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Recombinant Human FGF acidic/FGF1, Animal-Free Protein

Catalog #: AFL232 Datasheet
Catalog # Availability Size / Price Qty
AFL232-01M
AFL232-025
Recombinant Human FGF acidic/FGF1, Animal-Free Protein Bioactivity
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Recombinant Human FGF acidic/FGF1, Animal-Free Protein Summary

Learn more about Animal-Free Recombinant Proteins

Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.

Product Specifications

Purity
>97%, 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. Rizzino, A. et al. (1988) Cancer Res. 48:4266; Thomas, K. et al. (1987) Methods Enzymol. 147:120. The ED50 for this effect is 0.0150-0.150 ng/mL in the presence of 10 µg/mL of heparin.
Source
E. coli-derived human FGF acidic/FGF1 protein
Phe16-Asp155, with an N-terminal Met
Produced using non-animal reagents in an animal-free laboratory.
Accession #
NP_000791
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
15.5 kDa

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AFL232

Product Datasheet

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.

AFL232

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA.
Reconstitution Reconstitute at 0.2 mg/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.

Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.

Scientific Data

Bioactivity Recombinant Human FGF acidic/FGF1, Animal-Free Protein Bioactivity View Larger

Animal-FreeTMRecombinant Human FGF acidic/FGF1 (Catalog # AFL232) stimulates cell proliferation in the NR6R‑3T3 mouse fibroblast cell line. The ED50 for this effect is 0.1-0.3 ng/mL in the presence of 10 μg/mL heparin.

SDS-PAGE Recombinant Human FGF acidic/FGF1, Animal-Free Protein SDS-PAGE View Larger

1 μg/lane of Animal-FreeTMRecombinant Human FGF acidic/FGF1 (Catalog # AFL232) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 16 kDa.

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 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 cross-reactivity. 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 embryogenesis 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

Manufacturing Specifications

Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.  

 Production

  • All molecular biology procedures use animal-free media and dedicated labware.
  • Dedicated fermentors are utilized in committed animal-free areas.

Purification

  • Protein purification columns are animal-free.
  • Bulk proteins are filtered using animal-free filters.
  • Purified proteins are stored in animal-free containers in a dedicated cold storage room.

    Quality Assurance

    • Low Endotoxin Level.
    • No impairment of biological activity.
    • High quality product obtained under stringent conditions.
    • For ex vivo research or bioproduction, additional documentation can be provided.

    Please read our complete Animal-Free Statement

    FAQs

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