Cosmetic Products EGF Epidermal Growth Factor Recombinant Human Fibroblast Growth Factor-basic rh-bFGF

FGF2, also known as basic fibroblast growth factor (bFGF) and FGF-β, is a growth

factor and signaling protein encoded by the FGF2 gene. It is synthesized

primarily as a 155 amino acid polypeptide, resulting in protein. However,

there are four alternate start codons which provide N-terminal extensions of 41, 46,

55, or 133 amino acids, resulting in proteins of 22 kDa (196 aa total), 22.5 kDa (201

aa total), 24 kDa (210 aa total) and 34 kDa (288 aa total), respectively. Generally,

the 155 aa/18 kDa low molecular weight (LMW) form is considered cytoplasmic and

can be secreted from the cell, whereas the high molecular weight (HMW) forms are

directed to the cell's nucleus.

Fibroblast growth factor protein was first purified in 1975, but soon afterwards

others using different conditions isolated basic FGF, Heparin-binding growth factor-

2, and Endothelial cell growth factor-2. Gene sequencing revealed that this group

was in fact the same FGF2 protein and that it was a member of a family of FGF

proteins. FGF2 binds to and exerts effects via specific fibroblast growth factor

receptor (FGFR) proteins which themselves constitute a family of closely related

molecules.

Function
Like other FGF family members, basic fibroblast growth factor possess broad

mitogenic and cell survival activities, and is involved in a variety of biological

processes, including embryonic development, cell growth, morphogenesis, tissue

repair, tumor growth and invasion.

In normal tissue, bFGF is present in basement membranes and in the subendothelial

extracellular matrix of blood vessels. It stays membrane-bound as long as there is no

signal peptide.

It has been hypothesized that, during both wound healing of normal tissues and

tumor development, the action of heparan sulfate-degrading enzymes activates

bFGF, thus mediating the formation of new blood vessels, a process known as

angiogenesis.

In addition, it is synthesized and secreted by human adipocytes and the

concentration of FGF2 correlates with the BMI in blood samples. It was also shown

to act on preosteoblasts – in the form of an increased proliferation – after binding to

fibroblast growth factor receptor 1 and activating phosphoinositide 3-kinase.

FGF2 has been shown in preliminary animal studies to protect the heart from injury

associated with a heart attack, reducing tissue death and promoting improved

function after reperfusion.

Recent evidence has shown that low levels of FGF2 play a key role in the incidence

of excessive anxiety.

Additionally, FGF2 is a critical component of human embryonic stem cell culture

medium; the growth factor is necessary for the cells to remain in an undifferentiated

state, although the mechanisms by which it does this are poorly defined. It has been

demonstrated to induce gremlin expression which in turn is known to inhibit the

induction of differentiation by bone morphogenetic proteins. It is necessary in

mouse-feeder cell dependent culture systems, as well as in feeder and serum-free

culture systems. FGF2, in conjunction with BMP4, promote differentiation of

stem cells to mesodermal lineages. After differentiation, BMP4 and FGF2 treated

cells generally produce higher amounts of osteogenic and chondrogenic

differentiation than untreated stem cells.However, a low concentration of bFGF

(10 ng/mL) may exert an inhibitory effect on osteoblast differentiation.