FGF 8 Mouse
Fibroblast Growth Factor-8 Mouse Recombinant
Cat. No.
BT7715
Source
Escherichia Coli.
Synonyms
Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.
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
FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.
The FGF-8 is purified by proprietary chromatographic techniques.
The FGF-8 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Fibroblast growth factor 8 (FGF8) belongs to the fibroblast growth factor family. These factors exhibit diverse mitogenic and cell survival activities, playing crucial roles in various biological processes. These processes include embryonic development, cell growth, morphogenesis, tissue repair, and tumor progression (growth and invasion). Notably, FGF8 supports androgen-dependent and anchorage-independent growth in mammary tumor cells. Moreover, its overexpression is associated with increased tumor growth and angiogenesis. In adults, FGF8 gene expression is primarily confined to the testes and ovaries. Functionally, FGF8 acts as an embryonic epithelial factor, participating in midbrain and limb development, organogenesis, embryo gastrulation, and left-right axis determination.
Description
Recombinant Mouse FGF-8, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 246 amino acids, with a molecular weight of 28.1 kDa. The purification of FGF-8 is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder
Formulation
The FGF-8 protein was lyophilized from a 0.2 µm filtered concentrated solution in phosphate-buffered saline (PBS) at pH 7.4.
Solubility
For reconstitution, it is recommended to dissolve the lyophilized FGF-8 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 as needed.
Stability
Lyophilized FGF-8 demonstrates stability at room temperature for up to 3 weeks. However, for extended storage, it is advisable to store it desiccated below -18°C. Upon reconstitution, FGF-8 should be stored at 4°C for 2-7 days. For long-term storage, adding a carrier protein like 0.1% HSA or BSA is recommended. It is important to avoid repeated freeze-thaw cycles.
Purity
The purity is greater than 95.0% as determined by:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED50, determined by a dose-dependent cell proliferation assay using NR6R-3T3 mouse fibroblast cells, is less than 25 ng/ml in the presence of 0.1 µg/ml heparin. This corresponds to a specific activity exceeding 4.0 × 10⁴ units/mg.
Synonyms
Fibroblast growth factor 8, FGF-8, Androgen-induced growth factor, AIGF, Heparin-binding growth factor 8, HBGF-8, Fgf8.
Source
Escherichia Coli.
Amino Acid Sequence
QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR.
Product Science Overview
Discovery and Isoforms
FGF-8 was initially discovered as a growth factor essential for the androgen-dependent growth of mouse mammary carcinoma cells . The gene encoding FGF-8 undergoes alternative splicing, resulting in eight different isoforms, designated as FGF-8a to FGF-8h. However, only four of these isoforms (FGF-8a, FGF-8b, FGF-8e, and FGF-8f) are present in humans .
Functions and Mechanisms
FGF-8 is involved in a variety of biological processes, including:
- Embryonic Development: FGF-8 is crucial for setting up and maintaining the midbrain/hindbrain border, which acts as an organizer during development . It regulates the growth and differentiation of progenitor cells in this region, contributing to the formation of the midbrain and hindbrain structures .
- Cell Growth and Morphogenesis: FGF-8 promotes cell proliferation and differentiation, playing a significant role in tissue repair and regeneration .
- Tumor Growth and Invasion: FGF-8 has been implicated in the progression of certain cancers, including breast and prostate cancers .
Signaling Pathways
FGF-8 functions by binding to and activating high-affinity FGF receptors (FGFRs) on target cells. This interaction triggers a signal transduction cascade involving kinases and transcription factors, leading to various cellular effects such as mitogenesis, differentiation, migration, angiogenesis, and wound healing .
Applications in Biomedical Research
Recombinant FGF-8 proteins are widely used in biomedical research for various applications, including:
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