FGF 1 Mouse

Fibroblast Growth Factor-Acidic Mouse Recombinant
Cat. No.
BT5837
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 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 Mouse Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9kDa.

The FGF acidic is purified by proprietary chromatographic techniques. 

Product Specs

Introduction

Acidic fibroblast growth factor (FGF-1) belongs to the FGF family, known for their roles in cell growth, survival, and various biological processes. FGFs contribute to embryonic development, tissue repair, and angiogenesis (blood vessel formation). FGF-1 specifically influences endothelial cell activity, crucial for blood vessel formation. It acts as a mitogen, promoting cell division in various cell types derived from mesoderm and neuroectoderm, highlighting its role in organ development. Multiple forms of FGF-1 exist due to alternative splicing, leading to variations in its protein structure. These growth factors stimulate cell growth in various tissues and are potent mitogens for different cell types in laboratory settings. The distribution and concentration of these growth factors vary across tissues.

Description

Recombinant Mouse Fibroblast Growth Factor-acidic (FGF-1), expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 141 amino acids. This protein has a molecular weight of 15.9 kDa.

FGF-acidic is purified using specialized chromatographic techniques.

Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in phosphate-buffered saline (PBS) at pH 7.5.

Solubility
To reconstitute the lyophilized Fibroblast Growth Factor-acidic, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Fibroblast Growth Factor-1 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it should be kept desiccated at or below -18°C. After reconstitution, FGF-a should be stored at 4°C for no more than 2-7 days. For prolonged storage, store below -18°C. Avoid repeated freeze-thaw cycles.
Purity

Purity is determined to be greater than 95.0% as assessed by SDS-PAGE analysis.

Biological Activity

The ED50, determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2 ng/ml. This corresponds to a Specific Activity of 5 x 106 IU/mg.

Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Source
Escherichia Coli.
Amino Acid Sequence

MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

Product Science Overview

Structure and Function

FGF-acidic is a single-chain protein with a molecular weight of approximately 15.8 kDa . It binds to and activates high-affinity FGF receptors (FGFR1-4) on target cells, initiating a signal transduction cascade involving kinases and transcription factors . This activation leads to several cellular effects, such as:

  • Mitogenesis: Promoting cell division and proliferation.
  • Differentiation: Guiding cells to develop into specific types.
  • Migration: Assisting cells in moving to their required locations.
  • Angiogenesis: Formation of new blood vessels.
  • Wound Healing: Facilitating tissue repair and regeneration .
Biological Activity

FGF-acidic is highly regulated and acts as a direct angiogenesis factor . It is known for its mitogenic activity, particularly targeting endothelial cells . However, unlike some other FGFs, FGF-acidic lacks a signal peptide segment, meaning it is not secreted via the endoplasmic reticulum (ER) and Golgi bodies .

Applications in Research

Recombinant FGF-acidic proteins are widely used in biomedical research. They are essential for maintaining, expanding, and differentiating various cell types in culture . Some specific applications include:

  • Stem Cell Research: Maintaining pluripotent stem cells.
  • Cancer Research: Studying pathways involved in tumor growth and angiogenesis.
  • Developmental Biology: Investigating processes like mesoderm induction and inner ear development .
Clinical Implications

Due to its role in angiogenesis, FGF-acidic is considered a potential oncogene. Its overexpression is closely associated with several cancers, including those affecting the eyes, joints, and pancreas . Understanding the regulation and function of FGF-acidic can provide insights into therapeutic targets for these diseases.

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