Human TIE2/TEK/CD202b protein (Recombinant) (C-hFc & His) (STJP002572)

SKU:
STJP002572

Current Stock:
Host: HEK293 cells
Reactivity: Human
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Recombinant-Human TIE2/TEK/CD202b-C-hFc & His protein was developed from hek293 cells and has a target region of C-hFc & His. For use in research applications.
Formulation: Lyophilized from a 0.22 Mu m filtered solution of PBS, pH 7.4.
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Immunoreactivity: Measured by its binding ability in a functional ELISA. Immobilized Human ANGP2 at 1 Mu g/mL (100 Mu L/well) can bind Human Tie2 with a linear range of 3.98-467.9 ng/mL.2.Measured by its binding ability in a functional ELISA.Immobilized PE anti-human
Gene Symbol: TEK
Gene ID: 7010
Uniprot ID: TIE2_HUMAN
Immunogen Region: Ala23-Lys745
Immunogen: Recombinant Human TIE2/TEK/CD202b Protein is produced by HEK293 expression system. The target protein is expressed with sequence (Ala23-Lys745) of human Tie2/CD202b/TEK (Accession #NP_000450.2) fused with an Fc, 6×His tag at the C-terminus.
Post Translational Modifications 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.
Function 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.
Protein Name Angiopoietin-1 Receptor
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
Cd Antigen Cd202b
Database Links Reactome: R-HSA-210993
Reactome: R-HSA-5673001
Cellular Localisation Cell Membrane
Single-Pass Type I Membrane Protein
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
Alternative Protein Names Angiopoietin-1 Receptor protein
Endothelial Tyrosine Kinase protein
Tunica Interna Endothelial Cell Kinase protein
Tyrosine Kinase With Ig And Egf Homology Domains-2 protein
Tyrosine-Protein Kinase Receptor Tek protein
Tyrosine-Protein Kinase Receptor Tie-2 protein
Htie2 protein
P140 Tek protein
Cd Antigen Cd202b protein
TEK protein
TIE2 protein
VMCM protein
VMCM1 protein

Information sourced from Uniprot.org

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