Boster

ELISA/assay

Human TIE2 PicoKine ELISA Kit

EK0519

96 wells/kit

380 USD

EK0519

Human TIE2 PicoKine ELISA Kit

380 USD

Expression system for standard: NSO; Immunogen sequence: A23-K745

Sandwich High Sensitivity ELISA kit for Quantitative Detection of Human TIE2

96 wells/kit

Human

ELISA

Tyrosine kinase with Ig and EGF homology domain 2(Tie-2), also called TEK tyrosine kinase, endothelial(TEK). Tie-2 and tie-1 are expressed in early embryonic vascular system and in maternal decidual vascular endothelial cells, where the vasculature undergoes an active angiogenesis. Tie-2, but not tie-1, expression was also detected in extraembryonic mesoderm of the amnion. Angiogenesis is coordinated with follicular cell growth in goitrogenesis. The angiopoietins, Ang-1 and Ang-2, are angiogenic growth factors acting through Tie-2. Tie-2 and Ang-1 are expressed in thyroid epithelial and endothelial cells, and Tie-2 is regulated by TSH and cAMP in follicular cells. And Tie-2 expression is increased in goiter in both humans and rats, consistent with a role in goitrogenesis. Tie2/Ang-1 signaling pathway plays a critical role in the maintenance of HSCs in a quiescent state in the BM niche. And the Tie-2 signaling pathway is also critical for endothelial cell-smooth muscle cell communication in venous morphogenesis.

There is cross-reactivity with human TIE1< 0.1%.

Angiopoietin-1 receptor

TEK

Tyrosine-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.

Angiopoietin-1 receptor

Nothing Found

Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.

Store at 4ËšC for 6 months, at -20ËšC for 12 months. Avoid multiple freeze-thaw cycles(Shipped with wet ice.)

Cell membrane; Single-pass type I membrane protein. 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.

Angiopoietin-1 receptor;2.7.10.1;Endothelial tyrosine kinase;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;hTIE2;p140 TEK;CD202b;TEK;TIE2, VMCM, VMCM1;

Detected 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.

Q02763