Human Crossveinless-2/CV-2 Biotinylated Antibody

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Product Details
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Human Crossveinless-2/CV-2 Biotinylated Antibody Summary

Species Reactivity
Detects human Crossveinless‑2/CV‑2 in Western blots. In Western blots, approximately 15% cross-reactivity with recombinant mouse CV-2 is observed.
Polyclonal Sheep IgG
Antigen Affinity-purified
Mouse myeloma cell line NS0-derived recombinant human Crossveinless‑2/CV‑2
Accession # Q8N8U9
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.


Recommended Concentration
Western Blot
0.1 µg/mL
Recombinant Human Crossveinless‑2/CV‑2 (Catalog # 1956-CV)

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.

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Preparation and Storage

Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
Reconstitution Buffer 1 (PBS)
Catalog #
Size / Price
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.
  • 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) 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 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).

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

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