Recombinant Mouse BAMBI/NMA Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its ability to induce cell death using Mv1Lu mink lung epithelial cells. The ED50 for this effect is 1-6 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse BAMBI/NMA protein
Mouse BAMBI/NMA (Glu27-Ala152) Accession # Q9D0L6 |
IEGRMDP |
Mouse IgG2A (Glu98-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Glu27 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Bambi |
Purity |
>95%, by SDS-PAGE with silver staining |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
41 kDa. 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 |
48-53 kDa, reducing conditions |
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 PBS. |
Purity |
>95%, by SDS-PAGE with silver staining |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse BAMBI/NMA Fc Chimera Protein, CF
Background
BMP and Activin Membrane-Bound Inhibitor (BAMBI), also called Non-Metastatic Gene A (NMA), is a type I transmembrane protein that shares sequence homology with the TGF-beta type I receptor family and functions as a decoy receptor (1). Mouse BAMBI is synthesized as a 260 amino acid (aa) precursor and has a predicted molecular weight of approximately 29 kDa (1). Its extracellular domain contains only one potential N-glycosylation site, and shares 91% and 98% aa sequence identity with the human and rat orthologs, respectively. BAMBI differs from other members of the TGF-beta RI family in that it has a short cytoplasmic region that lacks the intracellular serine/threonine kinase domain (1, 2). It competes with type I receptors to form heterodimers with type II receptors, thus interfering with BMP, Activin, and TGF-beta signaling (2). In fact, BAMBI is believed to be one component of a negative feedback loop for BMP signaling that serves to increase the dynamic signaling range for BMPs (3, 4). During development, BAMBI is prominently expressed in gastrulation, neurulation, and during the development of teeth and bones, and is often co-expressed with other BMP family members (1-5). BAMBI is also ubiquitously expressed in the adult, with the highest levels being observed in heart, lung, spleen, kidney, bladder, and testes (6). BAMBI expression is induced by TGF-beta and Wnt signaling (7, 8). It cooperates with inhibitory Smad6 and Smad7 to inhibit TGF-beta signaling (9). In contrast, BAMBI promotes Wnt signaling via its interactions with Frizzled receptors (10). BAMBI has been shown to modulate various processes including adipogenesis, thrombus formation and stability, cell proliferation, and opioid signaling in neuropathic pain (10-13). Additionally, aberrant BAMBI expression is believed to be a factor in the development of cancer, inflammation, and fibrotic processes (7, 14-18).
- Knight, C. et al. (2001) J. Dent. Res. 80:1895.
- Onichtchouk, D. et al. (1999) Nature 401:480.
- Paulsen, M. et al. (2011) Proc. Natl. Acad. Sci. USA 108:10202.
- Montero, J.A. et al. (2008) Dev. Biol. 321:343.
- Grotewold, L. et al. (2001) Mech. Dev. 100:327.
- Lakoski, K. et al. (2003) Endocrinology 144:4180.
- Sekiya, T. et al. (2004) J. Biol. Chem. 279:6840.
- Sekiya, T. et al. (2004) Biochem. Biophys. Res. Commun. 320:680.
- Yan, X. et al. (2009) J. Biol. Chem. 284:30097.
- Lin, Z. et al. (2008) J. Biol. Chem. 283:33053.
- Luo, X. et al. (2012) Diabetes 61:124.
- Salles-Crawley, I.I. et al. (2014) Blood 123:2873.
- Lantero, A. et al. (2014) J. Neurosci. 34:5385.
- Seki, E. et al. (2007) Nat. Med. 13:1324.
- Khin, S.S. et al. (2009) Int. J. Cancer 125:328.
- Fritzmann, J. et al. (2009) Gastroenterology 137:165.
- Drömann, D. et al. (2010) Respir. Res. 11:67.
- Li, Y.S. et al. (2013) PLoS One 8:e76289.
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