| 货号 | AF2299-SP |
| 别名 | 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 | 全称 | BMP-binding Endothelial Regulator Protein |
| 反应种属 | Mouse |
| 应用 | Western Blot(0.1 µg/mL) Immunohistochemistry(5-15 µg/mL) |
| 目标/特异性 | Detects mouse Crossveinless-2/CV-2 in direct ELISAs and Western blots. In Western blots, approximately 50% cross-reactivity with recombinant human CV-2 is observed. |
| 使用方法 | Western Blot: 0.1 µg/mL Immunohistochemistry: 5-15 µg/mL |
| 来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 产品组分 |
| 供应商 | R&D Systems |
| Entrez Gene IDs | 168667 (Human); 73230 (Mouse) |
| 应用文献 | |
| 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. Crossveinless-2 is required for the relocalization of Chordin protein within the vertebral field in mouse embryos. | |
| 纯化方式 | Antigen Affinity-purified |
| 免疫原 | Mouse myeloma cell line NS0-derived recombinant mouse Crossveinless-2/CV-2 (R&D Systems, Catalog # 2299-CV) Ala39-Arg685 Accession # AAH66153 |
| 内毒素水平 | <0.10 EU per 1 μg of the antibody by the LAL method. |
| 生物活性 | Mouse |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
| 背景 | 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 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 Drosophilasuggest 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). |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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Crossveinless‑2/CV‑2 in Mouse Embryo. Crossveinless‑2/CV‑2 was detected in immersion fixed frozen sections of mouse embryo (E13.5) using Mouse Crossveinless‑2/CV‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2299) at 10 µg/mL overnight at 4 °C. Tissue was stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to the epithelium surrounding the nasal cavity. View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections. |
