Recombinant Mouse BMPR-IA/ALK-3 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its ability to inhibit rhBMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Nakamura, K. et al. (1999) Exp. Cell Res. 250:351. The ED 50 for this effect is 0.03-0.12 μg/mL in the presence of 30 ng/mL of recombinant human BMP-4. |
Source |
Mouse myeloma cell line, NS0-derived mouse BMPR-IA/ALK-3 protein Mouse BMPR-1A/ALK-3 (Met1 - Arg152) Accession # NP_033888 | IEGRDP | MouseIgG 2A (Glu98 - Lys330) | N-terminus | | C-terminus | |
Accession # |
|
N-terminal Sequence |
No results obtained: Gln24 predicted, N-sequencing might be blocked |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Bmpr1a |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
41.3 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 |
57-60 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 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse BMPR-IA/ALK-3 Fc Chimera Protein, CF
Background
Bone Morphogenetic Protein Receptor IA (BMPR-IA), also known as ALK-3, BRK-1, and CD292, is a glycosylated 60 - 65 kDa type I receptor in the TGF-beta serine/threonine kinase receptor family (1 - 3). Binding of TGF-beta superfamily ligands induces formation of a heterotetrameric complex that contains two chains each of a type I and a type II receptor in multiple combinations. The type II receptors phosphorylate the type I receptors which then phosphorylate and activate Smad signal transduction proteins (1, 2). Mature mouse BMPR-IA consisits of a 129 amino acid (aa) extracellular domain (ECD), a 24 aa transmembrane segment, and a 356 aa cytoplasmic region that contains the tyrosine kinase domain (4, 5). Within the ECD, mouse BMPR-IA shares 98% aa sequence identity with human and rat BMPR-IA. BMPR-IA is involved in the development and function of a wide range of tissues. During early embryogenesis it is required for migration of the anterior visceral endoderm (AVE) and proper development of the anterior-posterior axis (6). Tissue-specific conditional knockout experiments have demonstrated the importance of BMPR-IA in the development and morphogenesis of the heart, lung, palate, teeth, and mandible (7 - 9). In the adult, BMPR-IA plays a role in glucose-stimulated insulin secretion by pancreatic beta cells, osteoclast activity and bone remodeling, reactive astrocyte-mediated scar formation following spinal cord injury, and ovulation and fertility (10 - 13).
- Wu, M.Y. and C.S. Hill (2009) Dev. Cell 16:329.
- Nickel, J. et al. (2009) Cytokine Growth Factor Rev. 20:367.
- de Caestecker, M. (2004) Cytokine Growth Factor Rev. 15:1.
- Dewulf, N. et al. (1995) Endocrinology 136:2652.
- Koenig, B.B. et al. (1994) Mol. Cell. Biol. 14:5961.
- Miura, S. et al. (2010) Dev. Biol. 341:246.
- Gaussin, V. et al. (2002) Proc. Natl. Acad. Sci. 99:2878.
- Sun, J. et al. (2008) Am. J. Pathol. 172:571.
- Li, L. et al. (2011) Dev. Biol. 349:451.
- Goulley, J. et al. (2007) Cell Metab. 5:207.
- Kamiya, N. et al. (2008) J. Bone Miner. Res. 23:2007.
- Sahni, V. et al. (2010) J. Neurosci. 30:1839.
- Edson, M.A. et al. (2010) Mol. Endocrinol. 24:1251.
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