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Recombinant Mouse Crossveinless-2 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Crossveinless-2 Protein, CF 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 #
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
Publications
Read Publications using
2299-CV/CF in the following applications:

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
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 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 Mouse Crossveinless-2 Protein, CF

  • 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.

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Bioinformatics

Gene Symbol Bmper
Uniprot