25
#O95390
10220
Background
Bone morphogenetic proteins (BMPs), also known as growth differentiation factors (GDFs), were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs are synthesized as precursor proteins that are processed by cleavage to produce mature proteins. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad to the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).
Growth differentiation factor 11 (GDF11), also known as BMP-11, belongs to the BMP family of transforming growth factor beta (TGF-β) superfamily and is very closely related to GDF8 (5). GDF11 plays a critical role in neurogenesis and mesodermal formation in early stages of development and is a key negative regulator of skeletal muscle mass (5-7). With age, GDF11 levels decline. Administration of high levels of GDF11 can result in age-related cardiac hypertrophy to be reversed (8). Additionally, administration of high levels of GDF11 is shown to have effects demonstrating the ability to restore regenerative functions, including muscle aging, reversal of age-related skeletal muscle and stem cell dysfunction, and enhanced neurogenesis (9,10).
- Wang, E.A. et al. (1988) Proc Natl Acad Sci U S A 85, 9484-8.
- Wozney, J.M. et al. (1988) Science 242, 1528-34.
- Kawabata, M. et al. (1998) Cytokine Growth Factor Rev 9, 49-61.
- Nohe, A. et al. (2004) Cell Signal 16, 291-9.
- Gamer, L.W. et al. (1999) Dev Biol 208, 222-32.
- Souza, T.A. et al. (2008) Mol Endocrinol 22, 2689-702.
- Sako, D. et al. (2010) J Biol Chem 285, 21037-48.
- Loffredo, F.S. et al. (2013) Cell 153, 828-39.
- Katsimpardi, L. et al. (2014) Science 344, 630-4.
- Sinha, M. et al. (2014) Science 344, 649-52.
Endotoxin
Endotoxin levels are less than or equal to 1 EU / 1 μg h/m/rGDF11.
Purity
A greater than or equal to 95% purity was determined by SDS-PAGE.
Source / Purification
Recombinant human/mouse/rat GDF11 was expressed in E. coli and is supplied in a lyophilized form.
Bioactivity
The bioactivity of recombinant h/m/rGDF11 was determined by measuring the alkaline phosphatase activity in ATDC-5 cells. The ED50 of each lot is less than or equal to 100 ng/mL.
Background
Bone morphogenetic proteins (BMPs), also known as growth differentiation factors (GDFs), were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs are synthesized as precursor proteins that are processed by cleavage to produce mature proteins. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad to the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).
Growth differentiation factor 11 (GDF11), also known as BMP-11, belongs to the BMP family of transforming growth factor beta (TGF-β) superfamily and is very closely related to GDF8 (5). GDF11 plays a critical role in neurogenesis and mesodermal formation in early stages of development and is a key negative regulator of skeletal muscle mass (5-7). With age, GDF11 levels decline. Administration of high levels of GDF11 can result in age-related cardiac hypertrophy to be reversed (8). Additionally, administration of high levels of GDF11 is shown to have effects demonstrating the ability to restore regenerative functions, including muscle aging, reversal of age-related skeletal muscle and stem cell dysfunction, and enhanced neurogenesis (9,10).
Background References
Cross-Reactivity Key
H: human M: mouse R: rat Hm: hamster Mk: monkey Vir: virus Mi: mink C: chicken Dm: D. melanogaster X: Xenopus Z: zebrafish B: bovine Dg: dog Pg: pig Sc: S. cerevisiae Ce: C. elegans Hr: horse GP: Guinea Pig Rab: rabbit All: all species expected
Trademarks and Patents
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