FGF17 Human

Fibroblast Growth Factor 17 Human Recombinant
Cat. No.
BT8657
Source
Escherichia Coli.
Synonyms
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
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.
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

FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa. 

Product Specs

Introduction
Fibroblast Growth Factor 17 (FGF17) is a member of the fibroblast growth factor family, known for its roles in cell growth and survival. FGFs are involved in various biological processes, such as embryonic development, tissue repair, and tumor progression. FGF17 is primarily found in the brain, specifically the cerebellum and cortex. Studies in mice suggest its involvement in the development of the central nervous system, bones, and blood vessels.
Description
Recombinant Human FGF17, produced in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 22.6kDa. It consists of 195 amino acids.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The FGF17 protein was lyophilized from a 0.2µm filtered concentrated solution in phosphate-buffered saline (PBS) at pH 7.4.
Solubility

To reconstitute the lyophilized FGF17, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions.

Stability
Lyophilized FGF17 is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. After reconstitution, FGF17 can be stored at 4°C for 2-7 days. For extended storage, adding a carrier protein like HSA or BSA (0.1%) is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 95.0% as determined by:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC).
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE).
Biological Activity
This product exhibits full biological activity compared to the standard. The ED50, determined by a cell proliferation assay using murine balb/c 3T3 cells, is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.
Synonyms
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
Source
Escherichia Coli.
Amino Acid Sequence
MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

Product Science Overview

Structure and Expression

FGF-17 is a heparin-binding growth factor that is preferentially expressed in the embryonic brain . It shares a high degree of homology with other members of the FGF family, being 60% identical to FGF-8 and 50% identical to FGF-18 . The human recombinant form of FGF-17 is typically produced in Escherichia coli (E. coli) and is available as a lyophilized powder . This recombinant protein is a single, non-glycosylated polypeptide chain containing 219 amino acids and has a molecular mass of approximately 25.2 kDa .

Biological Functions

FGF-17 functions as a ligand for gonadotropin-releasing hormone (GnRH), which plays a role in neuron ontogeny . It is involved in the control of differentiation and proliferation of midline cerebrum cells through temporal and spatial gradients . Additionally, FGF-17 has been implicated in congenital hypogonadotropic hypogonadism (CHH) due to mutations in its gene .

Applications in Biomedical Research

Recombinant FGF-17 is widely used in biomedical research for its ability to stimulate cellular processes such as mitogenesis, differentiation, migration, angiogenesis, and wound healing . It is particularly important for maintaining, expanding, and differentiating various types of cells in culture . For example, FGF-17 is used to study signaling interactions and pathways involved in neuron development and function.

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