FGF8 Human, HEK
Sterile Filtered colorless solution.
Greater than 90% as obsereved by SDS-PAGE.
Description
FGF-8 Human Recombinant is a single, glycosylated, polypeptide chain (23-215 a.a) containing a total of 204 amino acids and having a molecular mass of 23.7 kDa.
FGF-8 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Product Specs
Recombinant Human FGF-8 is a single, glycosylated polypeptide chain. It consists of 204 amino acids (23-215 a.a) and has a molecular weight of 23.7 kDa. The protein includes a 6 a.a histidine tag fused at the C-terminus. Purification is achieved using proprietary chromatographic techniques.
Sterile Filtered colorless solution.
The FGF-8 solution is provided at a concentration of 0.25 mg/ml. It is formulated in a buffer containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (up to 2-4 weeks), the FGF-8 vial can be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein such as HSA or BSA (0.1%). Repeated freezing and thawing should be avoided.
The purity of the protein is determined to be greater than 90% based on SDS-PAGE analysis.
The biological activity of the protein, represented by ED50, is determined to be less than or equal to 5 µg/ml. This value is obtained from a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10 µg/ml of heparin.
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
Product Science Overview
FGF-8 exists in multiple isoforms, including FGF-8a, FGF-8b, FGF-8e, and FGF-8f, which are produced through alternative splicing . These isoforms have distinct biological activities and expression patterns. For instance, FGF-8b is known for its role in embryogenesis and the activation of Homeobox genes, which are critical for the regulation of patterns of anatomical development .
FGF-8 is a heparin-binding growth factor that promotes cellular proliferation and differentiation . It is essential for the proper development of various tissues and organs. In adults, FGF-8 expression was initially thought to be restricted to the testes and ovaries, but it has been detected in several other organ systems . Overexpression of FGF-8 has been linked to increased tumor growth and angiogenesis, highlighting its potential role in cancer biology .
Human recombinant FGF-8 is produced using HEK 293 cells, which provide authentic glycosylation patterns that are absent when the protein is expressed in bacterial systems like E. coli . Glycosylation is crucial for the stability and activity of the protein in cell culture and other applications. The recombinant protein is typically purified to high levels of purity and tested for biological activity, such as its ability to stimulate cell proliferation .
Recombinant FGF-8 is widely used in research to study its role in development and disease. It is also utilized in cell culture systems to promote the growth and differentiation of various cell types. The protein’s ability to support androgen and anchorage-independent growth of mammary tumor cells makes it a valuable tool in cancer research .
