Recombinant Human FGF-acidic/FGF1

 

Recombinant (E.coli)

Lyophilizate, sterile-filtered

 

Cat.No.     RP1003                 10μg/50μg              store at -20 ℃

 

Synonyms :  Fibroblast Growth Factor-acidic, FGF-1, HBGF-1, ECGF-beta, FGF-a

 

Description:  Fibroblast Growth Factor-1 Human Recombinant (FGF-1) produced in E.coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17460 Dalton. The FGF1 is purified by proprietary chromatographic techniques.

 

Source:        Escherichia Coli.

 

Purity:         Greater than 90.0% as determined by SDS-PAGE.

Endotoxin Level: Endotoxin level is less than 0.1 ng per μg (1EU/μg) as determined by the LAL method.

Biological Activity: The ED50, calculated by the dose-dependent proliferation of mouse BALB/c 3T3 cells is <1.0 ng/ml, corresponding to a Specific Activity of 1 x 1,000,000 IU/mg.

Amino acid sequence:

MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD

Formulation: The protein was lyophilized from a concentrated (0.2mg/ml) sterile solution containing 10mM sodium phosphate pH=7.4.

Solubility: It is recommended to reconstitute the lyophilized FGF1 in sterile 18MΩ-cm H₂O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability: Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -20°C. Upon reconstitution FGF1 should be stored at 4°C between 2-7 days and for future use below -20°C.
          For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles. Recommend to aliquot the protein into smaller quantities for optimal storage.

Usage: Follow the instructions on the vial. Centrifuge the vial at 4℃ before opening to recover the entire contents.

The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

 

Background

FGF acidic, also known as FGF1, ECGF, and HBGF1, 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 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 no classical 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 recept 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.