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March 2013 Archive

Posted by Chris on March 7th, 2013  ⟩  0 comments

In the weeks to come, we want to spend some time discussing some of our more popular and interesting growth factors and growth factor families. We begin with the Fibroblast Growth Factor family!

Fibroblast growth factors (FGFs) form one of the largest families of growth factors. FGFs are found in nearly all multicellular lifeforms, ranging from nematodes to humans. They are crucial in the embryonic development process; responsible for developing the vascular system, CNS system, the mesoderm, limb development, branching morphogenesis and even brain patterning. They are found throughout the body and phenotypic knock-out studies of the FGF family show a large number of developmental arrests and often lethality.

Their function is no less important in post-embryonic growth. They continue to be responsible for vascular repair, the regulation of electrical excitability of cells and in the hormonal regulation of the metabolism. If that were not enough, FGF-signaling disorders have been implicated in a number of pathological conditions and many types of cancer. In the human/murine systems, there are 22 gene members of the FGF family (FGF-15 and FGF-19 are orthologs of each other). They range in mass between 17-34 kDa and share 13-71% amino acid homology.

According to Itoh and Ornitz (2008), the FGF family can be broken into 3 large subfamilies, the intracellular (iFGF) subfamily (FGF-11/12/13/14), and two intercellular subfamilies: the hormone-like (hFGF) FGF-15/21/23, and the canonical subfamilies which include the FGF-1/2/5, FGF-3/4/6, FGF-7/10/22, FGF-8/17/18 and FGF-9/16/20 subfamilies. You can find this evolutionary relationship map on any of our FGF product pages.

The iFGF family (FGF-11/12/13/14) is characterized as the being FGF Receptor (FGFR) independent (intracrene). Though they bear a strong sequence similarity to canonical FGFs, their functional and biochemical properties are mostly unrelated. They are important to the intracellular domains of sodium channels as well as neuronal proteins. And unlike canonical or hFGFs, their coding region is divided by 4 introns (two of which are identical to the other two FGF subfamilies).

The hFGF, or endocrine FGF, family (FGF-15/21/23) has low affinity for heparin-binding sites and has been found to act on target cells far from their site of production. These FGFs play a significant role as regulatory hormones in bile acid metabolism, phosphate and Vitamin D metabolism as well as postnatal energy metabolism. The hFGF family also requires the use of co-receptors, like Klotho or βKlotho in order to activate any FGFRs, indicating that they have evolved a novel mechanism of regulation unlike any of the other FGF genes.

The largest FGF subfamily is the Canonical FGF family. Representing 15 FGF genes, these growth factors activate FGFRs in varying degrees of specificity but with a very high affinity. They are all either excreted or extracellular proteins that induce dimerization and phosphorylation of specific tyrosine residues. All canonical FGFs bind in a paracrine manner to heparin and heparin sulfate and their coding region is divided by 2 introns (which are identical to the introns in the hFGFs). Canonical FGFs have essential roles as proliferation or differentiation factors in the development of a variety of organs and tissue.

Over the next few weeks we will start to drill down into some of the more exciting FGF proteins and their particular stories. Stay tuned and if you have questions or would just like to learn more about these products, please email us at!


Itoh, Nobuyuki, and David M. Ornitz. "Functional evolutionary history of the mouse Fgf gene family." Developmental Dynamics 237.1 (2008): 18-27.

Haugsten, Ellen Margrethe, et al. "Roles of fibroblast growth factor receptors in carcinogenesis." Molecular Cancer Research 8.11 (2010): 1439-1452.

Itoh, Nobuyuki, and David M. Ornitz. "Fibroblast growth factors: from molecular evolution to roles in development, metabolism and disease." Journal of Biochemistry 149.2 (2011): 121-130.

Coutu, Daniel L., and Jacques Galipeau. "Roles of FGF signaling in stem cell self-renewal, senescence and aging." Aging (Albany NY) 3.10 (2011): 920.

Dorey, Karel, and Enrique Amaya. "FGF signalling: diverse roles during early vertebrate embryogenesis." Development 137.22 (2010): 3731-3742.

Category Code: 79101 79108

Posted by Chris on March 14th, 2013  ⟩  0 comments

For this Growth Factor Focus week, we want to take a closer look at the FGF8 subfamily of Fibroblast Growth Factors. This subfamily comprises of FGF-8, FGF-17, and FGF-18. At Gold Bio, we have murine FGF-8 as well as human FGF-18 and rat FGF-18 available for your research.

The FGF8 subfamily of the Fibroblast Growth Factors is principally involved with brain, ear, limb and eye development. The members of this family have distinct and overlapping expression patterns in various prenatal developing tissues such as the mid-hindbrain junction. They are also required for the central nervous system (CNS) morphogenesis, limb development and long-bone ossification. Beenken, et al., (2009) have shown that FGF-8 knockout mice fail to undergo gastrulation, whereas FGF-17 knockout mice appear to have developmental aberrations in several brain structures. FGF-18 knockout mice have delayed bone development and poor expression of their osteogenic markers which may point to similarly poor development of osteoblasts.

As with all of the Canonical FGFs, the FGF8 subfamily activates a number of the FGFRs (FGF Receptors), specifically 3c and FGFR4 (4Δ). And while they will also bind to FGFR2c and 1c, it is to a much lesser extent, and they do not prefer any of the FGFRb isoforms at all (Zhang 2006). You can find a more detailed look at the receptor preference of the FGF8 subfamily or an overview of all of the receptor preferences of all of the FGF subfamilies in the JBC online journal.

FGF-18 has also been shown to enhance BMP (Bone Morphogenetic Protein) function and suppress Noggin expression. Noggin is an extracellular protein that normally inhibits the functions of growth factors such as BMP2 or BMP4. FGF-18 suppression of Noggin may help lead to accelerated bone formation and possibly bone repair, and may also compensate for FGF2 suppression in skeletal development and formation. But FGF-18 is also crucial in for various organs as well, such as the liver, small intestine, kidneys and the pancreas and is highly expressed in the lungs and brain.

FGF-8 has been shown to be crucial in the development of the anterior heart field (AHF) (Ilagan 2006) as well as in nephrogenesis, or the development of the kidneys (Grieshammer 2005). In addition, conditions that cause the loss of function of FGF-8 or impair in its receptor binding have been associated with Kallmann Syndrome (Falardeau 2008), which is a genetic condition characterized by hypogonadism.

Stay tuned for next week’s Growth Factor Highlight and if you have questions or would just like to learn more about these products, please email us at!


Beenken, Andrew, and Moosa Mohammadi. "The FGF family: biology, pathophysiology and therapy." Nature Reviews Drug Discovery 8.3 (2009): 235-253.

Zhang, Xiuqin, et al. "Receptor specificity of the fibroblast growth factor family." Journal of Biological Chemistry 281.23 (2006): 15694-15700.

Haque, T., S. Nakada, and Reggie C. Hamdy. "A review of FGF18: Its expression, signaling pathways and possible functions during embryogenesis and post-natal development." Histology and Histopathology 22 (2007): 97-105.

Ilagan, Roger, et al. "Fgf8 is required for anterior heart field development." Development 133.12 (2006): 2435-2445.

Grieshammer, Uta, et al. "FGF8 is required for cell survival at distinct stages of nephrogenesis and for regulation of gene expression in nascent nephrons." Development 132.17 (2005): 3847-3857.

Falardeau, John, et al. "Decreased FGF8 signaling causes deficiency of gonadotropin-releasing hormone in humans and mice." Journal of Clinical Investigation 118.8 (2008): 2822-2831.

Category Code: 79101

Posted by Patrick on March 18th, 2013  ⟩  0 comments

With the launch of our new growth factor product line, we thought it would be interesting to look back at the history of growth factors. Today we know that growth factors are a powerful tool that researchers can use to study the development of embryonic or induced pluripotent stem cells, and this is all thanks to two researchers that helped deepen our understanding of cell biology.  Those two are Stanley Cohen and Rita Levi-Montalcini, who discovered Nerve Growth Factor (NGF) and Epidermal Growth Factor (EGF), and were awarded the Nobel Prize in Physiology or Medicine in 1986.

The story begins in the 1950’s in the lab of Dr. Viktor Hamburger (and yes, that is his real name) at Washington University, St. Louis.  Dr. Levi-Montalcini had arrived in 1946, and was there working on an unexplained biological phenomenon (and although it is beyond the scope of this blog post, she has an incredible life story that I strongly encourage everyone read about). She had been studying nerve development in chick embryos, and had observed that if she grafted a certain tumor cell line anywhere on a developing embryo, then nerve fibers would grow very rapidly. She then discovered that even if she grafted the tumor nowhere near the area where the nerve fibers were, they would still develop more rapidly than normal embryos. In order to further study this phenomenon, she even went as far as to develop a special tissue culture system where she placed a sensory ganglion near a tumor fragment, and after only one day of growth, she could see nerve fibers extend towards the tumor. So in 1952 she inferred that there must be some kind of biochemical agent being released from these tumor cells that was capable of inducing the growth of nerve fibers from a distance. Unfortunately she was not a biochemist, so in order to find out what this agent was she enlisted the help of a one working in the Zoology department at Wash U., Dr. Stanley Cohen.

Dr. Cohen began by making a crude extract from the tumor cells, and when he applied this extract to the ganglion he saw that it had the same effect as the live cells.  He was then able to determine that the agent in the extract was probably a protein because it was affected by heat, non-dialyzable, and was inactivated by proteases. However he also wanted to make sure it wasn’t a virus that was causing this effect. This caused him to procure some crude phosphodiesterase that had been purified from snake venom, and this was where the big break came in. When the tumor cells were treated with the snake venom phosphodiesterase, the nerve growth in the ganglion was multiple times better than it had been with the tumor extract alone, and even stranger, the ganglion treated with just the phosphodiesterase showed this same growth.  Through more experimentation he discovered that there was another protein in the snake venom extract causing the effect, and once purified, and in 1957 Dr. Levi-Montalcini was able to inject this protein into the yolk sac of developing embryo’s and see the same effect as the tumor cells. They named this new protein Nerve Growth Factor. Continuing their partnership and through even more research, they also discovered Epidermal Growth Factor, which could stimulate the proliferation of epithelial cells.

Although the research didn’t make a huge impact at the time it was published, it is viewed as the beginning of our understanding of growth factors and how proteins can influence cell differentiation. Its importance was also aided by the continued work of Dr. Levi-Montancini and Dr. Cohen, and it is thanks to them that we currently have the understanding that we do.  Their autobiographies and more can be found on Thanks for reading, and if you have any questions about Goldbio’s line of Growth Factors, check our website or contact us at

Levi-Montalcini, R., and Cohen, S. “In vitro and in vivo effects of a nerve growth-stimulating agent isolated from snake venom.” Proc. Natl. Acad. Sci. U. S. A. 42 (1956), 695–699

Cohen, S., and Levi-Montalcini, R. “Purification and properties of a nerve growth-promoting factor isolated from mouse sarcoma 180.” Cancer Res. 17 (1957), 15–20

Cohen S. “Origins of growth factors: NGF and EGF.” J Biol Chem.  283(49) (2008) 33793-33797

Category Code: 79101

Posted by Chris on March 21st, 2013  ⟩  0 comments

For this Growth Factor Focus week, we want to take a closer look at the FGF7 subfamily of Fibroblast Growth Factors (FGFs). At Gold Bio, we have human, mouse and rat FGF10 as well as both human and mouse FGF7 available for research purposes. FGFs form one of the largest families of growth factors. They are found in nearly all multicellular lifeforms, ranging from nematodes to humans. They are crucial in the embryonic development process; responsible for developing the vascular system, CNS system, the mesoderm, limb development, branching morphogenesis and even brain patterning.

The three major members of the FGF7 Subfamily are FGF7, FGF10 and FGF22. Historically, FGF3 has also been grouped into this subfamily based on phylogenetic or functional analysis, but its best association is still being debated in literature. Itoh and Ornitz (2008) further described that FGF3 is actually closer to FGF4 and FGF6 based on gene location and should probably be associated with that family instead. (Click on the thumbnail for a gene location map of the 7 subfamilies characterized by Itoh and Ornitz.)

The main characterization of the FGF7 subfamily is its specificity with the FGF2Rb receptor. Kuro-o (2012) describes the β1 strands of these growth factors as being “extended two residues N-terminally due to additional strand pairing with β4.” This critical extension allows the FGF7 subfamily to engage specifically with the βC’- βE loop of the FGFR2b. Interestingly, that extension also clashes with the loop of FGFR2c, actively discouraging any binding of the FGF7 subfamily to that receptor.

FGF7 and FGF10 are also known as KGF1 and KGR2, or Keratinoncyte Growth Factors. Keratinocytes are the predominant cells in the epidermal (outermost) layer of the skin. As the epidermis is damaged, additional keratinocytes are induced by growth factors and cover over the wound bed, creating a new barrier over the healing tissue. FGF7 levels increase 150 fold in skin after cutaneous injury (Beenken, 2009). But these growth factors are also crucial in embryonic development of the mesenchymal tissue. Disruption of FGF10 signaling has been shown to result in severe defects in limb development and branching organs, like the pancreas, lungs or salivary glands (Zhang, 2006).

A truncated version of FGF7, known as Palifermin (or Kepivance under Biovitrum), is currently an FDA approved treatment for use during cancer therapies. Palifermin is used for the treatment of oral mucositis, a common side effect of high dosage radiation or chemotherapy for bone marrow transplants or leukemia. According to Beenken, et al. (2009), “when administered on 3 consecutive days before high-dose chemotherapy, as well as for 3 days following haematopoietic stem cell transplantation, Palifermin reduced the median duration of mucositis from 9 to 6 days, and reduced the incidence of grade 4 mucositis from 62% to 20%. This corresponds with a significant improvement in the patients’ quality of life, as grade 4 mucositis is of such severity that oral feeding is impossible.”

Stay tuned for next week’s Growth Factor Highlight and if you have questions or would just like to learn more about these products, please email us at!


Itoh, Nobuyuki, and David M. Ornitz. “Functional evolutionary history of the mouse Fgf gene family.” Developmental Dynamics 237.1 (2008): 18-27.

Kuro-o, Makoto, ed. Endocrine FGFs and klothos. Vol. 728. Springer, 2012.

Zhang, Xiuqin, et al. “Receptor specificity of the fibroblast growth factor family.” Journal of Biological Chemistry 281.23 (2006): 15694-15700.

Umemori, Hisashi, et al. "FGF22 and its close relatives are presynaptic organizing molecules in the mammalian brain." Cell 118.2 (2004): 257-270.

Oulion, Silvan, Stephanie Bertrand, and Hector Escriva. "Evolution of the FGF Gene Family." International Journal of Evolutionary Biology 2012 (2012).

Beenken, Andrew, and Moosa Mohammadi. “The FGF family: biology, pathophysiology and therapy.” Nature Reviews Drug Discovery 8.3 (2009): 235-253.

Category Code: 79101 79108

Posted by Chris on March 29th, 2013  ⟩  0 comments

At Gold Bio, we just love it when we can find two products which can be used in conjunction. It’s even better when we have both of those products available for your research! As we continue delve deeper into the potential applications of our new line of Growth Factors, we are constantly amazed at the ingenuity and the creativity of scientists.

There are literally thousands of papers detailing the use of various growth factors to induce genes. Quezada, et al. recently used TGF-β to regulate the Smad7 proteins. IGF-1, EGF and VEGF are all popularly known inducers that have been heavily cited in literature, whether in relation to cancer research, stem cell research, cell apoptosis or hormone studies. The fibroblast family is equally cited across a wide spectrum of research interests and gene/protein study.

But when a scientist wants to see the fruits of their research clearly and quickly, they often turn to some kind of luciferase reporter assay. And why wouldn’t they? Bioluminescent Imaging (BLI) is one of the simplest and robust systems we have for detection of gene injunction or regulation. It’s versatile enough to use both in vitro as well as in vivo in a wide variety of animal models. So it’s a natural progression to want to put these two systems together!

The Gambhir lab first reported using the NF-κB promoter in conjunction with firefly luciferase several years ago (Ray 2002 and Paulmurugan 2002). The great value of using NF-κB is that it known to be inducible by the Tumor Necrosis Factor-alpha (TNF-α) growth factor. Ray set out to provide an Inducible Yeast Two-Hybrid (IYTH) system which would allow for a visible reporter of the interaction of two proteins. They showed that it was possible to see the inducement of the luc-gene, via NF-κB, both in cells as well as in vivo mice with the addition of luciferin and TNF-α even after 24 hours. Cell cultures induced with TNF-α had approximately 4 fold higher BLI than in non-induced cultures. Paulmurugan carried it forward, utilizing the strong interaction of Myod and ID proteins to show the signal amplification, gene delivery and expression in vivo in a split luciferase reporter system. Myod is normally expressed in the skeletal muscle and is a myogenic regulatory protein. The ID protein is a negative regulator of myogenic differentiation and can associate with the Myod protein. TNF-α is a pleiotropic growth factor secreted by macrophages which can induce a variety of cell-specific events and causes tumor necrosis in vivo when injected into tumor bearing mice (Boland 1998).

Gold Bio continues to provide the best and cost efficient reagents for your research. Recently we added several human and mouse TNF-α growth factors. We always provide one of the lowest cost, proven and cited sources of d-Luciferin around. For more information on our new growth factors or any of our other products, you can email us at!

Quezada, Marisol, et al. "Smad7 is a transforming growth factor-beta–inducible mediator of apoptosis in granulosa cells." Fertility and sterility 97.6 (2012): 1452-1459.

Fukuda, Ryo, et al. "Insulin-like growth factor 1 induces hypoxia-inducible factor 1-mediated vascular endothelial growth factor expression, which is dependent on MAP kinase and phosphatidylinositol 3-kinase signaling in colon cancer cells." Journal of Biological Chemistry 277.41 (2002): 38205-38211.

Zheng, Shizhong, and Anping Chen. "Disruption of transforming growth factor-β signaling by curcumin induces gene expression of peroxisome proliferator-activated receptor-γ in rat hepatic stellate cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 292.1 (2007): G113-G123.

Paulmurugan, R., Y. Umezawa, and S. S. Gambhir. "Noninvasive imaging of protein–protein interactions in living subjects by using reporter protein complementation and reconstitution strategies." Proceedings of the National Academy of Sciences 99.24 (2002): 15608-15613.

Ray, P., et al. "Noninvasive quantitative imaging of protein–protein interactions in living subjects." Proceedings of the National Academy of Sciences 99.5 (2002): 3105-3110.

Boland, Marion P., and Luke AJ O’Neill. "Ceramide activates NFκB by inducing the processing of p105." Journal of Biological Chemistry 273.25 (1998): 15494-15500.

Category Code: 79101