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Human TIE2 Protein 2530

$270.00$900.00

Summary

  • Expression: HEK293
  • Binding assay: Yes (SPR)
  • Amino Acid Range: Ala23-Leu748
SKU: 2530parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

AAA61139

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Angiopoietin-1 (Ang-1) is the primary agonist for Tie2 tyrosine kinase receptor (Tie2), and the effect of Ang-1-Tie2 signalling is context-dependent. Deficiency in either Ang-1 or Tie2 protein leads to severe microvascular defects and subsequent embryonic lethality in murine model. Tie2 receptors are expressed in several cell types, including endothelial cells, smooth muscle cells, fibroblasts, epithelial cells, monocytes, neutrophils, eosinophils and glial cells.

molecular weight

The protein has a predicted MW of 82.09 kDa. Due to glycosylation, the protein migrates to 90-110 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human TIE2 Protein 2530

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Angiopoietin-1 (Ang-1) is the primary agonist for Tie2 tyrosine kinase receptor (Tie2), and the effect of Ang-1-Tie2 signalling is context-dependent. Deficiency in either Ang-1 or Tie2 protein leads to severe microvascular defects and subsequent embryonic lethality in murine model. Tie2 receptors are expressed in several cell types, including endothelial cells, smooth muscle cells, fibroblasts, epithelial cells, monocytes, neutrophils, eosinophils and glial cells.
Protein names
Angiopoietin-1 receptor (EC 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) (CD antigen CD202b)
Protein family
Protein kinase superfamily, Tyr protein kinase family, Tie subfamily
Mass
125830Da
Function
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 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. {ECO:0000269|PubMed:12816861, ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:18366015, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:20651738, ECO:0000269|PubMed:9204896}.
Catalytic activity
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:11513602, ECO:0000269|PubMed:12609966, ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:8382358};
Subellular location
Cell membrane {ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:19079259, ECO:0000269|PubMed:27270174}; Single-pass type I membrane protein. Cell junction {ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:27270174}. Cell junction, focal adhesion {ECO:0000305|PubMed:19293632}. Cytoplasm, cytoskeleton. Secreted {ECO:0000269|PubMed:11806244}. Note=Recruited to cell-cell contacts in quiescent endothelial cells (PubMed:18425119, PubMed:18425120). 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 (PubMed:11806244). {ECO:0000269|PubMed:11806244, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120}.
Tissues
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. {ECO:0000269|PubMed:11806244, ECO:0000269|PubMed:8382358}.
Structure
Homodimer. Heterodimer with TIE1. Interacts with ANGPT1, ANGPT2 and ANGPT4 (PubMed:15284220, PubMed:32908006, PubMed:9204896). At cell-cell contacts in quiescent cells, forms a signaling complex composed of ANGPT1 plus TEK molecules from two adjoining cells. In the absence of endothelial cell-cell contacts, interaction with ANGPT1 mediates contacts with the extracellular matrix. Interacts with PTPRB; this promotes endothelial cell-cell adhesion. Interacts with DOK2, GRB2, GRB7, GRB14, PIK3R1 and PTPN11/SHP2. Colocalizes with DOK2 at contacts with the extracellular matrix in migrating cells. Interacts (tyrosine phosphorylated) with TNIP2. Interacts (tyrosine phosphorylated) with SHC1 (via SH2 domain). {ECO:0000269|PubMed:12609966, ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:16732286, ECO:0000269|PubMed:17253678, ECO:0000269|PubMed:17350837, ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:19451274, ECO:0000269|PubMed:19689429, ECO:0000269|PubMed:19854647, ECO:0000269|PubMed:32908006, ECO:0000269|PubMed:9204896, ECO:0000269|Ref.33}.
Post-translational modification
Proteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2). {ECO:0000269|PubMed:11806244}.; 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. {ECO:0000269|PubMed:11513602, ECO:0000269|PubMed:14665640}.; Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation. {ECO:0000269|PubMed:19689429}.
Domain
The soluble extracellular domain is functionally active in angiopoietin binding and can modu
Target Relevance information above includes information from UniProt accession: Q02763
The UniProt Consortium

SPR with Human TIE2 Protein
Human TIE2, His Tag immobilized on CM5 Chip can bind Human ANGPT2, His Tag with an affinity constant of 2.38 µM as determined in SPR assay (Biacore T200).
HPLC of Human TIE2 Protein
The purity of Human TIE2 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human TIE2 Protein
Human TIE2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

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