Recombinant Mouse Crossveinless-2 Protein

• Reactivity: Mu
• Applications: Bioactivity

Recombinant Mouse Crossveinless-2 Protein Summary

• Details of Functionality: Measured by its ability to inhibit rhBMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Binnerts, M.E. et al. (2004) Biochem. Biophys. Res. Commun. 315:272. The ED₅₀ for this effect is 0.5-2 µg/mL in the presence of 30 ng/mL of Recombinant Human BMP-4 (Catalog # 314-BP).
• Source: Mouse myeloma cell line, NS0-derived mouse Crossveinless-2/CV-2 protein
  Val34-Arg685, with an N-terminal 9-His tag, Ala39-Asp369 & Pro370-Arg685
• Accession #: AAH66153
• N-terminal Sequence: His, Ala39 & Pro370
• Structure / Form: Disulfide-linked heterodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Bmper
• Purity: >95%, 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
• SDS-PAGE: 36-39 kDa and 50-55 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 with BSA as a carrier protein.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Mouse Crossveinless-2 Protein

• BMP binding endothelial regulator
• BMP-binding endothelial regulator precursor protein
• BMP-binding endothelial regulator protein
• BMPER
• Bone morphogenetic protein-binding endothelial cell precursor-derived regulator
• CRIM3
• crossveinless 2
• Crossveinless-2
• CV2
• CV-2
• hCV2
• KIAA1965
• Protein crossveinless-2

Background

Crossveinless-2 (CV-2), also known as bone morphogenetic protein-binding endothelial cell precursor-derived regulator (BMPER), is a secreted chordin-like protein that modulates the BMP signaling pathway (1-3). Mouse CV-2 is synthesized as a 685 amino acid (aa) residue precursor protein with a putative 39 aa signal peptide, five tandem chordin-like cysteine-rich (CR) domains, a partial von Willebrand factor type D domain (vWD), and a carboxyl trypsin inhibitor-like cysteine-rich domain (TIL) (1, 2, 4). Secreted CV-2 is reported to be proteolytically cleaved to generate two fragments that are disulfide-linked (1, 2). The cleavage site of R&D Systems’ recombinant CV-2 is found to be between asp³⁶⁹ and pro³⁷⁰ in the GDPH sequence within the vWD domain. This cleavage is likely due to an autocatalytic mechanism triggered by low pH comparable to that of the late secretory pathway (5). The GDPH sequence is conserved in CV-2 from other species. It is also found in multiple proteins that undergo a similar type of cleavage (5). Mouse CV-2 message is detected in many tissues, with the highest expression detected in the heart, lungs, and skin (2). It is also expressed in flk-1⁺ endothelial cell precursors and in primary chondrocytes (2). During embryonic development, CV-2 is expressed in the dorsal midline, regions of the telencephalon, migrating cells of the branchial neural crest and endothelial cells in the yolk sac (2). Mouse CV-2 shares 92% and 34% aa sequence identity with the human and Drosophila homologs, respectively (1, 4). Results from biochemical experiments using recombinant CV-2 show that CV-2 directly interacts with BMP-2, -4, and -6 to antagonize BMP signaling, which can regulate a wide range of differentiation processes (1, 2). In contrast, genetic data from Drosophila suggest that CV-2 potentiates BMP-signaling (6). It is possible that like TSG, CV-2 can positively and negatively modulate BMP signal transduction depending on the cell context (7).

1. Binnerts, M.E. et al. (2004) Biochem Biophys Res Commun. 315:272.
2. Moser, M. et al. (2003) Mol Cell Biol. 23:5664.
3. Garcia-Abreu, J. et al. (2002) Gene 287:39.
4. Coffinier, C. et al. (2002) Mech Dev. 119:S179.
5. Lidell, M.E. et al. (2003) J. Biol. Chem. 278:13944.
6. Conley, C.A. et al. (2000) Development 127:3947.
7. Kamimura, M. et al. (2004) Developmental Dynamics 230:434.

Publications for Crossveinless-2/CV-2/BMPER (2299-CV)(4)

Publications using 2299-CV

• Alison C. McGarvey, Stanislav Rybtsov, Céline Souilhol, Sara Tamagno, Ritva Rice, David Hills et al. A molecular roadmap of the AGM region reveals BMPER as a novel regulator of HSC maturation Journal of Experimental Medicine 2017-12-04 [PMID: 29093060] (Bioassay, Mouse)
• P Lockyer, H Mao, Q Fan, L Li, LY Yu-Lee, NT Eissa, C Patterson, L Xie, X Pi LRP1-Dependent BMPER Signaling Regulates Lipopolysaccharide-Induced Vascular Inflammation Arterioscler. Thromb. Vasc. Biol., 2017-06-08;37(8):1524-1535. 2017-06-08 [PMID: 28596374] (Bioassay, Mouse)
• Kelley R, Ren R, Pi X, Wu Y, Moreno I, Willis M, Moser M, Ross M, Podkowa M, Attisano L, Patterson C A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling. J. Cell Biol., 2009-02-16;184(4):597-609. 2009-02-16 [PMID: 19221194] (Bioassay, Mouse)
• Ambrosio AL, Taelman VF, Lee HX, Metzinger CA, Coffinier C, De Robertis EM Crossveinless-2 Is a BMP feedback inhibitor that binds Chordin/BMP to regulate Xenopus embryonic patterning. Dev. Cell, 2008-08-01;15(2):248-60. 2008-08-01 [PMID: 18694564] (Binding Assay, Enzyme Assay, Human)

Bioinformatics

• Gene Symbol: Bmper
• Uniprot:
  • AAH66153()