FGF 9 Human

Fibroblast Growth Factor-9 Human Recombinant
Cat. No.
BT7842
Source
Escherichia coli.
Synonyms
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
Appearance
Sterile Filtered white lyophilized powder.
Purity
Greater than 95.0% as determined by RP-HPLC and SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY.They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Fibroblast Growth Factor-9 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.4 kDa. The FGF-9 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Human FGF-9, encoded by the FGF9 gene, is a 208-amino acid protein with a potential N-glycosylation site. It is synthesized as a glycosylated protein and efficiently secreted despite lacking a typical signal peptide. FGF-9 exhibits high homology across humans, rats, and mice. Transcripts of FGF-9 are found in brain and kidney tissues. As a member of the fibroblast growth factor (FGF) family, FGF-9 possesses mitogenic and cell survival activities, playing crucial roles in embryonic development, cell growth, morphogenesis, tissue repair, and tumor progression. Initially isolated as a secreted factor stimulating glial cell growth, FGF-9 is primarily produced by neurons in the nervous system and is implicated in glial cell development. Studies have shown that the expression of its mouse homolog depends on Sonic hedgehog (Shh) signaling. FGF-9 knockout mice exhibit a male-to-female sex reversal phenotype, suggesting its role in testicular embryogenesis. In summary, FGF-9 contributes to glial cell growth and differentiation during development, gliosis in brain tissue repair, neuronal cell differentiation and survival, and the stimulation of glial tumor growth.
Description
Recombinant Human Fibroblast Growth Factor-9, produced in E.coli, is a non-glycosylated polypeptide chain comprising 207 amino acids. With a molecular weight of 23.4 kDa, this single-chain protein is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile, lyophilized powder with a white appearance.
Formulation
The protein is provided as a sterile, lyophilized powder. It is lyophilized from a solution containing 1 mg/ml of the protein in 1xPBS.
Solubility
To reconstitute the lyophilized Human Fibroblast Growth Factor-9, it is recommended to dissolve the powder in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Human Fibroblast Growth Factor 9 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store the lyophilized protein desiccated at a temperature below -18°C. After reconstitution, the FGF-9 solution can be stored at 4°C for 2-7 days. For extended storage, it should be kept at -18°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of this protein is determined to be greater than 95.0% using RP-HPLC and SDS-PAGE analysis.
Biological Activity
The biological activity of this product is determined by its ability to stimulate the proliferation of BAF3 cells expressing FGF receptors. The ED50, measured by 3H-thymidine uptake, is less than 0.5 ng/ml. This corresponds 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
APLGEVGNYF GVQDAVPFGN VPVLPVDSPV LLSDHLGQSE AGGLPRGPAV
TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA
VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN
LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY
KDILSQS.

Product Science Overview

Structure and Function

FGF-9 is a glycosylated protein with a molecular weight of approximately 26 kDa . It primarily binds to several FGF receptors, including FGFR1c, FGFR2c, FGFR3b, FGFR3c, and FGFR4 . The binding of FGF-9 to its receptor requires interaction with heparin, which induces receptor dimerization, subsequent transphosphorylation, and downstream activation of signaling pathways such as Erk, Akt, and PLCγ .

Biological Roles
  1. Development: FGF-9 is essential for various developmental processes. During embryogenesis, it plays a key role in gonad development and the determination of sexual phenotype . It is also involved in skeletal development and lung development .

  2. Nervous System: In the nervous system, FGF-9 is secreted by neurons and induces survival signals for glial cells and astrocytes . It exhibits a growth-stimulating effect on cultured glial cells .

  3. Cancer: FGF-9 is expressed in certain cancers, including prostatic and brain cancers . Its role in cancer involves promoting cell proliferation and survival.

Recombinant Human FGF-9

Recombinant human FGF-9 is produced using Escherichia coli (E. coli) expression systems and is supplied in a lyophilized form . It is optimized for use in cell culture, differentiation studies, and functional assays . The recombinant protein is highly pure, with endotoxin levels typically less than 1 EU/μg .

Applications

Recombinant human FGF-9 is used in various research applications, including:

  • Developmental Studies: Investigating tissue differentiation and organ development.
  • Cell Culture: Maintenance of neuronal and glial cell cultures.
  • Functional Assays: Studying cell proliferation and differentiation .
Storage and Handling

For optimal stability, recombinant human FGF-9 should be stored at -20°C in its lyophilized form. Once reconstituted with sterile water, it can be stored at 4°C for short-term use or at -20°C to -80°C for long-term storage .

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