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anti-Human TIE1 Antibodies:
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Human Polyclonal TIE1 Primary Antibody for CyTOF, FACS - ABIN4899695
Danet, Pan, Luongo, Bonnet, Simon: Expansion of human SCID-repopulating cells under hypoxic conditions. in The Journal of clinical investigation 2003
Show all 7 Pubmed References
Human Polyclonal TIE1 Primary Antibody for IHC (p), ELISA - ABIN544355
Lin, Lee, Sun: Functions of the activation loop in Csk protein-tyrosine kinase. in The Journal of biological chemistry 2003
Show all 3 Pubmed References
Human Polyclonal TIE1 Primary Antibody for ICC, WB - ABIN871088
Gu, Zhang, Wang, Mo, Zhou, Chen, Liu, Zhang: Global expression of cell surface proteins in embryonic stem cells. in PLoS ONE 2011
Show all 2 Pubmed References
We identified colorectal cancer as a novel Tie1-expressing tumor, with Tie1-positive cells hardly detectable in the normal intestine. Tie1 expression did not influence cancer cell proliferation in regular in vitro cultures, but significantly affected malignant growth of transplanted tumors in vivo.
Tie1 directly interacts with Tie2 to promote ANG-induced vascular responses under noninflammatory conditions, whereas in inflammation, Tie1 cleavage contributes to loss of ANG2 agonist activity and vascular stability
Ang,Tie1 and Tie2 play roles in vascular development and pathogenesis of vascular diseases.[review]
In vitro binding assays with purified components reveal that Tie-integrin recognition is direct, and further demonstrate that the receptor binding domain of the Tie2 ligand Ang-1, but not the receptor binding domain of Ang-2, can independently associate with a5b1 or aVb3. cooperative Tie/integrin interactions selectively stimulate ERK/MAPK signaling in the presence of both Ang-1 and fibronectin
The inhibition of Tie-2 exerted by Tie-1can be relieved by Tie-1 ectodomain cleavage mediated by tumor- and inflammatory-related factors, which causes destabilization of vessels and initiates vessel remodeling in cancer. (Review)
T794A-expressing human umbilical vein endothelial cells formed significantly shorter tubes with fewer branches in three-dimensional Matrigel cultures, but did not alter Tie1 or Tie2 tyrosine phosphorylation or downstream signaling.
The decreasing expression of Tie1 may play an important role in the pathogenesis of primary lower extremity varicose veins.
Data propose that EndMT associated with Tie1 downregulation participates in the pathological development of stroma observed in tumours.
the effects of factors activating ectodomain cleavage on both Tie1 and Tie2 within the same population of cells, and their impact on angiopoietin signalling
these results suggest that the expression level of Tie1 and its physical interaction with Tie2 defines whether Ang2 functions as a Tie2 agonist or antagonist, thereby determining the context-dependent differential endothelial sensitivity to Ang2.
The Tie-1 immunoreactivity was dominantly observed in the heamangiogenic cells and cells cords, whereas the matured villi showed immunoreactivity only in other components.
Provide evidence for Tie1-Tie2 complex formation on the cell surface and identify molecular surface areas essential for recognition. The Tie1-Tie2 interactions are dynamic, inhibitory, and differentially modulated by angiopoietin-1 and -2.
A natural antisense transcript was identified for tyrosine kinase containing immunoglobulin and epidermal growth factor homology domain-1 (tie-1), tie-1AS long noncoding RNA in zebrafish, mouse, and humans.
Vascular endothelial growth factor modulates the Tie-2:Tie-1 receptor complex
high expression independently associated with shorter survival in patients with early chronic phase CML
Results describe the expression of angiopoietin-1, 2 and 4 and Tie-1 and 2 in gastrointestinal stromal tumors, leiomyomas and schwannomas.
Activation of Tie1 ectodomain cleavage increases cartilage oligomeric protein angiopoietin 1 activation of Tie2.
Overexpression and activation of Tie1 is associated with breast and colonic neopalsms
the trophoblastic shell of the very early human placenta, as well as endothelial cells and ACC exhibited strong staining intensity for Tie-1
Tie-1 has an inflammatory function in endothelial cells.
Data support an interactive model of Tie1 and Tie2 function, in which dynamically regulated Tie1 versus Tie2 expression determines the net positive or negative effect of Tie1 on Tie2 signaling.
Data indicate that receptor tyrosine kinase Tie1 deletion resulted in lack of lymphatic valves and collecting vessel defects.
In contrast to the important role of Tie2 in the regulation of blood vascular development, Tie1 is crucial in the process of lymphatic remodeling and maturation, which is independent of Tie2.
Tie1 regulates tumor angiogenesis, postnatal sprouting angiogenesis, and endothelial cell survival, which are controlled by VEGF, Angpt, and Notch signals
Shear stress conditions that modulate atherogenic events also regulate Tie1 expression. Therefore, Tie1 may play a novel proinflammatory role in atherosclerosis.
Developing lymphatic vasculature is particularly sensitive to alterations in Tie1 expression in mice.
Loss of Tie1 results in lymphatic vascular abnormalities that precede the blood vessel phenotype, suggesting that Tie1 is involved in lymphangiogenesis.
In the lung, Tie1 expression increases prior to birth and rises in the newborn animal, a pattern not found in other organs.
not required for differentiation and proliferation of hematopoiesis in the embryo, but required during postnatal bone marros hematopoiesis
Blood vessel homeostasis and endothelial cell survival depend on proper signalling through angiopoietin receptors such as the receptor tyrosine kinases Tie-1 and Tie-2. Tie-1 and Tie-2 localized to motile cilia of the oviduct.
Data show that angiopoietin 1 induces Tie1 phosphorylation in endothelial cells, and that this phosphorylation is Tie2 dependent.
Tie-1 upregulates VCAM-1, E-selectin, and ICAM-1, partly through a p38-dependent mechanism.
XAF1 possesses a potential antiangiogenesis effect. Suppressed expression of Tie-1, Ang-1, Ang-2 and c-Myc may be mechanistically responsible for the observed antiangiogenesis effect.
Expression of a non-phosphorylatable mutant of the Tie1 juxtamembrane domain threonine site (T794A) significantly disrupted vascular development, resulting in fish with stunted and poorly branched intersomitic vessels.
Tie-1 and Tie-2 are not required for early heart development, yet they have redundant roles for the maintenance of endocardial-myocardial connection in later stages.
This gene encodes a member of the tyrosine protein kinase family. The encoded protein plays a critical role in angiogenesis and blood vessel stability by inhibiting angiopoietin 1 signaling through the endothelial receptor tyrosine kinase Tie2. Ectodomain cleavage of the encoded protein relieves inhibition of Tie2 and is mediated by multiple factors including vascular endothelial growth factor. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
tyrosine kinase with immunoglobulin and epidermal growth factor homology domains 1
, tyrosine-protein kinase receptor Tie-1
, tyrosine kinase receptor 1
, tyrosine kinase with immunoglobulin and epidermal growth factor homology domains