FGF 1 Human
Fibroblast Growth Factor-Acidic Human Recombinant
Cat. No.
BT5730
Source
Escherichia Coli.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
Fibroblast Growth Factor-acidic Human Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15.8kDa.
The FGF acidic is purified by proprietary chromatographic techniques.
The FGF acidic is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Acidic fibroblast growth factor (aFGF or FGF-1) is a member of the fibroblast growth factor (FGF) family. FGFs are involved in various biological processes, including embryonic development, cell growth, tissue repair, and angiogenesis. aFGF plays a role in endothelial cell migration and proliferation. It acts as a mitogen for various cell types, suggesting involvement in organogenesis. Multiple isoforms of aFGF exist due to alternative splicing. Heparin-binding growth factors, including aFGF, exhibit angiogenic properties and potent mitogenic activity. The tissue distribution and concentration of these growth factors can differ.
Description
Recombinant Human Fibroblast Growth Factor-acidic (FGF-1) is produced in E. coli. This non-glycosylated polypeptide chain consists of 140 amino acids, resulting in a molecular weight of approximately 15.8 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
White, sterile-filtered lyophilized powder.
Formulation
The protein was lyophilized from a sterile solution containing PBS at pH 7.4 and a concentration of 1 mg/mL.
Solubility
To reconstitute the lyophilized Fibroblast Growth Factor-acidic, dissolve in sterile 18 MΩ-cm H2O at 4°C to a concentration of 0.1-0.25 mg/mL. Let the solution sit undisturbed for 5 minutes at 4°C, then centrifuge briefly to remove any insoluble particles.
Stability
Lyophilized Fibroblast Growth Factor-1 remains stable at room temperature for up to 3 weeks. For long-term storage, store desiccated below -18°C. Reconstituted FGF-a should be stored at 4°C for 2-7 days. For extended storage after reconstitution, freeze aliquots below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined using the following methods, with a result of greater than 95%:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The half-maximal effective concentration (ED₅₀) is determined by measuring dose-dependent proliferation of mouse BALB/c 3T3 cells. It is less than 0.5 ng/mL, corresponding to a specific activity greater than 2,000,000 IU/mg.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Source
Escherichia Coli.
Amino Acid Sequence
MFNLPPGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SVGEVYIKST ETGQYLAMDT DGLLYGSQTP NEECLFLERL EENHYNTYIS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
Product Science Overview
Structure and Characteristics
FGF-acidic is a single-chain polypeptide consisting of 140 amino acids and has a molecular weight of approximately 15.8 kDa . It is produced in a non-glycosylated form in Escherichia coli (E. coli) and is purified using proprietary chromatographic techniques . The protein is known for its ability to bind heparin, which is essential for its interaction with fibroblast growth factor receptors (FGFRs) .
Biological Functions
FGF-acidic is a potent activator of DNA synthesis, cell proliferation, and chemotaxis . It plays a crucial role in various physiological processes, including:
- Development: FGF-acidic is involved in the development of multiple tissues and organs. It is highly expressed in the central and peripheral nervous systems .
- Regeneration: The protein promotes tissue repair and regeneration by stimulating the proliferation of various cell types, including fibroblasts, endothelial cells, and neurons .
- Angiogenesis: FGF-acidic is a key player in angiogenesis, the formation of new blood vessels, which is vital for wound healing and tissue growth .
Mechanism of Action
FGF-acidic exerts its effects by binding to specific FGFRs on the cell surface. This binding triggers a cascade of intracellular signaling pathways, including the activation of protein kinase C and the inhibition of p53 and proapoptotic signaling . These pathways promote cell survival, proliferation, and differentiation .
Applications
Human recombinant FGF-acidic is widely used in research and therapeutic applications. Some of its notable uses include:
- Cell Culture: FGF-acidic is used as a growth factor in cell culture media to promote the proliferation of various cell types .
- Tissue Engineering: The protein is incorporated into biomaterials to enhance tissue regeneration and repair .
- Neuroscience Research: FGF-acidic is used to study neural development and neuroprotection .
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