2-155) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 19 kDa.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

View Available Formulations
Catalog# & Formulation Size Price
Standard Formulation
231-BC-025/CF
Carrier Free
231-BC-025/CF
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Recombinant Human FGF acidic/FGF1 (aa 2-155) Protein Summary

Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Rizzino, A. et al. (1988) Cancer Res. 48:4266; Thomas, K. et al. (1987) Methods Enzymol. 147:120. The ED50 for this effect is 0.015-0.15 ng/mL in the presence of 10 µg/mL of heparin.
Source
E. coli-derived human FGF acidic/FGF1 protein
Ala2-Asp155
Accession #
N-terminal Sequence
Ala2
Protein/Peptide Type
Recombinant Proteins
Gene
FGF1
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
17 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
231-BC in the following applications:

Packaging, Storage & Formulations

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 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, TCEP and EDTA with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGF acidic/FGF1 (aa 2-155) Protein

  • AFGF
  • alpha
  • alpha-ECGF
  • beta-ECGF
  • ECGF
  • ECGFB
  • ECGF-betaAcidic fibroblast growth factor
  • endothelial cell growth factor, beta
  • FGF acidic
  • FGF-1
  • FGFABeta-endothelial cell growth factor
  • FGF-alpha
  • fibroblast growth factor 1 (acidic)
  • GLIO703
  • HBGF1
  • HBGF-1
  • heparin-binding growth factor 1

Background

FGF acidic, also known as FGF1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types, stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It plays a number of roles in development, regeneration, and angiogenesis (1-3). Human FGF acidic shares 54% amino acid (aa) sequence identity with FGF basic and 17%-33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, mouse, porcine, and rat FGF acidic, respectively, and exhibits considerable species crossreactivity. Alternate splicing generates a truncated isoform of human FGF acidic that consists of the N-terminal 40% of the molecule and functions as a receptor antagonist (4). During its nonclassical secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of synaptotagmin 1 (5). It is released extracellularly as a disulfide-linked homodimer and is stored in complex with extracellular heparan sulfate (6). The ability of heparan sulfate to bind FGF acidic is determined by its pattern of sulfation, and alterations in this pattern during embryognesis thereby regulate FGF acidic bioactivity (7). The association of FGF acidic with heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors (8, 9). Ligation triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF complexes (10). Internalized FGF acidic can translocate to the cytosol with the assistance of Hsp90 and then migrate to the nucleus by means of its two nuclear localization signals (11-13). The phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol where it is dephosphorylated and degraded (14, 15). Intracellular FGF acidic functions as a survival factor by inhibiting p53 activity and proapoptotic signaling (16).

  1. Jaye, M. et al. (1986) Science 233:541.
  2. Galzie, Z. et al. (1997) Biochem. Cell Biol. 75:669.
  3. Presta, M. et al. (2005) Cytokine Growth Factor Rev. 16:159.
  4. Yu, Y.L. et al. (1992) J. Exp. Med. 175:1073.
  5. Rajalingam, D. et al. (2007) Biochemistry 46:9225.
  6. Guerrini, M. et al. (2007) Curr. Pharm. Des. 13:2045.
  7. Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
  8. Robinson, C.J. et al. (2005) J. Biol. Chem. 280:42274.
  9. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
  10. Wiedlocha, A. and V. Sorensen (2004) Curr. Top. Microbiol. Immunol. 286:45.
  11. Wesche, J. et al. (2006) J. Biol. Chem. 281:11405.
  12. Imamura, T. et al. (1990) Science 249:1567.
  13. Wesche, J. et al. (2005) Biochemistry 44:6071.
  14. Wiedlocha, A. et al. (2005) Mol. Biol. Cell 16:794.
  15. Nilsen, T. et al. (2007) J. Biol. Chem. 282:26245.
  16. Bouleau, S. et al. (2005) Oncogene 24:7839.

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Recombinant Human
FGF acidic/FGF1 (aa 2 ...
231-BC
Recombinant Human FGF acidic/FGF1 (aa 2-155) Protein
Species: Hu
Applications: Bioactivity

Publications for FGF acidic/FGF1 (231-BC)(6)

We have publications tested in 2 confirmed species: Human, Porcine.

We have publications tested in 1 application: Bioassay.


Filter By Application
Bioassay
(6)
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Human
(5)
Porcine
(1)
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Showing Publications 1 - 6 of 6.
Publications using 231-BC Applications Species
SI Mae, M Ryosaka, S Sakamoto, K Matsuse, A Nozaki, M Igami, R Kabai, A Watanabe, K Osafune Expansion of Human iPSC-Derived Ureteric Bud Organoids with Repeated Branching Potential Cell Rep, 2020-07-28;32(4):107963. 2020-07-28 [PMID: 32726627] (Bioassay, Human) Bioassay Human
AI Yu, L Zhao, KA Eaton, S Ho, J Chen, S Poe, J Becker, A Gonzalez, D McKinstry, M Hasso, J Mendoza-Ca, J Whitfield, C Koumpouras, PD Schloss, EC Martens, GY Chen Gut Microbiota Modulate CD8�T Cell Responses to Influence Colitis-Associated Tumorigenesis Cell Rep, 2020-04-07;31(1):107471. 2020-04-07 [PMID: 32268087] (Bioassay, Human) Bioassay Human
MacKenzie B, Korfei M, Henneke I, Sibinska Z, Tian X, Hezel S, Dilai S, Wasnick R, Schneider B, Wilhelm J, El Agha E, Klepetko W, Seeger W, Schermuly R, Gunther A, Bellusci S Increased FGF1-FGFRc expression in idiopathic pulmonary fibrosis. Respir Res, 2015-07-03;16(0):83. 2015-07-03 [PMID: 26138239] (Bioassay, Human) Bioassay Human
Kanehira M, Kikuchi T, Santoso A, Tode N, Hirano T, Ohkouchi S, Tamada T, Sugiura H, Harigae H, Ichinose M Human marrow stromal cells downsize the stem cell fraction of lung cancers by fibroblast growth factor 10. Mol Cell Biol, 2014-05-27;34(15):2848-56. 2014-05-27 [PMID: 24865969] (Bioassay, Human) Bioassay Human
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 Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, Human) Bioassay Human
Murasawa Y, Hayashi T, Wang PC The role of type V collagen fibril as an ECM that induces the motility of glomerular endothelial cells. Exp. Cell Res., 2008-09-25;314(20):3638-53. 2008-09-25 [PMID: 18845143] (Bioassay, Porcine) Bioassay Porcine

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Bioinformatics

Gene Symbol FGF1
Uniprot