Recombinant Human/Mouse/Rat GDF-11/BMP-11 Protein, CF Summary
Additional Information |
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Details of Functionality |
Measured by its ability to induce hemoglobin expression in K562 human chronic myelogenous leukemia cells. Schwall, R.H. et al. (1991) Method Enzymol. 198:340. The ED50 for this effect is 0.8-4.8 ng/mL. |
Source |
E. coli-derived GDF-11/BMP-11 protein Asn299-Ser407, with an N-terminal Met |
Accession # |
|
N-terminal Sequence |
Met-Asn299-Leu-Gly-Leu-Asp-(Cys)-Asp-Glu-His |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
GDF11 |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
12.6 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Publications |
Read Publications using 1958-GD/CF in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile 4 mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human/Mouse/Rat GDF-11/BMP-11 Protein, CF
Background
Growth Differentiation Factor 11 (GDF-11), also known as BMP-11, is a member of the TGF-beta superfamily and is highly related to GDF-8. GDF-11 encodes a 407 amino acid (aa) prepropeptide which contains a signal sequence for secretion and an RXXR proteolytic processing site to yield a 109 aa residue carboxy-terminal mature protein (1). Mature GDF-11 contains the canonical 7-cysteine motif common to other TGF-beta superfamily members; however, like the TGF-beta s, Activins and GDF-8, GDF-11 also contains one extra pair of cysteine residues. At the amino acid sequence level, mature human, mouse, rat and chicken GDF-11 are 99-100% identical. GDF-11 and GDF-8 share 90% amino acid sequence identity within the mature protein. As detected by in situ hybridization, GDF-11 is expressed in diverse regions of the mouse embryo: tailbud, somitic precursors, limbs, mandibular and branchial arches, dorsal neural tube, odontoblasts, nasal epithelium, and particular regions of the brain (1, 2). Targeted deletion of GDF-11, in mice, results in a spectrum of abnormalities including palatal malformation, vertebral defects, elongated trunks with a reduced or absent tail, missing or malformed kidneys, and an increased number of neurons in the olfactory epithelium (2-5). GDF-11 signals through the Activin type II receptors and induces phosphorylation of Smad2 to mediate axial patterning (6). Systemic GDF-11 levels decline with age and administration of higher levels of GDF-11 can reverse age-related cardiac hypertrophy (7). In addition, systemic administration of recombinant GDF-11 protein restores genomic integrity and health of muscle stem cells, neurovasculature and enhances neurogenesis (8, 9). R&D Systems recombinant GDF-11 preparations have been shown to act similarly to GDF-8 in both the Xenopus animal cap and the K562 assays.
- Gamer, L.W. et al. (1999) Dev. Biol. 208: 222.
- Nakashima, M. et al. (1999) Mech. Dev. 80:185.
- Gad, J.M. and P.P.L. Tam (1999) Curr. Biol. 9:R783.
- McPherron, A.C. et al. (1999) Nat. Genet. 22:260.
- Esquela, A.F. and S.J. Lee (2003) Dev. Biol. 257:356.
- Oh, S.P. et al. (2002) Genes & Dev. 16:274.
- Loffredo, F.S. et. al. (2013) Cell. 153.828.
- Katsimpardi, L. et. al. (2014) Science (ahead of print).
- Sinha, M. et. al. (2014) Science (ahead of print).
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