Anti-Human BMPR-II (Clone 73805)

NS0-Derived Recombinant Human BMPR-II Extracellular Domain (Accession # Q13873)

This monoclonal antibody has been 0.2 µm filtered and lyophilized from modified Dulbecco's phosphate buffered saline (1X PBS) pH 7.2 - 7.3 containing 5.0% w/v trehalose with no calcium, magnesium or preservatives present.

The lyophilized antibody can be stored desiccated at -20°C to -70°C for up to twelve months. The reconstituted antibody can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted antibody, aseptically aliquot into working volumes and store at -20°C to -70°C in a manual defrost freezer. Avoid repeated freeze thaw cycles. No detectable loss of activity was observed after six months.

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Mouse Anti-Human Bone Morphogenic Protein Receptor II (BMPR-II) (Clone 73805) recognizes an epitope on Human BMPR-II. This monoclonal antibody was purified using multi-step affinity chromatography methods such as Protein A or G depending on the species and isotype.

Bone morphogenetic protein receptor type II or BMPR2 is a serine/threonine receptor kinase. It binds Bone morphogenetic proteins, members of the TGF beta superfamily of ligands. BMPs are involved in host of cellular functions including osteogenesis, cell growth and cell differentiation. Signaling in the BMP pathway begins with the binding of a BMP to the the type II receptor. This causes the recruitment of a BMP type I receptor, which it phosphorylates. The Type I receptor phosphorylates an R-SMAD a transcriptional regulator. Unlike the TGFβ type II receptor, which has a high affinity for TGF-β1, BMPR2 does not have a high affinity for BMP-2, BMP-7 and BMP-4, unless it is co-expressed with a type I BMP receptor. In TGF beta signaling all of the receptors exist in homodimers before ligand binding. In the case of BMP receptors only a small fraction of the receptors exist in homomeric forms before ligand binding. Once a ligand has bound to a receptor, the amount of homomeric receptor oligomers increase, suggesting that the equilibrium shifts towards the homodimeric form. The low affinity for ligands suggests that BMPR2 may differ in the from other type II TGF beta receptors in that the ligand may bind the type I receptor first.

Human and mouse BMPR-II are highly conserved sharing 97% sequence identity.