Recombinant Human 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 15 ng/mL of Recombinant Human BMP‑4 (Catalog # 314-BP).
Source
Mouse myeloma cell line, NS0-derived human BMPR-IA/ALK-3 protein
Gln24 predicted: No results obtained, sequencing might be blocked
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
BMPR1A
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
Bioactivity
Theoretical MW
40.8 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
59 kDa, reducing conditions
Publications
Read Publication using 2406-BR in the following applications:
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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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 Human BMPR-IA/ALK-3 Fc Chimera Protein, CF
ACVRLK310q23del
ALK-3
ALK3EC 2.7.11.30
BMP type-1A receptor
BMPR1A
BMPR-1A
BMPRIA
BMPR-IA
bone morphogenetic protein receptor type-1A
bone morphogenetic protein receptor, type IA
CD292 antigen
CD292
EC 2.7.11
Serine/threonine-protein kinase receptor R5
SKR5
type II-like kinase 3
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 human 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). Within the ECD, human BMPR-IA shares 98% and 97% aa sequence identity with mouse and rat BMPR‑IA, respectively. 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 (5). 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 (6‑8). 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 (9‑12).
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.
ten Dijke, P. et al. (1993) Oncogene 8:2879.
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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