FGF5 Human

Fibroblast Growth Factor-5 Human Recombinant
Cat. No.
BT9462
Source
Escherichia Coli.
Synonyms
Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.
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

FGF5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 252 amino acids and having a molecular mass of 27.7kDa.
The FGF-5 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Fibroblast Growth Factor-5 (FGF5), a member of the FGF family, is a mitogenic peptide. Recombinant human FGF5 (rhFGF5) exhibits mitogenic activity on Balb/3T3 fibroblasts and bovine heart endothelial cells in vitro. It also acts as a muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF5 is believed to have crucial roles in embryology and neurobiology. During development, FGF5 mRNA is initially observed in the embryoblast and later in the lateral somatic mesoderm and myotomes. In the mesoderm, it might contribute to angiogenesis. In the myotomes, particularly those cranial to the tail region, FGF5 may play a role in delaying the terminal differentiation of myoblasts during cell migration.
Description
Recombinant Human FGF5, produced in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 27.7 kDa. It comprises 252 amino acids. The purification of FGF-5 is carried out using proprietary chromatographic methods.
Physical Appearance
White, lyophilized powder, sterile-filtered.
Formulation
FGF-5 protein was lyophilized from a 0.2µm filtered solution containing 10mM sodium phosphate, 100mM sodium chloride, at pH 7.5.
Solubility
For reconstitution of lyophilized FGF5, sterile 18M-cm H₂O is recommended at a concentration not less than 100µg/ml. This solution can be further diluted into other aqueous solutions.
Stability
Lyophilized FGF5, while stable at room temperature for up to 3 weeks, should ideally be stored desiccated at a temperature below -18°C. After reconstitution, FGF-5 should be stored at 4°C for a period of 2-7 days. For long-term storage, it is recommended to store it below -18°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.
Source
Escherichia Coli.
Amino Acid Sequence
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.

Product Science Overview

Structure and Expression

FGF-5 is a secreted, heparin-binding protein with a molecular weight of approximately 27.7 kDa . It is expressed in various tissues, including the mesenchyme, skeletal muscles, central nervous system, and hair follicles . The human recombinant form of FGF-5 is typically produced in Escherichia coli and is available as a lyophilized powder suitable for cell culture .

Biological Functions

FGF-5 plays a crucial role in several physiological processes:

  1. Hair Growth Regulation: FGF-5 is known to regulate the hair growth cycle. Its inactivation in mice leads to the angora phenotype, characterized by long hair . In humans, FGF-5 causes the regression of hair follicles, thereby controlling hair length .

  2. Neurotrophic Activity: In the peripheral nervous system, FGF-5 acts as a muscle-derived trophic factor for motor neurons. It demonstrates neurotrophic activity in vivo and influences astroglial characteristics in vitro .

  3. Oncogenic Potential: FGF-5 functions as an oncogene in glioblastoma due to its autocrine and paracrine functions. Its expression is elevated in human astrocytic brain tumors, which is linked to increased malignancy .

  4. Cell Differentiation and Proliferation: FGF-5 promotes cell differentiation and proliferation by binding to FGF receptor 1 and FGF receptor 2 (FGFR1 and FGFR2, respectively) . It plays an important regulatory role in skeletal muscle development and has been identified in neurons of the limbic system, especially those of the olfactory bulb and pyramidal cells of the hippocampus .

Applications

Human recombinant FGF-5 is widely used in research and biotechnology. It has been utilized for the induction of differentiation in various embryonic stem cell lines and for studying the mechanisms of hair growth and neurotrophic activity . Additionally, FGF-5’s role in oncogenesis makes it a potential target for cancer research and therapy .

Physical Form and Storage

The human recombinant FGF-5 is typically lyophilized from a solution containing MOPS, sodium sulfate, EDTA, DTT, and trehalose, with bovine serum albumin as a stabilizer . It is recommended to store the lyophilized powder at -20°C to maintain its stability and avoid repeated freeze-thaw cycles .

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