Recombinant Mouse Crossveinless-2 Protein Summary
Product Specifications
Val34-Arg685, with an N-terminal 9-His tag, Ala39-Asp369 & Pro370-Arg685
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.
2299-CV
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 250 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.
|
2299-CV/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 250 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). 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).
- 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 Mouse 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 - 3
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LRP1-Dependent BMPER Signaling Regulates Lipopolysaccharide-Induced Vascular Inflammation
Authors: P Lockyer, H Mao, Q Fan, L Li, LY Yu-Lee, NT Eissa, C Patterson, L Xie, X Pi
Arterioscler. Thromb. Vasc. Biol., 2017-06-08;37(8):1524-1535.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
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.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Crossveinless-2 Is a BMP feedback inhibitor that binds Chordin/BMP to regulate Xenopus embryonic patterning.
Authors: Ambrosio AL, Taelman VF, Lee HX, Metzinger CA, Coffinier C, De Robertis EM
Dev. Cell, 2008-08-01;15(2):248-60.
Species: Human
Sample Types: N/A, Recombinant Protein
Applications: Binding Assay, Enzyme Assay
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