Recombinant Human BMP-6 Protein Summary
Details of Functionality |
Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Nakamura, K. et al. (1999) Exp. Cell Res. 250:351. The ED50 for this effect is 0.02‑0.15 µg/mL. |
Source |
Mouse myeloma cell line, NS0-derived human BMP-6 protein Gln382-His513 |
Accession # |
|
N-terminal Sequence |
Gln382 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
BMP6 |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
15 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. |
SDS-PAGE |
18 kDa, reducing conditions |
Publications |
Read Publications using 507-BP 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 with BSA as a carrier protein. |
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 containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human BMP-6 Protein
Background
Bone Morphogenetic Protein 6 (BMP-6), also known as Vgr-1, is a member of the BMP subfamily of TGF-beta superfamily proteins. BMPs are involved in a wide range of processes including embryogenesis, tissue morphogenesis, cell differentiation and migration, and tumorigenesis (1). Human BMP-6 is synthesized as a 513 amino acid (aa) precursor protein that is cleaved at the dibasic cleavage site (RxxR) to release the 18 kDa C-terminal mature protein. Biologically active BMP-6 consists of a disulfide-linked homodimer of the mature protein, although it can also form heterodimers with mature BMP-2 (2, 3). Mature human BMP-6 shares 96% and 98% aa sequence identity with mouse and rat BMP-6, respectively. Cellular responses to BMP-6 are mediated by hetero-oligomeric complexes of type I (Activin RIA/ALK-2 and BMPR-IA/ALK-3) and type II (Activin RIIA and BMPR-II) serine/threonine kinase receptors (4, 5). BMP-6 induces the expression of Noggin and is subsequently antagonized by Noggin (6). BMP-6 induces a wide range of cellular responses. It promotes osteoblast differentiation from mesenchymal stem cells (7), chondrocyte maturation (8), Ang II-induced aldosterone production in the adrenal cortex (4), hormone production and responsiveness in ovarian granulosa cells (9), iNOS and TNF-alpha production in macrophages (5), the cell death of B cells (10), and neurite outgrowth (11). BMP-6 expression is induced in astrocytes surrounding sites of brain injury where it functions as a neuroprotectant (11, 12). It enhances tumor progression by promoting local angiogenesis and differentiation of immune tolerizing M2 macrophages (13-15). Through interactions with the BMP coreceptor RGM-C/Hemojuvelin, BMP-6 plays an important role in iron homeostasis by promoting Hepcidin expression and preventing serum iron overload (16). Heterodimers of BMP-2 and BMP-6 show increased potency at inducing osteoblastic calcium deposition, chondrogenesis, and
in vivo bone formation compared to either BMP-2 or BMP-6 homodimers (3).
- Bragdon, B. et al. (2010) Cell Signal. 23:609.
- Celeste, A.J. et al. (1990) Proc. Natl. Acad. Sci. USA 87:9843.
- Israel, D.I. et al. (1996) Growth Factors 13:291.
- Inagaki, K. et al. (2006) Endocrinology 147:2681.
- Hong, J.H. et al. (2008) Immunology 128:e442.
- Haudenschild, D.R. et al. (2004) Cancer Res. 64:8276.
- Lavery, K. et al. (2008) J. Biol. Chem. 283:20948.
- Grimsrud, C.D. et al. (1999) J. Bone Miner. Res. 14:475.
- Shi, J. et al. (2009) Fertil. Steril. 92:1794.
- Kersten, C. et al. (2005) BMC Immunol. 6:9.
- Yabe, T. et al. (2002) J. Neurosci. Res. 68:161.
- Zhang, Z. et al. (2006) Neuroscience 138:47.
- Dai, J. et al. (2005) Cancer Res. 65:8274.
- Kwon, S.J. et al. (2014) Prostate 74:121.
- Lee, J.-H. et al. (2013) Cancer Res. 73:3604.
- Andriopoulos, B. Jr. et al. (2009) Nat. Genet. 41:482.
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