FGF2 (147), Bovine

Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant
Cat. No.
BT8953
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.

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-basic (147 a.a.) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 147 amino acid and having a molecular mass of approximately 16.5kDa.
FGF2 (147) is purified by proprietary chromatographic techniques.

Product Specs

Introduction

Fibroblast growth factor-basic (FGF-basic), also known as FGF2, is a member of the fibroblast growth factor (FGF) family. These proteins exhibit broad mitogenic and angiogenic activities and bind to heparin. FGF-basic is involved in various biological processes, including wound healing, tumor growth, and development of the nervous system and limbs. The mRNA for FGF-basic can be translated from different initiation codons (AUG and CUG) and contains multiple polyadenylation sites, giving rise to five isoforms with distinct properties. CUG-initiated isoforms are localized in the nucleus and have intracrine effects, while the AUG-initiated isoform is primarily cytosolic and exerts paracrine and autocrine effects. Heparin-binding growth factors, including FGF-basic, act as potent mitogens for various cell types in vitro and as angiogenic agents in vivo. The tissue distribution and concentration of these growth factors can vary.

Description

Recombinant Bovine Fibroblast Growth Factor-basic (147 a.a.), produced in E. coli, is a non-glycosylated polypeptide chain comprising 147 amino acids. It has a molecular mass of about 16.5 kDa. FGF2 (147) is purified using proprietary chromatographic techniques.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in PBS with a pH of 7.4.

Solubility

To reconstitute the lyophilized Fibroblast Growth Factor-basic (147 a.a.), it is recommended to use sterile PBS at a concentration of at least 100 µg/ml. The reconstituted solution can be further diluted in other aqueous solutions.

Stability

Lyophilized FGF2 remains stable at room temperature for up to 3 weeks. However, it is recommended to store it desiccated below -18°C. After reconstitution, Fibroblast Growth Factor-basic (147 a.a.) 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

The purity is determined using the following methods:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE
The purity is greater than 97.0%.

Biological Activity

The ED50, determined by a cell proliferation assay using murine balb/c 3T3 cells, is less than 0.1 ng/ml. This corresponds to a specific activity of greater than 1.0 × 107 IU/mg.

Synonyms

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.

Source

Escherichia Coli.

Amino Acid Sequence

MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS.

Product Science Overview

Introduction

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF2 or bFGF, is a member of the fibroblast growth factor family. This family of growth factors is known for its broad mitogenic and angiogenic activities, playing crucial roles in various biological processes such as wound healing, limb and nervous system development, and tumor growth .

Structure and Production

The recombinant bovine FGF-basic is a non-glycosylated polypeptide chain consisting of 147 amino acids, with a molecular mass of approximately 16.5 kDa . It is produced in Escherichia coli (E. coli) using proprietary chromatographic techniques to ensure high purity and stability . The amino acid sequence of this recombinant protein is as follows:

MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS
Biological Activity

FGF-basic binds to heparin and exhibits potent mitogenic effects on a variety of cell types in vitro. It is also a significant angiogenic agent in vivo . The biological activity of FGF-basic is determined by its ability to stimulate cell proliferation. For instance, the ED50 (the effective dose at which 50% of its maximal effect is observed) for cell proliferation using murine BALB/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of greater than 1.0 × 10^7 IU/mg .

Applications

Recombinant bovine FGF-basic has been widely used in research and clinical settings due to its ability to promote wound healing. It has been applied topically to manage burns, fresh wounds, and chronic wounds . The protein’s interaction with target cell surfaces triggers active repair processes, stimulating cell division, proliferation, migration, and differentiation, thereby accelerating wound healing and improving the quality of the healed tissue .

Stability and Storage

The lyophilized form of FGF-basic is stable at room temperature for up to three weeks. However, for long-term storage, it should be kept desiccated below -18°C. Upon reconstitution in sterile PBS, the solution should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .

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