FGF 8 Human

Fibroblast Growth Factor-8 Human Recombinant
Cat. No.
BT7644
Source
Escherichia Coli.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% as determined by 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

FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa. 

Product Specs

Introduction
FGF8, a member of the fibroblast growth factor family, plays a crucial role in various biological processes, including embryonic development, cell growth, and tissue repair. It exhibits mitogenic and cell survival activities and is involved in morphogenesis, tumor growth, and invasion. FGF8 supports androgen and anchorage-independent growth in mammary tumor cells, and its overexpression can enhance tumor growth and angiogenesis. In adults, FGF8 expression is primarily restricted to the testes and ovaries. As an embryonic epithelial factor, FGF8 participates in midbrain and limb development, organogenesis, embryo gastrulation, and left-right axis determination.
Description
Recombinant Human FGF 8, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 194 amino acids. It has a molecular weight of 22.5 kDa.
Physical Appearance
The product appears as a sterile, white powder obtained by lyophilization (freeze-drying).
Formulation

The product is lyophilized from a sterile aqueous solution with a pH of 0.1% TFA and filtered through a 0.2-micron filter.

Solubility

To reconstitute the lyophilized FGF-8, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions.

Stability

Lyophilized FGF-8 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. Once reconstituted, FGF-8 should be stored at 4°C for 2-7 days or below -18°C for extended periods. To ensure optimal stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advised. It is crucial to avoid repeated freeze-thaw cycles to maintain product integrity.

Purity

The purity of FGF-8 is greater than 95.0% as determined by SDS-PAGE analysis.

Biological Activity

The ED50, determined by the product's ability to induce proliferation in NR6-R 3T3 cells, is 0.915 ng/ml. This corresponds to a specific activity of 1.1 x 106 units/mg.

Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Source
Escherichia Coli.
Amino Acid Sequence
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGD
PFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.

Product Science Overview

Isoforms and Structure

In humans, FGF-8 exists in four isoforms: FGF-8a, FGF-8b, FGF-8e, and FGF-8f . These isoforms are generated through alternative splicing of the FGF-8 mRNA. Among these, FGF-8b is the predominant form and has been shown to possess significant oncogenic transforming capacity . The amino acid sequence of human FGF-8b shares 100% identity with its mouse counterpart .

Biological Functions

FGF-8 plays a pivotal role in embryogenesis, influencing the development of the brain, limbs, heart, and facial structures during gastrulation . It is also involved in the differentiation of embryonic stem cells into neural progenitor cells and further into dopaminergic neurons . Additionally, FGF-8 stimulates the proliferation of various cell types, including osteoblasts, endothelial cells, and myogenic cells .

Oncogenic Potential

FGF-8 is known to support the androgen and anchorage-independent growth of mammary tumor cells . Overexpression of FGF-8 has been associated with increased tumor growth and angiogenesis . This protein’s expression, once thought to be restricted to the testes and ovaries in adults, has been observed in several other organ systems .

Applications of Human Recombinant FGF-8

Human recombinant FGF-8 is optimized for use in cell culture, differentiation studies, and functional assays . It is utilized in various applications, including:

  • Differentiation of embryonic stem cells into neural progenitor cells .
  • Stimulation of osteoblast proliferation .
  • Proliferation of endothelial and myogenic cells .
  • Tumor growth studies of prostate and breast cancer .
  • Protection of hippocampal cultures from oxidative stress .
Quality and Purity

Research-grade human recombinant FGF-8 is typically sterile-filtered before lyophilization, with endotoxin levels below 0.1 ng/μg and purities exceeding 95% . The biological activity of each batch is tested in appropriate bioassays to ensure reproducibility in cell culture experiments .

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