CAS 106096-93-9 Recombinant Human bFGF rbFGF Growth Factors Rice Grain Expressed

CAS 106096-93-9 Human Recombinant Growth Factors BFGF Rice Grain Expressed ​

Description

The State-of-the-art platform called Oryz^HiExp, which using rice endosperm as a bioreactor to specifically and highly express recombinant proteins and growth factors.

The recombinant proteins are storaged and accumulated in the rice protein bodies, which will result in a large number of proteins and maintain the protein bioactivity and correct folding. We use this technology to produce the OsrhbFGF, which is known as real plant origin. And OsrhbFGF have high purity that is more than 95%. Compared with the E.coli derived bFGF, Healthgen Biotech bFGF has a higher bioactivity, which is more than 1X10⁶ Units/mg.

Quick Details

1. CAS No.: 106096-93-9
2. Other Names: Plant-derived bFGF, OsrhbFGF, rbFGF, recombinant bFGF, bFGF, FGF2, FGF-β
3. EINECS No.: 274-272-6
4. Brand Name: Oryzogen
5. Model Number: HYC005M01
6. Physical Appearance: White lyophilized powder
7. Biological Activity: The ED₅₀ is ≤1ng/ml determined by a cell proliferation assay using
8. Restrictions: FOR RESEARCH, LABORATORY AND MANUFACTURE USE ONLY

Advantages

1. Wuhan Healthgen Biotechnology Corp. is a private company founded in 2006. We specialize in molecular pharmaceutical technology research and high-tech innovation-oriented product development, which is developing, manufacturing and marketing a series of recombinant proteins and growth factors by rice endosperm platform. We have 400 square meters of research center, in which 30% of the research personnels have doctoral degree and major in different directions of the research and development. Healthgen Biotech has strong capability in developing a series of biological products.

2. Healthgen Biotech recombinant bFGF is free of animal origin, which effectively avoid any potential risk of animal bacteria, prions, virus and contagious protein disease.

Supplemental Description

FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum, and placenta. This factor contains four cysteine residues, but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. A variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. Binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF basic stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. FGF basic induces neuron differentiation, survival, and regeneration. FGF basic also modulates embryonic development and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may participate in the production of a variety of pathological conditions resulting from excessive cell proliferation and excessive angiogenesis.