• Species Reactivity

  Human

• Specificity

  Detects human Crossveinless‑2/CV‑2 in direct ELISAs and Western blots. In Western blots, 25% cross-reactivity with recombinant mouse CV-2 is observed.

• Source

  Monoclonal Rat IgG    _2A Clone # 355304

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant human Crossveinless‑2/CV‑2    
  Val34-Arg685    
  Accession # Q8N8U9

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Western Blot

  1 µg/mL

  Recombinant Human Crossveinless‑2/CV‑2 (Catalog # )

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Preparation and Storage

• Reconstitution

  Reconstitute at 0.5 mg/mL in sterile PBS.

• Shipping

  The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & 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.

• 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).

• References:

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.

• Long Name:

  BMP-binding Endothelial Regulator Protein

• Entrez Gene IDs:

  168667 (Human); 73230 (Mouse)

• Alternate Names:

  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