|Application ||WB, IHC, FC|
|Calculated MW||115201 Da|
|Positive Control||Western blot: mouse heart tissue lysate, IHC: human hepatocarcinoma and kidney tissues, FACS: HepG2 cells.|
|Application & Usage||WB: 1:1000, IHC: 1:10 – 1:50, FC: 1:10 – 1:50.|
|Other Names||BMPR2; PPH1; Bone morphogenetic protein receptor type-2; Bone morphogenetic protein receptor type II|
|Formulation||In PBS with 0.09% (W/V) sodium azide.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||BMPR2 Antibody (NT) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Highly expressed in heart and liver.|
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Provided below are standard protocols that you may find useful for product applications.
BMPR2 is a type II serine/threonine receptor kinase that binds to an array of secreted bone morphogenetic proteins (BMPs). BMPs belong to the superfamily of TGF-β ligands that modulate gastrulation, neurogenesis, chondrogenesis, interdigital cell death, and bone morphogenesis. In contrast to the TGF-β type II receptor, BMPR2 contains an extended carboxyl-terminal region that interacts with multiple signaling molecules to modulate the responsiveness of target genes to BMPs. BMP signaling requires oligomerization of both type I and type II receptors to elicit a functional response of target genes. BMP binding to type I and II receptors induces Smad1/5/8 phosphorylation which is required for the activation of target genes. In vitro and in vivo evidence suggests that defects in BMPR2 may contribute to pulmonary hypertension, inflammation, and endothelial injury.
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