GDF-11/BMP-11 Protein, Human (HEK293)

Bone morphogenetic protein 11 (BMP-11; GDF11), also known as growth/differentiation factor 11, is a polymorphic ligand protein belonging to the TGFβ family. The GDF-11/BMP-11 signal activates the signal through activator receptor types I and II, resulting in the phosphorylation of SMAD2 and SMAD3^[1]. GDF-11/BMP-11 is an important regulator of central nervous system (CNS) formation and fate^[2]. Exogenous peripheral delivery of GDF-11/BMP-11 may enhance neurogenesis and angiogenesis and improve neuropathological outcomes in the elderly brain^[2]. The total length of human GDF-11/BMP-11 protein is 407 amino acids (M1-M407), with a glycosylation domain. GDF-11/BMP-11 Protein, Human (HEK293) has a total length of 109 amino acids (N299-S407), is expressed in HEK293 cells.

Bone Morphogenetic Protein 11 (BMP-11; GDF11), also known as growth/differentiation factor 11, is a ligand protein with pleiotropic, belongs to TGFβ family. BMP-11 signals through activin receptors type II, ACVR2A and ACVR2B, and activin receptors type I, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3^[1].
BMP-11 is highly similar with growth/differentiation factor 8 (GDF8), and exhibits more potent activator of SMAD2/3 and signals more effectively through the type I activin-like receptor kinase receptors ALK4/5/7 than GDF8. Furthermore, signaling by GDF-11/BMP-11 is controlled by extracellular protein antagonists, including FS, FSTL3, GASP1, and GASP2^[1].
GDF-11/BMP-11 plays pivotal roles during development, including anterior/posterior patterning, formation of the kidney, stomach, spleen and endocrine pancreas. In the embryo, BMP-11 also shows strong expression is seen in the palatal epithelia, including the medial edge epithelial and midline epithelial seam of the palatal shelves. Less pronounced expression is also seen throughout the palatal shelf and tongue mesenchyme^[3].
GDF-11/BMP-11 is lately found expressing in the adult central nervous system (CNS)^[3], is an important regulator of CNS formation and fate^[2]. In the aged brain, exogenous, peripherally delivered GDF-11/BMP-11 may enhance neurogenesis and angiogenesis, as well as improve neuropathological outcomes. Exogenously increasing circulating GDF-11/BMP-11 concentrations may be a viable approach for improving deleterious aspects of brain aging and neuropathology^[2].

"GDF-11/BMP-11 (5, 10, 20, and 40 ng/mL; 7 d) maintains the colony and cellular morphology of undifferentiated human embryonic stem cells (hESC), maintains POU5f1, NANOG, TRA-1-60, and SSEA4 expression, and displays increased SMAD2/3 phosphorylation in serum-free medium at 20 ng/mL concentration^[4].
GDF-11/BMP-11 (50-400 ng/mL; 2 d) induces browning of 3T3-L1 adipocytes via coordination of multiple signalling pathways, including mTORC1-COX2 and p38MAPK-PGC-1α as non-canonical pathways, as well as Smad1/5/8 as a canonical pathway^[5].
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Human

HEK293

Tag Free

O95390 (N299-S407)

10220  [NCBI]

NLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS

Approximately 14.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 50% glycerol, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Walker RG, et al. Structural basis for potency differences between GDF8 and GDF11. BMC Biol. 2017 Mar 3;15(1):19.  [Content Brief]

  [2]. Schafer MJ, et al. The influence of GDF11 on brain fate and function. Geroscience. 2019 Feb;41(1):1-11.  [Content Brief]

  [3]. Cox TC, et al. Mutations in GDF11 and the extracellular antagonist, Follistatin, as a likely cause of Mendelian forms of orofacial clefting in humans. Hum Mutat. 2019 Oct;40(10):1813-1825.  [Content Brief]

  [4]. Hannan NR, et al. BMP-11 and myostatin support undifferentiated growth of human embryonic stem cells in feeder-free cultures. Cloning Stem Cells. 2009 Sep;11(3):427-35.  [Content Brief]

  [5]. Pham HG, et al. BMP11 regulates thermogenesis in white and brown adipocytes. Cell Biochem Funct. 2021 Jun;39(4):496-510.  [Content Brief]