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

Source

E. coli-derived human FGF basic/FGF2/bFGF protein
Pro143-Ser288
Produced using non-animal reagents in an animal-free laboratory.

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.

N-terminal Sequence Analysis

Pro143 & Ala144

Predicted Molecular Mass

16 kDa

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.

The specific activity of Recombinant Human FGF basic/FGF2 is >8.0 x 10⁵ IU/mg, which is calibrated against the human FGF basic/FGF2 WHO International Standard (NIBSC code: 90/712).

Formulation, Preparation, and Storage

AFL3718

Formulation	Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl.
Reconstitution	Reconstitute at 100 μg/mL in 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.

Calculators

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.

Volume (to add to vial)

Mass (in vial)

Desired Reconstitution Concentration

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

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

Long Name

Fibroblast Growth Factor basic

Alternate Names

bFGF, FGF-2, FGF2, HBGF-2, Prostatropin

Entrez Gene IDs

2247 (Human); 14173 (Mouse); 281161 (Bovine); 403857 (Canine); 100033955 (Equine)

Gene Symbol

FGF2

UniProt

NP_001997.5 (Human)

Additional FGF basic/FGF2/bFGF Products

Product Documents for Recombinant Human FGF basic/FGF2/bFGF, Animal-Free Protein

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Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

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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