Mouse Crossveinless-2/CV-2 Antibody
Mouse Crossveinless-2/CV-2 Antibody Summary
Accession # AAH66153
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 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).
- Binnerts, M.E. et al. (2004) Biochem Biophys Res Commun. 315:272.
- Moser, M. et al. (2003) Mol Cell Biol. 23:5664.
- Garcia-Abreu, J. et al. (2002) Gene 287:39.
- Coffinier, C. et al. (2002) Mech Dev. 119:S179.
- Lidell, M.E. et al. (2003) J. Biol. Chem. 278:13944.
- Conley, C.A. et al. (2000) Development 127:3947.
- Kamimura, M. et al. (2004) Developmental Dynamics 230:434.
Citation for Mouse Crossveinless-2/CV-2 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling.
Authors: Kelley R, Ren R, Pi X, Wu Y, Moreno I, Willis M, Moser M, Ross M, Podkowa M, Attisano L, Patterson C
J. Cell Biol., 2009-02-16;184(4):597-609.
Sample Types: Cell Lysates
Applications: Western Blot
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