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 ED50 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 |
MouseIgG2A (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 °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 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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