FGF4 Human
Description
FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa.
The FGF4 is purified by proprietary chromatographic techniques.
Product Specs
Fibroblast growth factor 4 (FGF4) is a protein that plays a role in cell growth, development, and repair. It is involved in a variety of biological processes, including embryonic development, wound healing, and tumor growth. FGF4 is a potent mitogen, meaning that it stimulates cell division. It also promotes cell survival and differentiation. FGF4 is overexpressed in several types of cancer, and it has been implicated in tumor progression and metastasis. FGF4 binds to and activates the fibroblast growth factor receptor (FGFR) family of receptor tyrosine kinases. Activation of FGFRs leads to the activation of downstream signaling pathways that regulate cell proliferation, survival, and differentiation. FGF4 is a potential therapeutic target for the treatment of cancer and other diseases.
Recombinant human FGF4 is a single, non-glycosylated polypeptide chain containing 182 amino acids with a molecular mass of 19.8 kDa. The protein is produced in E. coli and purified using proprietary chromatographic techniques.
The appearance of this product is a sterile, filtered, white, lyophilized (freeze-dried) powder.
This product is formulated with 2X phosphate-buffered saline (PBS) at a pH of 7.4.
To reconstitute the lyophilized FGF4, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can then be further diluted into other aqueous solutions.
Lyophilized FGF4 is stable at room temperature for 3 weeks. However, it is recommended to store the lyophilized product desiccated below -18°C. After reconstitution, FGF4 should be stored at 4°C for 2-7 days or below -18°C for longer-term storage. Avoid repeated freeze-thaw cycles.
The purity of this product is greater than 95.0% as determined by SDS-PAGE analysis.
The biological activity of this product was determined by measuring its ability to stimulate the proliferation of NR6R-3T3 cells. The ED50 was found to be 0.543 ng/ml, corresponding to a specific activity of 1.8 x 10^6 units/mg.
GRGGAAAPTA PNGTLEAELE RRWESLVALS LARLPVAAQP KEAAVQSGAG DYLLGIKRLR RLYCNVGIGF HLQALPDGRI GGAHADTRDS LLELSPVERG VVSIFGVASR FFVAMSSKGK LYGSPFFTDE CTFKEILLPN NYNAYESYKY PGMFIALSKN GKTKKGNRVS PTMKVTHFLP RL.
Product Science Overview
FGF-4 is a heparin-binding growth factor and is expressed during embryonic development and in several tissues during adult life . The human recombinant form of FGF-4 is typically produced in human 293 cells and is a monomeric glycoprotein with an apparent molecular mass of 17 and 27 kDa . It binds to fibroblast growth factor receptors FGFR1c, FGFR2c, FGFR3c, and FGFR4, with varying affinities .
FGF-4 is known for its mitogenic activity, promoting the proliferation of fibroblasts and endothelial cells . It is a potent promoter of angiogenesis, which is the formation of new blood vessels, and is believed to be critical in embryonic limb development . Additionally, FGF-4 plays a significant role in cell differentiation and migration .
While FGF-4 is essential for normal development and tissue regeneration, it can also have pathological roles. Increased levels of FGF-4 have been found in several human tumors, indicating its potential role as an oncogene in tumor growth . Altered levels of FGF-4 during embryonic development can result in abnormal limb formation .
Recombinant human FGF-4 is produced under stringent quality control measures to ensure high purity and biological activity. It is typically endotoxin-free and has a purity of over 95% . The protein is stable when stored at -20°C to -80°C and should be reconstituted in sterile 1x PBS pH 7.4 for use .
