Human Crossveinless-2/CV-2 Antibody Summary
Val34-Arg685
Accession # Q8N8U9
Applications
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.
Reconstitution Calculator
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.
Background: Crossveinless-2/CV-2
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). Human CV-2 is synthesized as a 685 amino acid (aa) 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, 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). Human CV-2 message is detected in many tissues, with the highest expression detected in adult brain and adult and fetal lung (1). It is also expressed in Flk-1+ endothelial cell precursors and in primary chondrocytes (2). During embryonic development, CV-2 is expressed in regions of high BMP signaling, such as the posterior primitive streak and the ventral tail bud (4). Human CV-2 shares 92% and 34% aa sequence identity with the mouse 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.
Product Datasheets
Citations for Human 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.
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Extracellular bone morphogenetic protein modulator BMPER and twisted gastrulation homolog 1 preserve arterial-venous specification in zebrafish blood vessel development and regulate Notch signaling in endothelial cells
Authors: JS Esser, RE Steiner, M Deckler, H Schmitt, B Engert, S Link, A Charlet, C Patterson, C Bode, Q Zhou, M Moser
FEBS J., 2018-03-09;0(0):.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Osteoblast-like differentiation of cultured human coronary artery smooth muscle cells by bone morphogenetic protein endothelial cell precursor-derived regulator (BMPER).
Authors: Satomi-Kobayashi S, Kinugasa M, Kobayashi R, Hatakeyama K, Kurogane Y, Ishida T, Emoto N, Asada Y, Takai Y, Hirata K, Rikitake Y
J Biol Chem, 2012-07-09;287(36):30336-45.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Crossveinless 2 regulates bone morphogenetic protein 9 in human and mouse vascular endothelium.
Authors: Yao Y, Jumabay M, Ly A, Radparvar M, Wang AH, Abdmaulen R, Bostrom KI
Blood, 2012-04-03;119(21):5037-47.
Species: Human
Sample Types: Cell Lysates, Whole Cells
Applications: IHC, Immunoprecipitation, Western Blot -
Bone morphogenetic protein modulator BMPER is highly expressed in malignant tumors and controls invasive cell behavior.
Authors: Heinke J, Kerber M, Rahner S
Oncogene, 2011-10-24;31(24):2919-30.
Species: Human
Sample Types: Cell Lysates, Whole Cells
Applications: ICC, Western Blot -
Kruppel-like factor 15 regulates BMPER in endothelial cells.
Authors: Helbing T, Volkmar F, Goebel U, Heinke J, Diehl P, Pahl HL, Bode C, Patterson C, Moser M
Cardiovasc. Res., 2009-09-17;85(3):551-9.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot
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