BMPR1A Antibodies

Structure of BMPR1A

The BMPR1A gene encodes receptor IA for bone morphogenetic protein, with a molecular weight of approximately 55 kDa. There are sequence differences among different species, but the structure is highly conserved. The intracellular region of this receptor has serine/threonine kinase activity and transmits signals by phosphorylating SMAD proteins. The receptor is composed of a signal peptide, an extracellular ligand-binding domain, a transmembrane region, and an intracellular kinase domain. The extracellular region contains 10 cysteine residues that form a conserved disulfide bond structure, maintaining ligand recognition specificity. The intracellular kinase domain contains a characteristic glycine-rich loop and a conserved catalytic core sequence. The mutation of the arginine residue at position 229 leads to juvenile polyposis, and the phosphorylation of threonine at position 387 is a key switch for signal activation. After binding to the ligand, this receptor forms an heterotrimer and regulates downstream signal cascades through the GS domain.

Fig. 1 Evolution, Structure, and Horn-Specific Sites of BMPR1A.¹

Key structural properties of BMPR1A:

• The extracellular region contains 10 conserved cysteines forming disulfide bonds
• The transmembrane region is a single transmembrane structure
• The intracellular region has a serine/threonine kinase domain
• The GS domain contains the characteristic sequence SGSGS, which regulates the phosphorylation of downstream SMAD proteins
• The kinase activity depends on the ATP binding site, and the 277th lysine is crucial

Functions of BMPR1A

The BMPR1A gene encodes the bone morphogenetic protein receptor IA, which plays multiple roles in cellular signal transduction:

This receptor forms an heterotrimeric complex by recognizing BMP ligands. The signal intensity depends on the phosphorylation status of the intracellular GS domain. Unlike activin receptors, BMPR1A mainly phosphorylates SMAD1/5/8 proteins.

Applications of BMPR1A and BMPR1A Antibody in Literature

1. Zhang, Guoqing, et al. "Expression, polymorphism, and potential functional sites of the BMPR1A gene in the sheep horn." Genes 15.3 (2024): 376. https://doi.org/10.3390/genes15030376

This study reveals that the BMPR1A gene is closely related to the horn type of sheep: its expression is significantly higher in normal horned individuals than in short-horned sheep. Moreover, 43 SNPs and 10 ASE loci were found to potentially affect the size and presence of horns, providing molecular markers for horn type breeding.

2. Papadopulos, M. E., J. P. Plazzer, and F. A. Macrae. "Genotype–phenotype correlation of BMPR1a disease causing variants in juvenile polyposis syndrome." Hereditary Cancer in Clinical Practice 21.1 (2023): 12. https://doi.org/10.1186/s13053-023-00255-3

The study found that the pathogenic mutations of BMPR1a mainly cause colorectal polyps and malignant tumors, while gastric lesions are rare. It is recommended that mutation carriers only need to monitor colorectal conditions and do not require routine gastric screening, providing new basis for clinical management.

3. Zhang, Dali, et al. "Targeting local lymphatics to ameliorate heterotopic ossification via FGFR3-BMPR1a pathway." Nature communications 12.1 (2021): 4391. https://doi.org/10.1038/s41467-021-24643-2

The study found that FGFR3 regulates the formation of lymphatic endothelial cells through the BMPR1a signal, and affects post-traumatic ectopic ossification. Col2+ cells can differentiate into lymphatic endothelial cells. Activating FGFR3 to promote lymphatic vessel formation can inhibit ectopic bone formation, providing a new target for treatment.

4. Hochgerner, Mathias, et al. "BMPR1a is required for the optimal TGFβ1-dependent CD207+ langerhans cell differentiation and limits skin inflammation through CD11c+ cells." Journal of Investigative Dermatology 142.9 (2022): 2446-2454. https://doi.org/10.1016/j.jid.2022.02.014

The study found that TGFβ1 induces the differentiation of Langerhans cells through the BMPR1a signal and upregulates the expression of CD207. The absence of BMPR1a affects the development of LCs, but in psoriasis, it can inhibit the activation and migration of LCs, alleviate skin inflammation, and reveal its dual role in immune homeostasis.

5. Jiang, Bo, et al. "Lysosomal protein transmembrane 5 promotes lung-specific metastasis by regulating BMPR1A lysosomal degradation." Nature communications 13.1 (2022): 4141. https://doi.org/10.1038/s41467-022-31783-6

The study found that LAPTM5 recruits WWP2 to degrade BMPR1A, blocking the pulmonary BMP signal and promoting the stem cell characteristics of renal cancer and pulmonary-specific metastasis. LAPTM5 can serve as a predictor of lung metastasis and a therapeutic target.

Creative Biolabs: BMPR1A Antibodies for Research

Creative Biolabs specializes in the production of high-quality BMPR1A antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom BMPR1A Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our BMPR1A antibodies, custom preparations, or technical support, contact us at email.