Recombinant Human/Mouse BMPR-II Fc Chimera Protein, CF

• Reactivity: Hu, Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human/Mouse BMPR-II Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA.

  When Recombinant Mouse GDF-9 (Catalog # 739-G9) is immobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Human/Mouse BMPR‑II Fc Chimera that produces 50% of the optimal binding response is found to be approximately 0.1 ‑ 0.5 μg/mL.

• Source: Mouse myeloma cell line, NS0-derived BMPR-II protein
  

  Human BMPR-II (Ala26 - Ile151, with an N-terminal Met) Accession # Q13873	IEGRMD	Human IgG1 (Pro100 - Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: Q13873
• N-terminal Sequence: Met & Ser27
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: BMPR2
• Purity: >97%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW:

  41.5 kDa (monomer)

  .
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 65-75 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >97%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human/Mouse BMPR-II Fc Chimera Protein, CF

• BMP type II receptor
• BMP type-2 receptor
• BMPR2
• BMPR-2
• BMPR3
• BMPRII
• BMPR-II
• BMPR-IIprimary pulmonary hypertension 1
• Bone morphogenetic protein receptor type II
• bone morphogenetic protein receptor type-2
• bone morphogenetic protein receptor, type II (serine/threonine kinase)
• BRK-3
• EC 2.7.11
• EC 2.7.11.30
• FLJ41585
• FLJ76945
• PPH1BMR2
• T-ALK
• type II activin receptor-like kinase
• type II receptor for bone morphogenetic protein-4

Background

Like other members of the TGF-beta superfamily, cellular responses to bone morphogenetic proteins (BMPs) have been shown to be mediated by the binding to heteromeric complex of type I and type II serine-threonine kinase receptors. Both receptor types are required for the signl transduction. BMP receptor II (BMPR-II) is one of the five mammalian type II receptors (including TGF-beta R-II, ActR-II, ActR-IIB, BMPR-II and MISR-II) for the TGF-beta superfamily ligands. The type II receptors for TGF-beta and activin bind ligands with high affinity by itself. In contrast, BMPR-II binds BMP-2, BMP-4 and BMP-7 weakly in the absence of type I receptor, and the binding can be facilitated by the presence of the type I receptor. BMPR-II mRNA is widely expressed in fetal and adult tissues. Human and mouse BMPR-II are highly conserved sharing 97% sequence identity.

1. Rosenzweig, B.L. et al. (1995) Proc. Natl. Acad. Sci. USA 92:7632.
2. Beppu, H. et al. (1997) Biochem. Biophys. Res. Commun. 235:499.
3. Kawabata, M. et al. (1998) Cytokine and Growth Factor Reviews 9:49.

Publications for BMPR-II (811-BR)(10)

Publications using 811-BR

• J Guo, B Liu, M Thorikay, M Yu, X Li, Z Tong, RM Salmon, RJ Read, P Ten Dijke, NW Morrell, W Li Crystal structures of BMPRII extracellular domain in binary and ternary receptor complexes with BMP10 Nature Communications, 2022-05-03;13(1):2395. 2022-05-03 [PMID: 35504921] (Surface Plasmon Resonance, Human)
• RL Cate, N di Clement, C Racine, NP Groome, RB Pepinsky, A Whitty The anti-M�llerian hormone prodomain is displaced from the hormone/prodomain complex upon bivalent binding to the hormone receptor The Journal of Biological Chemistry, 2021-11-19;0(0):101429. 2021-11-19 [PMID: 34801555] (ELISA Capture, Human)
• T Mang, K Kleinschmi, F Ploeger, A Schoeneman, S Lindemann, A Gigout BMPR1A is necessary for chondrogenesis and osteogenesis while BMPR1B prevents hypertrophic differentiation J. Cell. Sci., 2020-08-21;0(0):. 2020-08-21 [PMID: 32764110] (Surface Plasmon Resonance, Human)
• B Huang, Y Yuan, T Li, S Ding, W Zhang, Y Gu, C Liu Facilitated receptor-recognition and enhanced bioactivity of bone morphogenetic protein-2 on magnesium-substituted hydroxyapatite surface Sci Rep, 2016-04-14;6(0):24323. 2016-04-14 [PMID: 27075233] (Bioassay, Mouse)
• BR Yoon, YH Chung, SJ Yoo, K Kawara, J Kim, IS Yoo, CG Park, SW Kang, WW Lee Preferential Induction of the T Cell Auxiliary Signaling Molecule B7-H3 on Synovial Monocytes in Rheumatoid Arthritis J. Biol. Chem, 2015-12-23;291(8):4048-57. 2015-12-23 [PMID: 26702052] (Bioassay, Human)
• Y Kienast, U Jucknischk, S Scheiblich, M Thier, M de Wouters, A Haas, C Lehmann, V Brand, D Bernicke, K Honold, S Lorenz Rapid Activation of Bone Morphogenic Protein 9 by Receptor-mediated Displacement of Pro-domains J. Biol. Chem, 2015-12-16;291(7):3395-410. 2015-12-16 [PMID: 26677222] (Bioassay, Human)
• Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor Growth. J. Biol. Chem., 2011-07-07;286(34):30034-46. 2011-07-07 [PMID: 21737454] (Surface Plasmon Resonance, Human, Mouse)
• Sengle G, Ono RN, Lyons KM, Bachinger HP, Sakai LY A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7. J. Mol. Biol., 2008-07-02;381(4):1025-39. 2008-07-02 [PMID: 18621057] (ELISA (Capture), Enzyme Assay, Surface Plasmon Resonance, Human)
• Serpe M, Umulis D, Ralston A, Chen J, Olson DJ, Avanesov A, Othmer H, O'Connor MB, Blair SS The BMP-binding protein Crossveinless 2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling in Drosophila. Dev. Cell, 2008-06-01;14(6):940-53. 2008-06-01 [PMID: 18539121] (Binding Assay, Drosophila)
• Reversade B, De Robertis EM Regulation of ADMP and BMP2/4/7 at opposite embryonic poles generates a self-regulating morphogenetic field. Cell, 2005-12-16;123(6):1147-60. 2005-12-16 [PMID: 16360041] (Receptor Binding Assay, Human)

Bioinformatics

• Gene Symbol: BMPR2
• Uniprot:
  • Q13873()