FGF 9 Mouse
Fibroblast Growth Factor-9 Mouse Recombinant
Cat. No.
BT8002
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.
(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 
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Description
Fibroblast Growth Factor-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids and having a molecular mass of 23308 Dalton.
The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.
The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Rat and mouse FGF-9 exhibit significant homology with human FGF-9. FGF-9 transcripts are present in brain and kidney tissues. As a member of the fibroblast growth factor (FGF) family, FGF-9 possesses broad mitogenic and cell survival properties and is implicated in various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, and tumor growth and invasion. FGF9 was initially identified as a secreted factor promoting the growth of cultured glial cells. Within the nervous system, it is primarily produced by neurons and may play a crucial role in glial cell development. Notably, the expression of the mouse homolog of the FGF-9 gene is regulated by Sonic hedgehog (Shh) signaling. Mice deficient in this homolog 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 and regeneration after injury, neuronal cell differentiation and survival, and the stimulation of glial tumor growth.
Description
Recombinant Mouse Fibroblast Growth Factor-9, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 205 amino acids. It has a molecular mass of 23,308 Daltons. The purification of Recombinant Mouse FGF-9 is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized in a buffer containing 10mM Tris, pH 8.0, and 0.15M Ammonium Sulfate.
Solubility
To reconstitute the lyophilized Fibroblast Growth Factor 9, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. Further dilutions can be made in other aqueous solutions.
Stability
Lyophilized Fibroblast Growth Factor-9 remains stable at room temperature for up to 3 weeks. However, for extended storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, Mouse Recombinant FGF9 should be stored at 4°C for 2-7 days. For long-term storage, it is advisable to store it below -18°C. To enhance stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% based on the following analyses: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Biological Activity
The ED50, which represents the effective dose for 50% stimulation, is determined to be less than 0.5 ng/ml. This value is calculated based on the dose-dependent proliferation of BAF3 cells expressing FGF receptors, measured through 3H-thymidine uptake. This corresponds to a specific activity of 2 MU/mg.
Synonyms
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Pro-Leu-Gly-Glu-Val.
Product Science Overview
Structure and Properties
Biological Functions
FGF-9 exhibits a growth-stimulating effect on cultured glial cells and is primarily produced by neurons in the nervous system . It is essential for glial cell development and has been shown to be involved in various developmental processes. For instance, mice lacking the FGF-9 gene display a male-to-female sex reversal phenotype, indicating its role in testicular embryogenesis .
Mechanism of Action
Applications
Recombinant mouse FGF-9 is widely used in research for its ability to stimulate cell proliferation. It is particularly useful in studies related to nervous system development, organ development, and bone repair . The protein is supplied in a lyophilized form and can be reconstituted for use in various assays, including cell proliferation assays .
Storage and Handling
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