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

Carrier Free

Catalog # Availability Size / Price Qty
231-BC-025/CF

With Carrier

Catalog # Availability Size / Price Qty
231-BC-025
Recombinant Human FGF acidic/FGF1 (aa 2-155) Protein Bioactivity
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Citations (5)
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Recombinant Human FGF acidic/FGF1 (aa 2-155) 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. 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
Analysis
Ala2
Predicted Molecular Mass
17 kDa

Product Datasheets

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231-BC (with carrier)

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231-BC/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.

231-BC

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, TCEP and EDTA with BSA as a carrier protein.
Reconstitution Reconstitute at 10 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 °C under sterile conditions after reconstitution.

231-BC/CF

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, TCEP and EDTA.
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 °C under sterile conditions after reconstitution.

Scientific Data

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

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.

SDS-PAGE Recombinant Human FGF acidic/FGF1 (aa 2-155) Protein SDS-PAGE View Larger

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.

Reconstitution Calculator

Reconstitution Calculator

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Background: FGF acidic/FGF1

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).

References
  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.
Long Name
Fibroblast Growth Factor acidic
Entrez Gene IDs
2246 (Human); 14164 (Mouse); 25317 (Rat); 281160 (Bovine)
Alternate Names
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

Citations for Recombinant Human FGF acidic/FGF1 (aa 2-155) 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.

5 Citations: Showing 1 - 5
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  1. Gut Microbiota Modulate CD8�T Cell Responses to Influence Colitis-Associated Tumorigenesis
    Authors: 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
    Cell Rep, 2020;31(1):107471.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Expansion of Human iPSC-Derived Ureteric Bud Organoids with Repeated Branching Potential
    Authors: SI Mae, M Ryosaka, S Sakamoto, K Matsuse, A Nozaki, M Igami, R Kabai, A Watanabe, K Osafune
    Cell Rep, 2020;32(4):107963.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Increased FGF1-FGFRc expression in idiopathic pulmonary fibrosis.
    Authors: 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
    Respir Res, 2015;16(0):83.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. 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;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. The role of type V collagen fibril as an ECM that induces the motility of glomerular endothelial cells.
    Authors: Murasawa Y, Hayashi T, Wang PC
    Exp. Cell Res., 2008;314(20):3638-53.
    Species: Porcine
    Sample Types: Whole Cells
    Applications: Bioassay

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