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Mouse Anti-BMPR1A Recombinant Antibody (4B7B2) (CBMAB-A4257-YC)

Provided herein is a Mouse monoclonal antibody against Human Bone Morphogenetic Protein Receptor Type 1A. The antibody can be used for immunoassay techniques, such as ELISA, FC, ICC, IHC-P, WB.
See all BMPR1A antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human
Clone
4B7B2
Antibody Isotype
IgG1
Application
ELISA, FC, ICC, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
0.03% sodium azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 179-378

Target

Full Name
bone morphogenetic protein receptor, type IA
Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, AC
Entrez Gene ID
UniProt ID
Alternative Names
Bone Morphogenetic Protein Receptor Type 1A; Bone Morphogenetic Protein Receptor, Type IA; Serine/Threonine-Protein Kinase Receptor R5; Activin Receptor-Like Kinase 3; BMP Type-1A Receptor; EC 2.7.11.30; ACVRLK3; BMPR-1A; ALK-3;
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. Receptor for BMP2, BMP4, GDF5 and GDF6. Positively regulates chondrocyte differentiation through GDF5 interaction. Mediates induction of adipogenesis by GDF6.
Biological Process
Atrioventricular node cell development Source: BHF-UCL
Atrioventricular valve development Source: BHF-UCL
BMP signaling pathway Source: BHF-UCL
BMP signaling pathway involved in heart development Source: BHF-UCL
Cardiac conduction system development Source: BHF-UCL
Cardiac right ventricle morphogenesis Source: BHF-UCL
Cellular response to BMP stimulus Source: BHF-UCL
Cellular response to growth factor stimulus Source: GO_Central
Chondrocyte differentiation Source: Ensembl
Developmental growth Source: Ensembl
Dorsal/ventral axis specification Source: Ensembl
Dorsal/ventral pattern formation Source: GO_Central
Dorsal aorta morphogenesis Source: BHF-UCL
Ectoderm development Source: Ensembl
Embryonic digit morphogenesis Source: Ensembl
Embryonic organ development Source: BHF-UCL
Endocardial cushion formation Source: BHF-UCL
Endocardial cushion morphogenesis Source: BHF-UCL
Fibrous ring of heart morphogenesis Source: BHF-UCL
Heart formation Source: Ensembl
Hindlimb morphogenesis Source: Ensembl
Immune response Source: BHF-UCL
In utero embryonic development Source: Ensembl
Lateral mesoderm development Source: Ensembl
Lung development Source: Ensembl
Mesendoderm development Source: Ensembl
Mesoderm formation Source: Ensembl
Mitral valve morphogenesis Source: BHF-UCL
Mullerian duct regression Source: Ensembl
Negative regulation of BMP signaling pathway Source: Reactome
Negative regulation of gene expression Source: BHF-UCL
Negative regulation of muscle cell differentiation Source: Ensembl
Negative regulation of neurogenesis Source: Ensembl
Negative regulation of smooth muscle cell migration Source: BHF-UCL
Neural crest cell development Source: Ensembl
Neural plate mediolateral regionalization Source: Ensembl
Odontogenesis of dentin-containing tooth Source: Ensembl
Osteoblast differentiation Source: Ensembl
Outflow tract morphogenesis Source: BHF-UCL
Outflow tract septum morphogenesis Source: BHF-UCL
Paraxial mesoderm structural organization Source: Ensembl
Pharyngeal arch artery morphogenesis Source: BHF-UCL
Pituitary gland development Source: Ensembl
Positive regulation of BMP signaling pathway Source: Reactome
Positive regulation of bone mineralization Source: BHF-UCL
Positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
Positive regulation of cardiac ventricle development Source: BHF-UCL
Positive regulation of epithelial cell proliferation Source: Ensembl
Positive regulation of mesenchymal cell proliferation Source: Ensembl
Positive regulation of osteoblast differentiation Source: BHF-UCL
Positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Positive regulation of pri-miRNA transcription by RNA polymerase II Source: Ensembl
Positive regulation of SMAD protein signal transduction Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of transforming growth factor beta2 production Source: BHF-UCL
Positive regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCL
Protein phosphorylation Source: HGNC-UCL
Regulation of cardiac muscle cell proliferation Source: BHF-UCL
Regulation of cellular senescence Source: Ensembl
Regulation of lateral mesodermal cell fate specification Source: Ensembl
Roof of mouth development Source: Ensembl
Somitogenesis Source: Ensembl
Stem cell population maintenance Source: Ensembl
Transforming growth factor beta receptor signaling pathway Source: ProtInc
Tricuspid valve morphogenesis Source: BHF-UCL
Ventricular compact myocardium morphogenesis Source: BHF-UCL
Ventricular septum morphogenesis Source: BHF-UCL
Ventricular trabecula myocardium morphogenesis Source: BHF-UCL
Cellular Location
Cell membrane; Cell surface
Involvement in disease
Juvenile polyposis syndrome (JPS): Autosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers.
Polyposis syndrome, mixed hereditary 2 (HMPS2): A disease is characterized by atypical juvenile polyps, colonic adenomas, and colorectal carcinomas.
A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome.
Topology
Extracellular: 24-152 aa
Helical: 153-176 aa
Cytoplasmic: 177-532 aa
PTM
Glycosylated.

Tomayko, M. M., Karaaslan, S., Lainez, B., Conter, L. J., Song, E., Venkatesan, S., ... & Shlomchik, M. J. (2021). Roles of Bone Morphogenetic Protein Receptor 1A in Germinal Centers and Long-Lived Humoral Immunity. ImmunoHorizons, 5(5), 284-297.

Choi, W., Lee, H. W., Pak, B., Han, O., Kim, M., & Jin, S. W. (2021). Transcriptomic analysis identifies novel targets for individual bone morphogenetic protein type 1 receptors in endothelial cells. The FASEB Journal, 35(3), e21386.

Wang, S., Li, J., Sun, H., Sha, L., Guo, Y., Gu, G., ... & Geng, Q. (2020). Treatment with soluble bone morphogenetic protein type 1A receptor fusion protein alleviates irradiation-induced bone loss in mice through increased bone formation and reduced bone resorption. American journal of translational research, 12(3), 743.

Alshangiti, A. M., Wyatt, S. L., McCarthy, E., Collins, L. M., Hegarty, S. V., Sullivan, A. M., & O’Keeffe, G. W. (2020). Association of distinct type 1 bone morphogenetic protein receptors with different molecular pathways and survival outcomes in neuroblastoma. Neuronal signaling, 4(1), NS20200006.

Islam, M. J., Parves, M. R., Mahmud, S., Tithi, F. A., & Reza, M. A. (2019). Assessment of structurally and functionally high-risk nsSNPs impacts on human bone morphogenetic protein receptor type IA (BMPR1A) by computational approach. Computational biology and chemistry, 80, 31-45.

Rezaei, Z., Dastjerdi, K., & Kordi-Tamandani, D. M. (2019). Bone morphogenic protein receptor type 1a (BMPR1A) and Caveolin-1 associated with trastuzumab resistance of breast cancer cells. Iranian Journal of Pharmacology and Therapeutics, 17(1), 1-5.

Geng, Q., Heng, K., Li, J., Wang, S., Sun, H., Sha, L., ... & Wang, J. (2019). A soluble bone morphogenetic protein type 1A receptor fusion protein treatment prevents glucocorticoid-Induced bone loss in mice. American journal of translational research, 11(7), 4232.

Liu, Y., Zhang, R. X., Yuan, W., Chen, H. Q., Tian, D. D., Li, H., ... & Wang, Y. (2018). Knockdown of bone morphogenetic proteins type 1a receptor (BMPR1a) in breast cancer cells protects bone from breast cancer-induced osteolysis by suppressing RANKL expression. Cellular Physiology and Biochemistry, 45(5), 1759-1771.

Ko, F. C., Van Vliet, M., Ellman, R., Grasso, D., Brooks, D. J., Spatz, J. M., ... & Bouxsein, M. L. (2017). Treatment with a soluble bone morphogenetic protein type 1A receptor (BMPR1A) fusion protein increases bone mass and bone formation in mice subjected to hindlimb unloading. JBMR plus, 1(2), 66-72.

Lee, H. W., Chong, D. C., Ola, R., Dunworth, W. P., Meadows, S., Ka, J., ... & Jin, S. W. (2017). Alk2/ACVR1 and Alk3/BMPR1A provide essential function for bone morphogenetic protein–induced retinal angiogenesis. Arteriosclerosis, thrombosis, and vascular biology, 37(4), 657-663.

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For research use only. Not intended for any clinical use.

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