phospho tie2 (R&D Systems)

R&D Systems is a verified supplier

R&D Systems manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

R&D Systems phospho tie2

a HMEC were transfected with scrambled-siRNA (sc-siRNA) or CHFR-siRNA. At 72 h post-transfection, cells stimulated with rAng1 (400 ng/ml) for different time intervals were used for IB analysis to determine phosphorylation of Akt1 at S473 and T308 ( n = 3 independent experiments). b Control HMEC and CHFR knockdown HMEC stimulated with rAng1 as above were stained with phospho-473-Akt1 specific antibody. c Control HMEC and CHFR knockdown HMEC were transfected with the Akt1 biosensor plasmid and then stimulated with rAng1 as above to assess live cell Akt1 activity by measuring the FRET ratio ( p <0.0001) ( left panel shows basal Akt activity; right panel shows Akt activity in response to rAng1 challenge). d-f Control HMEC and CHFR-siRNA treated HMEC stimulated with rAng1 were used for IB analysis to determine tyrosine phosphorylation <t>Tie2</t> ( d ), phosphorylation of GSK3β at S9 and phosphorylation of β-catenin ( e ), ( n = 3 independent experiments). a, d-e Shown are mean values ± SEM ( n = 3 independent experiments; two-way ANOVA followed by Tukey’s post-hoc test).

Phospho Tie2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tie2+antibody/Human%2FMouse+Phospho-Tie-2+(Y1102%2FY1100)+Antibody/bio_rxiv__64898__2026__03__31__715582-176-5-22
Average 91 stars, based on 5 article reviews

phospho tie2 - by Bioz Stars, 2026-10

91/100 stars

Images

1) Product Images from "Ubiquitin ligase CHFR impairs Tie2 signaling via K 48 -linked ubiquitylation and degradation of Akt1 in endothelial cells"

Article Title: Ubiquitin ligase CHFR impairs Tie2 signaling via K 48 -linked ubiquitylation and degradation of Akt1 in endothelial cells

Journal: bioRxiv

doi: 10.64898/2026.03.31.715582

Figure Legend Snippet: a HMEC were transfected with scrambled-siRNA (sc-siRNA) or CHFR-siRNA. At 72 h post-transfection, cells stimulated with rAng1 (400 ng/ml) for different time intervals were used for IB analysis to determine phosphorylation of Akt1 at S473 and T308 ( n = 3 independent experiments). b Control HMEC and CHFR knockdown HMEC stimulated with rAng1 as above were stained with phospho-473-Akt1 specific antibody. c Control HMEC and CHFR knockdown HMEC were transfected with the Akt1 biosensor plasmid and then stimulated with rAng1 as above to assess live cell Akt1 activity by measuring the FRET ratio ( p <0.0001) ( left panel shows basal Akt activity; right panel shows Akt activity in response to rAng1 challenge). d-f Control HMEC and CHFR-siRNA treated HMEC stimulated with rAng1 were used for IB analysis to determine tyrosine phosphorylation Tie2 ( d ), phosphorylation of GSK3β at S9 and phosphorylation of β-catenin ( e ), ( n = 3 independent experiments). a, d-e Shown are mean values ± SEM ( n = 3 independent experiments; two-way ANOVA followed by Tukey’s post-hoc test).

Techniques Used: Transfection, Phospho-proteomics, Control, Knockdown, Staining, Plasmid Preparation, Activity Assay

a HMEC were transfected with WT or K/R-mutant Akt1 constructs. At 36 h after transfection, cells were treated with LPS (5 μg/ml) for 0, 12, and 24h and then cells were used for IB to determine expression of Akt1 and VE-cadherin. Shown are mean values ± SEM (n = 3 independent experiments; two-way ANOVA followed by Tukey’s post hoc test). b TIME endothelial cells (telomerase-immortalized human dermal microvascular endothelial cell line) were transfected with WT or K/R mutant Akt1 constructs and stimulated with LPS (5 μg/ml) for 0 and 6 h. Confocal imaging showed that expression of K/R mutant Akt1 prevents degradation of VE-cadherin. c WT mice were injected (i.v.) with liposome-encapsulated pmCherry-tagged WT or K/R mutant Akt1 constructs. Lungs harvested 96 h after injection were subjected to cryosection and stained with EC marker antibody vWF (green). Confocal imaging confirms expression of pmCherry-Akt1 (red) plasmid in lung endothelial cells. d-f Liposome-mediated delivery of Akt1 (WT) or K/R-mutated Akt1 in WT mice prevents degradation of VE-cadherin, mitigates LPS-induced lung vascular leak (EBA uptake), and reduces PMN transmigration (MPO assay). Shown are mean values ± SEM ( n = 3 or n = 5 mice/group; two-way ANOVA followed by Tukey’s post hoc test). g Model for E3 ligase CHFR regulation of endothelial junctional barrier integrity. Under baseline condition, constitutive Ang1-Tie2 signaling in EC maintains endothelial junctional barrier through Akt1 activation-mediated inhibition of the transcription factor FoxO1 activation and Ang-2 expression. During vascular inflammatory conditions such as sepsis, TLR4 signaling induces the expression of E3 ligase CHFR in a FoxO1-dependent manner. Then the upregulated CHFR mediates K 48 -linked polyubiquitylation and degradation of Akt1 and VE-cadherin (Tiruppathi et al., 2023) to disassemble EC junctional barrier. CHFR-mediated loss of FoxO1 negative regulator Akt1 expression in EC leads to increased FoxO1 expression which in turn promotes sustained expression of Ang-2 in EC to induce life-threatening pulmonary edema.

Figure Legend Snippet: a HMEC were transfected with WT or K/R-mutant Akt1 constructs. At 36 h after transfection, cells were treated with LPS (5 μg/ml) for 0, 12, and 24h and then cells were used for IB to determine expression of Akt1 and VE-cadherin. Shown are mean values ± SEM (n = 3 independent experiments; two-way ANOVA followed by Tukey’s post hoc test). b TIME endothelial cells (telomerase-immortalized human dermal microvascular endothelial cell line) were transfected with WT or K/R mutant Akt1 constructs and stimulated with LPS (5 μg/ml) for 0 and 6 h. Confocal imaging showed that expression of K/R mutant Akt1 prevents degradation of VE-cadherin. c WT mice were injected (i.v.) with liposome-encapsulated pmCherry-tagged WT or K/R mutant Akt1 constructs. Lungs harvested 96 h after injection were subjected to cryosection and stained with EC marker antibody vWF (green). Confocal imaging confirms expression of pmCherry-Akt1 (red) plasmid in lung endothelial cells. d-f Liposome-mediated delivery of Akt1 (WT) or K/R-mutated Akt1 in WT mice prevents degradation of VE-cadherin, mitigates LPS-induced lung vascular leak (EBA uptake), and reduces PMN transmigration (MPO assay). Shown are mean values ± SEM ( n = 3 or n = 5 mice/group; two-way ANOVA followed by Tukey’s post hoc test). g Model for E3 ligase CHFR regulation of endothelial junctional barrier integrity. Under baseline condition, constitutive Ang1-Tie2 signaling in EC maintains endothelial junctional barrier through Akt1 activation-mediated inhibition of the transcription factor FoxO1 activation and Ang-2 expression. During vascular inflammatory conditions such as sepsis, TLR4 signaling induces the expression of E3 ligase CHFR in a FoxO1-dependent manner. Then the upregulated CHFR mediates K 48 -linked polyubiquitylation and degradation of Akt1 and VE-cadherin (Tiruppathi et al., 2023) to disassemble EC junctional barrier. CHFR-mediated loss of FoxO1 negative regulator Akt1 expression in EC leads to increased FoxO1 expression which in turn promotes sustained expression of Ang-2 in EC to induce life-threatening pulmonary edema.

Techniques Used: Transfection, Mutagenesis, Construct, Expressing, Imaging, Injection, Staining, Marker, Plasmid Preparation, Transmigration Assay, MPO Assay, Activation Assay, Inhibition

Incubation:

Article Title: Conversion of placental hemogenic endothelial cells to hematopoietic stem and progenitor cells.
Article Snippet: .. Frozen sections were cut into 10-μm slices and blocked in 5% BSA (0.3% Triton X-100) for 1 h at room temperature, followed by incubation with anti-CD44 antibody (Abcam, Cat.# ab157107) and anti-Tie2 antibody (R&D systems, Cat.# AF762) diluted in 1% BSA overnight at 4 °C. ..

Article Title: Conversion of placental hemogenic endothelial cells to hematopoietic stem and progenitor cells
Article Snippet: .. Frozen sections were cut into 10-μm slices and blocked in 5% BSA (0.3% Triton X-100) for 1 h at room temperature, followed by incubation with anti-CD44 antibody (Abcam, Cat.# ab157107) and anti-Tie2 antibody (R&D systems, Cat.# AF762) diluted in 1% BSA overnight at 4 °C. ..

Immunoprecipitation:

Article Title: Anti-angiopoietin-2 antibodies that induce Tie2 activation
Article Snippet: The membrane was blocked with TBS-T mixed with 5% (v/v) BSA for 1 hr at room temperature and incubated with anti-phospho tyrosine antibody (4G10, Millipore®) for 8 hrs at 4° C., followed by the incubation of HRP-conjugated anti-mouse antibody and subsequent Western blotting. .. To measure the amount of immunoprecipitated Tie2, the membrane was reacted in a stripping buffer (Thermo) for 15 min, then blocked again and reprobed with anti-Tie2 antibody (R&D® Systems, AF313). ..

Membrane:

Stripping Membranes:

Immunohistochemical staining:

Article Title: Finerenone ameliorates diabetic kidney disease exacerbated by deletion of natriuretic peptide/guanylyl cyclase-A signaling and dietary high-protein load.
Article Snippet: Neoamiyu was obtained from EA Pharma CO., Ltd. (Tokyo, Japan). .. Primary antibodies used for immunohistochemical and immunofluorescence studies were anti-GC-A antibody (GTX109810, GeneTex, Inc., Irvine, CA, USA), antiMAC2 antibody (CL8942F, Cedarlane, Ontario, Canada), anti-Wilms tumor 1 (WT1) antibody (sc-15421, Santa Cruz Biotechnology, Dallas, TX), anti-nephrin antibody (AF3159, R&D Systems, Inc., Minneapolis, MN, USA), and anti-Tie2 antibody (AF762, R&D Systems, Inc.). ..

Article Title: Finerenone ameliorates diabetic kidney disease exacerbated by deletion of natriuretic peptide/guanylyl cyclase-A signaling and dietary high-protein load
Article Snippet: Neoamiyu was obtained from EA Pharma CO., Ltd. (Tokyo, Japan). .. Primary antibodies used for immunohistochemical and immunofluorescence studies were anti-GC-A antibody (GTX109810, GeneTex, Inc., Irvine, CA, USA), anti-MAC2 antibody (CL8942F, Cedarlane, Ontario, Canada), anti-Wilms tumor 1 (WT1) antibody (sc-15421, Santa Cruz Biotechnology, Dallas, TX), anti-nephrin antibody (AF3159, R&D Systems, Inc., Minneapolis, MN, USA), and anti-Tie2 antibody (AF762, R&D Systems, Inc.). ..

Immunofluorescence:

Article Title: Finerenone ameliorates diabetic kidney disease exacerbated by deletion of natriuretic peptide/guanylyl cyclase-A signaling and dietary high-protein load
Article Snippet: Neoamiyu was obtained from EA Pharma CO., Ltd. (Tokyo, Japan). .. Primary antibodies used for immunohistochemical and immunofluorescence studies were anti-GC-A antibody (GTX109810, GeneTex, Inc., Irvine, CA, USA), anti-MAC2 antibody (CL8942F, Cedarlane, Ontario, Canada), anti-Wilms tumor 1 (WT1) antibody (sc-15421, Santa Cruz Biotechnology, Dallas, TX), anti-nephrin antibody (AF3159, R&D Systems, Inc., Minneapolis, MN, USA), and anti-Tie2 antibody (AF762, R&D Systems, Inc.). ..

other:

Article Title: TIE2 links MEKK3-KLF2/4 and PI3K signaling in cerebral cavernous malformation.
Article Snippet: TIE2 links MEKK3–KLF2/4 and PI3K signaling in cerebral cavernous malformation Lun Li1,2�, Marco Castro3,4�, Hiroki Hongo1,5�, Jian Ren1,6�, Robert Shenkar7�, Rashad Jabarkheel1,2�, Siqi Gao1�, Sweta Narayan1�, Maxwell Frankfurter1�, Alan T. Tang1�, Jisheng Yang1�, Mei Chen1�, Jenna Bockman1�, Patricia Mericko-Ishizuka1�, Roberto Alcazar7�, Georgio Sader7�, Javed Iqbal7�, Serena Kinkade7�, Rhonda Lightle7�, Andrew K. Ressler8�, Xianghu Qu9�, H. Scott Baldwin9�, Douglas A. Marchuk8�, Issam A. Awad7�, Jan-Karl Burkhardt2�, Michael Potente3,4�, and Mark L. Kahn1� Cerebral cavernous malformations (CCMs) are vascular lesions in the central nervous system that can cause strokes and seizures.. Aggressive CCM growth follows an endothelial cell two-hit mechanism in which enhanced MEKK3–KLF2/4 signaling stimulates PI3K signaling, but how these pathways are linked has been undefined.. Here, we use human CCM specimens, two mouse models of CCM disease, and primary human endothelial cells to examine the roles of the major endothelial growth factor receptors, VEGFR2 and TIE2.

Review