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Mouse Anti-ENG Antibody (P4A4) (CBMAB-0101-YC)

Provided herein are mouse monoclonal antibodies against Human ENG. The antibody clone P4A4 can be used for immunoassay techniques, such as WB.
See all ENG antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
P4A4
Antibody Isotype
IgG2b, ĸ
Application
WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2b, ĸ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Supernatant
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Endoglin
Introduction
Endoglin (ENG) is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex, which is a major glycoprotein of the vascular endothelium. ENG has a crucial role in angiogenesis, therefore, making it an important protein for tumor growth, survival and metastasis of cancer cells to other locations in the body. Mutations in this gene cause hereditary hemorrhagic telangiectasia, also known as Osler-Rendu-Weber syndrome 1, an autosomal dominant multisystemic vascular dysplasia.
Entrez Gene ID
UniProt ID
Alternative Names
Endoglin; CD105 Antigen; END; Osler-Rendu-Weber Syndrome 1; HHT1; ORW1
Research Area
Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:21737454, PubMed:23300529).

Required for normal structure and integrity of adult vasculature (PubMed:7894484).

Regulates the migration of vascular endothelial cells (PubMed:17540773).

Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity).

May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity).

May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors (PubMed:1692830).

Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:8370410, PubMed:21737454, PubMed:22347366, PubMed:23300529).

Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (PubMed:21737454, PubMed:22347366, PubMed:23300529).
Biological Process
Angiogenesis Source: GO_Central
Artery morphogenesis Source: BHF-UCL
Atrial cardiac muscle tissue morphogenesis Source: BHF-UCL
Atrioventricular canal morphogenesis Source: BHF-UCL
BMP signaling pathway Source: BHF-UCL
Bone development Source: Ensembl
Branching involved in blood vessel morphogenesis Source: BHF-UCL
Cardiac atrium morphogenesis Source: BHF-UCL
Cardiac ventricle morphogenesis Source: BHF-UCL
Cell adhesion Source: UniProtKB-KW
Cell chemotaxis Source: BHF-UCL
Cell migration Source: BHF-UCL
Cell migration involved in endocardial cushion formation Source: Ensembl
Cell motility Source: BHF-UCL
Cellular response to mechanical stimulus Source: Ensembl
Central nervous system vasculogenesis Source: BHF-UCL
Detection of hypoxia Source: BHF-UCL
Dorsal aorta morphogenesis Source: BHF-UCL
Endocardial cushion morphogenesis Source: BHF-UCL
Epithelial to mesenchymal transition Source: GO_Central
Epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
Extracellular matrix constituent secretion Source: Ensembl
Extracellular matrix disassembly Source: BHF-UCL
Heart looping Source: BHF-UCL
Negative regulation of cell migration Source: BHF-UCL
Negative regulation of endothelial cell proliferation Source: BHF-UCL
Negative regulation of gene expression Source: BHF-UCL
Negative regulation of nitric-oxide synthase activity Source: BHF-UCL
Negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Negative regulation of protein autophosphorylation Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: BHF-UCL
Negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Outflow tract septum morphogenesis Source: BHF-UCL
Positive regulation of angiogenesis Source: Ensembl
Positive regulation of BMP signaling pathway Source: BHF-UCL
Positive regulation of collagen biosynthetic process Source: Ensembl
Positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
Positive regulation of gene expression Source: Ensembl
Positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Positive regulation of protein kinase B signaling Source: BHF-UCL
Positive regulation of protein phosphorylation Source: BHF-UCL
Positive regulation of systemic arterial blood pressure Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of vascular associated smooth muscle cell differentiation Source: BHF-UCL
Regulation of cell adhesion Source: BHF-UCL
Regulation of cell population proliferation Source: BHF-UCL
Regulation of phosphorylation Source: BHF-UCL
Regulation of transcription, DNA-templated Source: HGNC-UCL
Regulation of transforming growth factor beta receptor signaling pathway Source: HGNC-UCL
Response to corticosteroid Source: Ensembl
Response to drug Source: Ensembl
Response to hypoxia Source: BHF-UCL
Smooth muscle tissue development Source: BHF-UCL
Transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Vascular associated smooth muscle cell development Source: BHF-UCL
Vasculogenesis Source: BHF-UCL
Venous blood vessel morphogenesis Source: BHF-UCL
Ventricular trabecula myocardium morphogenesis Source: BHF-UCL
Wound healing Source: BHF-UCL
Cellular Location
Cell membrane
Involvement in disease
Telangiectasia, hereditary hemorrhagic, 1 (HHT1):
A multisystemic vascular dysplasia leading to dilation of permanent blood vessels and arteriovenous malformations of skin, mucosa, and viscera. The disease is characterized by recurrent epistaxis and gastro-intestinal hemorrhage. Visceral involvement includes arteriovenous malformations of the lung, liver, and brain.
Topology
Extracellular: 26-586
Helical: 587-611
Cytoplasmic: 612-658

Vicen, M., Igreja Sá, I. C., Tripská, K., Vitverová, B., Najmanová, I., Eissazadeh, S., ... & Nachtigal, P. (2021). Membrane and soluble endoglin role in cardiovascular and metabolic disorders related to metabolic syndrome. Cellular and Molecular Life Sciences, 78(6), 2405-2418.

Tual-Chalot, S., Garcia-Collado, M., Redgrave, R. E., Singh, E., Davison, B., Park, C., ... & Arthur, H. M. (2020). Loss of endothelial endoglin promotes high-output heart failure through peripheral arteriovenous shunting driven by VEGF signaling. Circulation research, 126(2), 243-257.

Singh, E., Redgrave, R. E., Phillips, H. M., & Arthur, H. M. (2020). Arterial endoglin does not protect against arteriovenous malformations. Angiogenesis, 23(4), 559-566.

Rossi, E., Bernabeu, C., & Smadja, D. M. (2019). Endoglin as an adhesion molecule in mature and progenitor endothelial cells: a function beyond TGF-β. Frontiers in Medicine, 6, 10.

Meurer, S., Wimmer, A. E., van de Leur, E., & Weiskirchen, R. (2019). Endoglin trafficking/exosomal targeting in liver cells depends on N-glycosylation. Cells, 8(9), 997.

Lawera, A., Tong, Z., Thorikay, M., Redgrave, R. E., Cai, J., van Dinther, M., ... & Li, W. (2019). Role of soluble endoglin in BMP9 signaling. Proceedings of the National Academy of Sciences, 116(36), 17800-17808.

Puerto-Camacho, P., Amaral, A. T., Lamhamedi-Cherradi, S. E., Menegaz, B. A., Castillo-Ecija, H., Ordóñez, J. L., ... & de Álava, E. (2019). Preclinical Efficacy of Endoglin-Targeting Antibody–Drug Conjugates for the Treatment of Ewing SarcomaOMTX703 Targets Endoglin in Ewing Sarcoma. Clinical Cancer Research, 25(7), 2228-2240.

Vicen, M., Vitverova, B., Havelek, R., Blazickova, K., Machacek, M., Rathouska, J., ... & Nachtigal, P. (2019). Regulation and role of endoglin in cholesterol‐induced endothelial and vascular dysfunction in vivo and in vitro. The FASEB Journal, 33(5), 6099-6114.

Yang, X., Zhao, J., Duan, S., Hou, X., Li, X., Hu, Z., ... & Lu, X. (2019). Enhanced cytotoxic T lymphocytes recruitment targeting tumor vasculatures by endoglin aptamer and IP-10 plasmid presenting liposome-based nanocarriers. Theranostics, 9(14), 4066.

Sugden, W. W., & Siekmann, A. F. (2018). Endothelial cell biology of Endoglin in hereditary hemorrhagic telangiectasia. Current opinion in hematology, 25(3), 237-244.

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For research use only. Not intended for any clinical use.

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