FGF 9 Rat

Fibroblast Growth Factor-9 Rat Recombinant
Cat. No.
BT8075
Source
Escherichia Coli.
Synonyms
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
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

Rat FGF9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.3kDa.
The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Rat and mouse FGF-9 share significant homology with human FGF-9. FGF-9 transcripts are present in brain and kidney tissue. As a member of the fibroblast growth factor (FGF) family, FGF-9 exhibits mitogenic and cell survival properties, contributing to various biological processes like embryonic development, cell growth, morphogenesis, tissue repair, and tumor progression. Initially identified as a secreted factor promoting glial cell growth in cultures, FGF-9 is primarily produced by neurons in the nervous system and potentially plays a role in glial cell development. Studies indicate that the expression of the mouse FGF-9 homolog relies on Sonic hedgehog (Shh) signaling. FGF-9 knockout mice exhibit a male-to-female sex reversal phenotype, suggesting its involvement in testicular embryogenesis. FGF-9 may contribute to glial cell growth and differentiation during development, gliosis in brain tissue repair after injury, neuronal cell differentiation and survival, and the stimulation of glial tumor growth.
Description
Recombinant Rat FGF9, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 207 amino acids with a molecular weight of 23.3 kDa. Purification of the recombinant mouse FGF-9 is achieved using proprietary chromatographic methods.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The FGF-9 was lyophilized from a sterile solution at a concentration of 1 mg/ml, containing 10 mM NaP (pH 7.5) and 75 mM Ammonium Sulfate.
Solubility
For reconstitution of the lyophilized Rat FGF-9, sterile 18 MΩ-cm H2O is recommended at a concentration not less than 100 µg/ml. This solution can be further diluted into other aqueous solutions as needed.
Stability
Lyophilized Rat Fibroblast Growth Factor-9, while stable at room temperature for 3 weeks, should ideally be stored desiccated at a temperature below -18 °C. After reconstitution, Rat Recombinant FGF9 can be stored at 4 °C for 2-7 days. For long-term storage, it is advisable to store at a temperature 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
Purity exceeding 95.0% as determined by: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Biological Activity
The ED50, determined by the dose-dependent proliferation of BAF3 cells expressing FGF receptors (measured via ³H-thymidine uptake), is < 0.5 ng/ml, corresponding to a specific activity of ≥ 2,000,000 Units/mg.
Synonyms
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
Source
Escherichia Coli.
Amino Acid Sequence
MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.

Product Science Overview

Discovery and Isolation

FGF-9 was initially isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells . In the nervous system, this protein is primarily produced by neurons and plays a crucial role in glial cell development .

Biological Functions

FGF-9 binds to its receptor with the help of heparin, which induces receptor dimerization, subsequent transphosphorylation, and downstream activation of several signaling pathways, including Erk, Akt, and PLCγ . These pathways are essential for various cellular processes such as proliferation, differentiation, and survival.

Expression and Regulation

The expression of the mouse homolog of FGF-9 is dependent on Sonic hedgehog (Shh) signaling . This signaling pathway is vital for the regulation of embryonic development and has been implicated in various developmental disorders and cancers.

Recombinant Production

Recombinant FGF-9 proteins are produced using various expression systems, including E. coli and baculovirus-infected insect cells . These recombinant proteins are used in research to study the biological functions of FGF-9 and its role in various diseases.

Applications in Research

Recombinant FGF-9 is widely used in cell culture studies to stimulate the proliferation of various cell types, including fibroblasts and glial cells . It is also used in studies investigating the role of FGF-9 in development, tissue repair, and cancer.

Storage and Stability

Recombinant FGF-9 proteins are typically lyophilized and stored at -20°C to -70°C to maintain their stability . They are reconstituted in sterile PBS or other suitable buffers before use in experiments.

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