Rat Anti-Tek Recombinant Antibody (CBYJT-2506) (CBMAB-T1658-YJ)

Rat

Mouse

CBYJT-2506

IgG2a

ELISA, FC, IP, WB

The extracellular domain of mouse Tie2 receptor

Mouse

IgG2a

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

PBS, pH 7.4

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

TEK Gene(Protein Coding) TEK Receptor Tyrosine Kinase

Tek is a 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. Tek has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. It is required for normal angiogenesis and heart development during embryogenesis. It is required for post-natal hematopoiesis. After birth, Tek activates or inhibits angiogenesis, depending on the context. It inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts.

Hyk; STK1; Tie2; Tie-2; Cd202b; AA517024

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 pro-inflammatory 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.

Biological Process angiogenesisSource:UniProtKB
Biological Process cell-cell signalingSource:ProtInc1 Publication
Biological Process definitive hemopoiesisSource:UniProtKB1 Publication
Biological Process endothelial cell proliferationSource:UniProtKB
Biological Process glomerulus vasculature developmentSource:UniProtKB
Biological Process heart developmentSource:UniProtKB
Biological Process heart trabecula formationSource:UniProtKB
Biological Process negative regulation of angiogenesisSource:UniProtKB1 Publication
Biological Process negative regulation of apoptotic processSource:UniProtKB1 Publication
Biological Process negative regulation of endothelial cell apoptotic processSource:UniProtKB
Biological Process negative regulation of inflammatory responseSource:UniProtKB1 Publication
Biological Process peptidyl-tyrosine phosphorylationSource:UniProtKB1 Publication
Biological Process positive regulation of actin cytoskeleton reorganizationSource:UniProtKB1 Publication
Biological Process positive regulation of angiogenesisSource:UniProtKB1 Publication
Biological Process positive regulation of endothelial cell migrationSource:UniProtKB1 Publication
Biological Process positive regulation of endothelial cell proliferationSource:UniProtKB1 Publication
Biological Process positive regulation of ERK1 and ERK2 cascadeSource:UniProtKB1 Publication
Biological Process positive regulation of focal adhesion assemblySource:UniProtKB1 Publication
Biological Process positive regulation of intracellular signal transductionSource:UniProtKB1 Publication
Biological Process positive regulation of kinase activitySource:GO_Central1 Publication
Biological Process positive regulation of MAPK cascadeSource:GO_Central1 Publication
Biological Process positive regulation of phosphatidylinositol 3-kinase activitySource:UniProtKB2 Publications
Biological Process positive regulation of phosphatidylinositol 3-kinase signalingSource:UniProtKB3 Publications
Biological Process positive regulation of protein kinase B signalingSource:UniProtKB1 Publication
Biological Process positive regulation of protein phosphorylationSource:UniProtKB1 Publication
Biological Process protein autophosphorylationSource:UniProtKB1 Publication
Biological Process regulation of endothelial cell apoptotic processSource:UniProtKB1 Publication
Biological Process regulation of establishment or maintenance of cell polaritySource:UniProtKB1 Publication
Biological Process regulation of vascular permeabilitySource:UniProtKB2 Publications
Biological Process signal transductionSource:ProtInc1 Publication
Biological Process sprouting angiogenesisSource:UniProtKB1 Publication
Biological Process substrate adhesion-dependent cell spreadingSource:UniProtKB1 Publication
Biological Process Tie signaling pathwaySource:UniProtKB2 Publications
Biological Process transmembrane receptor protein tyrosine kinase signaling pathwaySource:UniProtKB1 Publication

Dominantly inherited venous malformations (VMCM):
An error of vascular morphogenesis characterized by dilated, serpiginous channels.
Glaucoma 3, primary congenital, E (GLC3E):
An autosomal dominant form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor.

Extracellular: 23-748
Helical: 749-769
Cytoplasmic: 770-1124

Proteolytic 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.