Key features and details
- Biotin Rat monoclonal [TEK4] to TIE2
- Reacts with: Mouse
- Conjugation: Biotin
- Isotype: IgG1
Product nameBiotin Anti-TIE2 antibody [TEK4]
See all TIE2 primary antibodies
DescriptionBiotin Rat monoclonal [TEK4] to TIE2
Species reactivityReacts with: Mouse
Mouse TIE2 extracellular domain
- Mouse bone marrow cell suspensions
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Storage bufferpH: 7.20
Preservative: 0.09% Sodium azide
Constituents: 0.87% Sodium chloride, PBS
Concentration information loading...
PurityProtein G purified
Light chain typekappa
FunctionTyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
Tissue specificityDetected in umbilical vein endothelial cells. Proteolytic processing gives rise to a soluble extracellular domain that is detected in blood plasma (at protein level). Predominantly expressed in endothelial cells and their progenitors, the angioblasts. Has been directly found in placenta and lung, with a lower level in umbilical vein endothelial cells, brain and kidney.
Involvement in diseaseDominantly inherited venous malformations
May play a role in a range of diseases with a vascular component, including neovascularization of tumors, psoriasis and inflammation.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.
Contains 3 EGF-like domains.
Contains 3 fibronectin type-III domains.
Contains 2 Ig-like C2-type (immunoglobulin-like) domains.
Contains 1 protein kinase domain.
DomainThe soluble extracellular domain is functionally active in angiopoietin binding and can modulate the activity of the membrane-bound form by competing for angiopoietins.
modificationsProteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2).
Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner, where Tyr-992 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at Tyr-1108 and at additional tyrosine residues. ANGPT1-induced phosphorylation is impaired during hypoxia, due to increased expression of ANGPT2. Phosphorylation is important for interaction with GRB14, PIK3R1 and PTPN11. Phosphorylation at Tyr-1102 is important for interaction with SHC1, GRB2 and GRB7. Phosphorylation at Tyr-1108 is important for interaction with DOK2 and for coupling to downstream signal transduction pathways in endothelial cells. Dephosphorylated by PTPRB.
Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
Cellular localizationCell membrane. Cell junction. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Secreted. Recruited to cell-cell contacts in quiescent endothelial cells. Colocalizes with the actin cytoskeleton and at actin stress fibers during cell spreading. Recruited to the lower surface of migrating cells, especially the rear end of the cell. Proteolytic processing gives rise to a soluble extracellular domain that is secreted.
- Information by UniProt
- Angiopoietin 1 receptor antibody
- Angiopoietin-1 receptor antibody
- CD202b antibody
ab95721 has been referenced in 3 publications.
- Ma M et al. Preeclampsia is associated with hypermethylation of IGF-1 promoter mediated by DNMT1. Am J Transl Res 10:16-39 (2018). PubMed: 29422991
- Lelievre E et al. Deficiency in the p110alpha subunit of PI3K results in diminished Tie2 expression and Tie2(-/-)-like vascular defects in mice. Blood 105:3935-8 (2005). PubMed: 15687236
- Hsu HC et al. Hematopoietic stem cells express Tie-2 receptor in the murine fetal liver. Blood 96:3757-62 (2000). PubMed: 11090057