At GoldBio, 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 [email protected]!

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.

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