Human BMP receptor-1A, soluble
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| Cat-Nr. | S01-021 |
| Size | 100 µg |
| Price | 299 € |
| Source | Insect cells |
| Label | His-Tag |
| Formulation | lyophilized |
| Purity Confirmation | > 90% by SDS-PAGE |
| Length [aa] | 135 |
| Molecular Weight | 23 kDa |
| Biological Activity | Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-5 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2. |
| Species Reactivity | Human |
| Buffer | PBS |
| Reconstitution | The lyophilized sBMPR-1A is soluble in water and most aqueous buffers and should be reconstituted in PBS or medium to a concentration not lower than 50µg/ml. |
| Stability and Storage | Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sBMPR-1A should be stored in working aliquots at -20°C. |
| Synonyms | ALK3; SKR5; CD292; ACVRLK3; 10q23del; bone morphogenetic protein receptor, type IA |
| Description | The extracellular domain of human BMPR-IA was fused with a carboxy-terminal 6X histidine-tag. The monomeric glycoprotein was expressed in baculovirus infected insect cells. Cellular responses to bone morphogenetic proteins (BMPs) have been shown to be mediated by the formation of hetero-oligomeric complexes of the type I and type II serine/threonine kinase receptors. BMP receptor 1A (BMPR-1A), also known as activin receptor-like kinase (ALK)-3, is a one of seven known type I serine/threonine kinases that are required for the signal transduction of TGF-b family cytokines. In contrast to the TGF-b receptor system in which the type I receptor does not bind TGF-b in the absence of the type II receptor, type I receptors involved in BMP signaling (including BMPR-IA, BMPR-IB/ALK-6, and ActR-I/ALK-2) can independently bind the various BMP family proteins in the absence of type II receptors. Recombinant soluble BMPR-IA binds BMP-2 and -4 with high-affinity in solution and is a potent BMP-2/4 antagonist in vitro. BMPR-IA is ubiquitously expressed during embryogenesis. In adult tissues, BMPR-IA mRNA is also widely distributed; with the highest expression levels found in skeletal muscle. The extracellular domain of BMPR-IA shares little amino acid sequence identity with the other mammalian ALK type I receptor kinases, but the cysteine residues are conserved. Human and mouse BMPR-IA are highly conserved and share 98% sequence identity. |
| Protein Sequence | QNLDSMLHGTGMKSDSDQKKSENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIRHHHHHH |
| Uniprot ID | P36894 |
| Protein RefSeq | NP_004320.2 |
| mRNA RefSeq | NM_004329.2 |
Figures
SDS-PAGE analysis of recombinant human soluble BMPR-1A from insect cells. Sample was loaded in 15% SDS-polyacrylamide gel under reducing condition and visualized with Silver stain.
Inhibition of BMP-2 induced proliferation of C2C12 cells with recombinant human BMPR-1A. C2C12 cells were plated with 1500cells/well in a 96well plate. Cells were stimulated with 0.5μg/ml BMP-2 [Cat# 200-001] and increasing amounts of recombinant human soluble BMPR-1A [Cat# S01-021] were added. The cells were incubated at 37°C, 5% CO2 for 4 days.
BMP-2 BioLISA using recombinant human soluble BMPR-1A [Cat# S01-021] for capturing and recombinant human BMP-2 [Cat# 200-001] as standard. A rabbit anti-human BMP-2 antibody [Cat# 102-PA106] in combination with a goat anti-rabbit Biotin-conjugated antibody was used for detection.
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