FGF-2 Bovine
Fibroblast Growth Factor-Basic Bovine Recombinant
Cat. No.
BT9012
Source
Escherichia Coli.
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% 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 dditives or household chemicals.
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Description
FGF-2 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17250 Dalton. The Fibroblast Growth Factor 2 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Fibroblast growth factor-basic (FGF-basic), also known as FGF-2, is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and angiogenic activities and bind heparin. FGF-basic is involved in various biological processes, including wound healing, limb and nervous system development, and tumor growth. The mRNA for this gene undergoes alternative translation from AUG and non-AUG (CUG) initiation codons and contains multiple polyadenylation sites, resulting in five distinct isoforms with different properties. The AUG-initiated form is primarily cytosolic and responsible for the autocrine and paracrine effects of FGF-basic, while the CUG-initiated isoforms are localized in the nucleus and responsible for the intracrine effect. Heparin-binding growth factors, including FGF-basic, are potent mitogens for various cell types in vitro and act as angiogenic agents in vivo. The tissue distribution and concentration of these growth factors can vary.
Description
Recombinant Bovine FGF-2, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 155 amino acids, with a molecular mass of 17.25 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile, white lyophilized powder.
Formulation
The lyophilization of Bovine FGF-b was carried out from a sterile solution (1 mg/ml) containing 1% HSA.
Solubility
For reconstitution of the lyophilized Bovine Fibroblast Growth Factor-2, sterile 18 MΩ-cm H2O is recommended at a concentration not less than 100 µg/ml. Further dilutions can be prepared in other aqueous solutions.
Stability
Lyophilized Bovine Fibroblast Growth Factor 2, though stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Following reconstitution, Recombinant FGF-b Bovine should be stored at 4°C for 2-7 days. For long-term storage, it should be kept below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined by the following methods and exceeds 97.0%:
(a) RP-HPLC analysis.
(b) SDS-PAGE analysis.
(a) RP-HPLC analysis.
(b) SDS-PAGE analysis.
Biological Activity
The ED50 was determined to be less than 0.1 ng/ml, corresponding to a specific activity of 3 x 106 Units/mg. This was measured using a mitogenic assay with quiescent NR6R-3T3 fibroblasts.
Protein Content
Protein quantitation was performed using two independent methods:
1. UV spectroscopy at 280 nm, utilizing an absorbance value of 0.85 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is determined through the PC GENE computer analysis program for protein sequences (IntelliGenetics).
2. RP-HPLC analysis, utilizing a calibrated solution of Bovine FGF-2 as a Reference Standard.
1. UV spectroscopy at 280 nm, utilizing an absorbance value of 0.85 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is determined through the PC GENE computer analysis program for protein sequences (IntelliGenetics).
2. RP-HPLC analysis, utilizing a calibrated solution of Bovine FGF-2 as a Reference Standard.
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Ala-Gly-Ser.
Product Science Overview
Structure and Production
Recombinant bovine bFGF is a monomeric protein consisting of 145 amino acids and has a molecular weight of approximately 17 kDa . The DNA sequence encoding the mature chain of bovine bFGF is expressed in Escherichia coli to produce the recombinant protein . The protein is typically purified using chromatographic techniques to ensure high purity, often greater than 98% as determined by SDS-PAGE and HPLC .
Biological Functions
bFGF is a multifunctional growth factor that stimulates the proliferation and differentiation of various cell types, particularly those derived from mesodermal and neuroectodermal origins . It is involved in several critical biological processes, including:
- Angiogenesis: The formation of new blood vessels from pre-existing ones, which is essential for wound healing and tissue regeneration .
- Cell Growth and Differentiation: bFGF promotes the growth and differentiation of fibroblasts, endothelial cells, and other cell types .
- Wound Healing: Topical application of rb-bFGF has been shown to enhance the healing of burns, fresh wounds, and chronic wounds by promoting cell proliferation and tissue repair .
Applications
Recombinant bovine bFGF has a wide range of applications in both research and clinical settings:
- Wound Healing: rb-bFGF is used to accelerate the healing process in various types of wounds, including burns and surgical wounds .
- Tissue Engineering: It is employed in the development of tissue-engineered constructs to promote cell growth and tissue regeneration .
- Research: rb-bFGF is widely used in cell culture to maintain the proliferation of stem cells and other cell types .
Stability and Storage
The lyophilized form of recombinant bovine bFGF is stable for several years when stored at -20°C . Upon reconstitution, the protein can be stored in working aliquots at 2-8°C for up to one month or at -20°C for up to six months, with a carrier protein to prevent loss of activity . It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and functionality .
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