Recombinant Human Crossveinless-2 Protein Summary
Product Specifications
Val34-Asp369, with an N-terminal 7-His tag & Ala39-Asp369 (N-terminal fragments) & Pro370-Arg685 (C-terminal fragment)
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
1956-CV
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 200 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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1956-CV/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 200 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
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) 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, 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.
Citations for Recombinant Human Crossveinless-2 Protein
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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Citations: Showing 1 - 6
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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: Whole Cells
Applications: Bioassay -
Bulk cell density and Wnt/TGFbeta signalling regulate mesendodermal patterning of human pluripotent stem cells
Nat Commun, 2016-12-09;7(0):13602.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Bone morphogenetic protein-9 suppresses growth of myeloma cells by signaling through ALK2 but is inhibited by endoglin.
Authors: Olsen O, Wader K, Misund K, Vatsveen T, Ro T, Mylin A, Turesson I, Stordal B, Moen S, Standal T, Waage A, Sundan A, Holien T
Blood Cancer J, 2014-03-21;4(0):e196.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
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: Whole Cells
Applications: Bioassay -
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
Applications: Bioassay -
BMP activity controlled by BMPER regulates the proinflammatory phenotype of endothelium.
Authors: Helbing T, Rothweiler R, Ketterer E, Goetz L, Heinke J, Grundmann S, Duerschmied D, Patterson C, Bode C, Moser M
Blood, 2011-09-07;118(18):5040-9.
Species: Human, Mouse
Sample Types: In Vivo, Whole Cells
Applications: Bioassay, In Vivo
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