Recombinant Mouse TIE2 protein is a Mouse Fragment protein, expressed in CHO, with >90% purity and suitable for SDS-PAGE.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Tyrosine-protein kinase that acts as a 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 pro-inflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for postnatal 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.
CD202b, Hyk, Tie-2, Tie2, Tek, Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, p140 TEK, mTIE2
Recombinant Mouse TIE2 protein is a Mouse Fragment protein, expressed in CHO, with >90% purity and suitable for SDS-PAGE.
Constituents: PBS
Purity: > 90%, by SDS-PAGE.
Tyrosine-protein kinase that acts as a 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 pro-inflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for postnatal 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.
Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.
Proteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2).
TIE2 also known as TEK or CD202B is a receptor tyrosine kinase with a mass of approximately 145 kDa. It plays an important role in vascular development and maintenance. TIE2 is mainly expressed in endothelial cells which line the interior surface of blood vessels. It binds angiopoietins predominantly Angiopoietin-1 (Angpt1) influencing vascular stability and permeability. Researchers use TIE2 antibodies including anti-TIE and anti-clone to study its role and functions across various contexts.
TIE2 plays a central role in angiogenesis and blood vessel maturation. It forms a receptor complex with other components to mediate its effects. This interaction mainly involves Angpt1 which binds to TIE2 stabilizing blood vessels and preserving their integrity. TIE2 also participates in cell survival and migration processes necessary for normal vascular function. Researchers often perform Angpt1 ELISA in bulk to quantify interactions involving TIE2 in experiments.
TIE2 is important in the angiopoietin-TIE signaling pathway regulating vascular development. TIE2 is related to proteins such as Angpt1 which are centrally involved in this pathway. It also interacts with various signaling molecules including phosphatidylinositol-3-kinase (PI3K) which contributes to cell survival pathways. Alterations in the TIE2 signaling cascade can lead to aberrant angiogenesis and related pathologies.
TIE2 is implicated in several vascular diseases and cancer. Mutations or dysregulation of TIE2 can result in venous malformations and further compromise blood vessel integrity. In cancer TIE2 expression can influence tumor angiogenesis enhancing tumor growth and metastasis. TIE2 interacts with proteins like vascular endothelial growth factor (VEGF) which are involved in neovascularization and cancer progression. Understanding these interactions helps target therapeutic strategies in relevant diseases.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com