tie2 plasmid  (Sino Biological)


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    Name:
    TIE2 cDNA ORF Clone Human N HA tag
    Description:
    Full length Clone DNA of Human TEK tyrosine kinase endothelial with N terminal HA tag
    Catalog Number:
    HG10700-NY
    Price:
    295.0
    Category:
    cDNA Clone
    Applications:
    Stable or Transient mammalian expression
    Size:
    1Unit
    Product Aliases:
    CD202B cDNA ORF Clone Human, TIE-2 cDNA ORF Clone Human, TIE2 cDNA ORF Clone Human, VMCM cDNA ORF Clone Human, VMCM1 cDNA ORF Clone Human
    Molecule Name:
    TEK,Tie2,
    Buy from Supplier


    Structured Review

    Sino Biological tie2 plasmid
    TIE2 cDNA ORF Clone Human N HA tag
    Full length Clone DNA of Human TEK tyrosine kinase endothelial with N terminal HA tag
    https://www.bioz.com/result/tie2 plasmid/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tie2 plasmid - by Bioz Stars, 2021-09
    92/100 stars

    Images

    1) Product Images from "Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand"

    Article Title: Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand

    Journal: ACS chemical biology

    doi: 10.1021/acschembio.9b00724

    Intravital Microscopy. Tie2 reporter mouse, with implanted dorsal skin chambers, were injected with Reb-TMR (20 mg/kg, tail vein I.V.). About 1 hour after injection, select sites in the vascularized region were imaged. The two sites above show Reb-TMR lining the endothelia of the blood vessels, overlaying Tie2.
    Figure Legend Snippet: Intravital Microscopy. Tie2 reporter mouse, with implanted dorsal skin chambers, were injected with Reb-TMR (20 mg/kg, tail vein I.V.). About 1 hour after injection, select sites in the vascularized region were imaged. The two sites above show Reb-TMR lining the endothelia of the blood vessels, overlaying Tie2.

    Techniques Used: Intravital Microscopy, Injection

    Quantitative binding data and inhibition of Reb-TMR (a) Representative images of Reb-TMR in HUVEC cells in the presence (below) or absence (top) of unlabeled rebastinib (10 uM). (b) Quantification of Reb-TMR fluorescent intensity as a function of increasing concentration of unlabeled rebastinib. Reported is the mean single cell fluorescent intensity per well, N = 2 wells. Error bars correspond to S.D. (c) Biochemical fluorescent polarization assay of rebastinib-bodipy TMR (0.8 uM) on enzymatic domain of Tie2. Leftmost point corresponds to polarization of Reb-TMR in PBS, and right points correspond to polarization of Reb-TMR with Tie2, and in increasing concentrations of unlabeled rebastinib (0,0.1,1,10 uM). Reported is mean over N = 2 wells. Error bars correspond to S.D.
    Figure Legend Snippet: Quantitative binding data and inhibition of Reb-TMR (a) Representative images of Reb-TMR in HUVEC cells in the presence (below) or absence (top) of unlabeled rebastinib (10 uM). (b) Quantification of Reb-TMR fluorescent intensity as a function of increasing concentration of unlabeled rebastinib. Reported is the mean single cell fluorescent intensity per well, N = 2 wells. Error bars correspond to S.D. (c) Biochemical fluorescent polarization assay of rebastinib-bodipy TMR (0.8 uM) on enzymatic domain of Tie2. Leftmost point corresponds to polarization of Reb-TMR in PBS, and right points correspond to polarization of Reb-TMR with Tie2, and in increasing concentrations of unlabeled rebastinib (0,0.1,1,10 uM). Reported is mean over N = 2 wells. Error bars correspond to S.D.

    Techniques Used: Binding Assay, Inhibition, Concentration Assay

    Co-localization (a) High resolution imaging of HUVECs. Treatment of HUVECs with Reb-TMR (100 nM) followed by a stain for Tie2 shows colocalization of the two markers in the cytoplasm (b) Correlation of Reb-TMR and Tie2 immunofluorescence signals (Pearson r 2 = 0.88)
    Figure Legend Snippet: Co-localization (a) High resolution imaging of HUVECs. Treatment of HUVECs with Reb-TMR (100 nM) followed by a stain for Tie2 shows colocalization of the two markers in the cytoplasm (b) Correlation of Reb-TMR and Tie2 immunofluorescence signals (Pearson r 2 = 0.88)

    Techniques Used: Imaging, Staining, Immunofluorescence

    Modeling. Addition of a linker to the amide of rebastinib allows for coupling of a fluorophore to the small molecule. Based on a previously published structure of rebastinib in complex with Tie2 (PDB: 6MWE), we predicted this addition should not interfere with binding of rebastinib to Tie2.
    Figure Legend Snippet: Modeling. Addition of a linker to the amide of rebastinib allows for coupling of a fluorophore to the small molecule. Based on a previously published structure of rebastinib in complex with Tie2 (PDB: 6MWE), we predicted this addition should not interfere with binding of rebastinib to Tie2.

    Techniques Used: Binding Assay

    Related Articles

    Plasmid Preparation:

    Article Title: Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand
    Article Snippet: .. TIE2 plasmid was obtained from SinoBiological (HG10700-NY). ..

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    Sino Biological tie 2 deletion mouse tie2 mtie2 cdna plasmids
    Deletion of <t>Tie2</t> gene in primary ECs using CRISPR-Cas9. ( A ) Cultured primary HLMVECs were transduced by EGFP-Cas9 adenovirus and sgRNA lentivirus targeting on Tie2 and subjected to flow cytometry analysis of EGFP expression. In a separate study, HLMVECs were transduced by GFP lentivirus and subjected to flow cytometry analysis of EGFP expression as an indicator of lentivirus transduction efficiency. ( B ) Protein expression of Tie2 in vector control and Tie2 knockout HLMVECs induced by CRISPR-Cas9 was determined by immunoblotting. Overexpression of mouse Tie2 in Tie2 −/− HLMVECs was determined to assess the ability to rescue Tie2 expression after deletion. The uncropped full-length gels can be found in Supplementary Fig. S1 . ( C ) Quantification of Tie2 protein expression from 3 independent experiments. sgRNA Tie2-1 and sgRNA Tie2-2 are CRISPR-Cas9-mediated deletions of <t>Tie-2</t> at two distinction domains of Tie2 (two different sgRNAs). HuTie2KO1 and HuTie2KO2 + mTie2 represent restoration of Tie-2 expression in cells having undergone Tie-2 deletion. Differences were calculated using one-way ANOVA. P values less than 0.05 are indicated in the graph. ( D ) T7E1 assay detecting mutation on HLMVECs edited by CRISPR-Cas9 with Tie2 sgRNAs as showing a series of bands. Wild-types cells with or without Cas9 or vector only show single bands (negative controls).
    Tie 2 Deletion Mouse Tie2 Mtie2 Cdna Plasmids, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tie 2 deletion mouse tie2 mtie2 cdna plasmids/product/Sino Biological
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tie 2 deletion mouse tie2 mtie2 cdna plasmids - by Bioz Stars, 2021-09
    90/100 stars
      Buy from Supplier

    92
    Sino Biological tie2 plasmid
    Intravital Microscopy. <t>Tie2</t> reporter mouse, with implanted dorsal skin chambers, were injected with Reb-TMR (20 mg/kg, tail vein I.V.). About 1 hour after injection, select sites in the vascularized region were imaged. The two sites above show Reb-TMR lining the endothelia of the blood vessels, overlaying Tie2.
    Tie2 Plasmid, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tie2 plasmid/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tie2 plasmid - by Bioz Stars, 2021-09
    92/100 stars
      Buy from Supplier

    Image Search Results


    Deletion of Tie2 gene in primary ECs using CRISPR-Cas9. ( A ) Cultured primary HLMVECs were transduced by EGFP-Cas9 adenovirus and sgRNA lentivirus targeting on Tie2 and subjected to flow cytometry analysis of EGFP expression. In a separate study, HLMVECs were transduced by GFP lentivirus and subjected to flow cytometry analysis of EGFP expression as an indicator of lentivirus transduction efficiency. ( B ) Protein expression of Tie2 in vector control and Tie2 knockout HLMVECs induced by CRISPR-Cas9 was determined by immunoblotting. Overexpression of mouse Tie2 in Tie2 −/− HLMVECs was determined to assess the ability to rescue Tie2 expression after deletion. The uncropped full-length gels can be found in Supplementary Fig. S1 . ( C ) Quantification of Tie2 protein expression from 3 independent experiments. sgRNA Tie2-1 and sgRNA Tie2-2 are CRISPR-Cas9-mediated deletions of Tie-2 at two distinction domains of Tie2 (two different sgRNAs). HuTie2KO1 and HuTie2KO2 + mTie2 represent restoration of Tie-2 expression in cells having undergone Tie-2 deletion. Differences were calculated using one-way ANOVA. P values less than 0.05 are indicated in the graph. ( D ) T7E1 assay detecting mutation on HLMVECs edited by CRISPR-Cas9 with Tie2 sgRNAs as showing a series of bands. Wild-types cells with or without Cas9 or vector only show single bands (negative controls).

    Journal: Scientific Reports

    Article Title: Method for Dual Viral Vector Mediated CRISPR-Cas9 Gene Disruption in Primary Human Endothelial Cells

    doi: 10.1038/srep42127

    Figure Lengend Snippet: Deletion of Tie2 gene in primary ECs using CRISPR-Cas9. ( A ) Cultured primary HLMVECs were transduced by EGFP-Cas9 adenovirus and sgRNA lentivirus targeting on Tie2 and subjected to flow cytometry analysis of EGFP expression. In a separate study, HLMVECs were transduced by GFP lentivirus and subjected to flow cytometry analysis of EGFP expression as an indicator of lentivirus transduction efficiency. ( B ) Protein expression of Tie2 in vector control and Tie2 knockout HLMVECs induced by CRISPR-Cas9 was determined by immunoblotting. Overexpression of mouse Tie2 in Tie2 −/− HLMVECs was determined to assess the ability to rescue Tie2 expression after deletion. The uncropped full-length gels can be found in Supplementary Fig. S1 . ( C ) Quantification of Tie2 protein expression from 3 independent experiments. sgRNA Tie2-1 and sgRNA Tie2-2 are CRISPR-Cas9-mediated deletions of Tie-2 at two distinction domains of Tie2 (two different sgRNAs). HuTie2KO1 and HuTie2KO2 + mTie2 represent restoration of Tie-2 expression in cells having undergone Tie-2 deletion. Differences were calculated using one-way ANOVA. P values less than 0.05 are indicated in the graph. ( D ) T7E1 assay detecting mutation on HLMVECs edited by CRISPR-Cas9 with Tie2 sgRNAs as showing a series of bands. Wild-types cells with or without Cas9 or vector only show single bands (negative controls).

    Article Snippet: Rescue of Tie2 expression in HLMVECs following Tie-2 deletion Mouse Tie2 (mTie2) cDNA plasmids was purchased from Sino Biological Inc. (# MG51087-G).

    Techniques: CRISPR, Cell Culture, Flow Cytometry, Expressing, Transduction, Plasmid Preparation, Knock-Out, Over Expression, Mutagenesis

    Tie2 deletion by CRISPR-Cas9 in primary ECs increases endothelial permeability and mitigates recovery of permeability in response to thrombin challenge. ( A ) Basal TER and post-thrombin (1 U/ml) TER were studied in confluent control, Tie2-deleted HLMVECs and mTie2 overexpressing cells in which Tie2 had been deleted. Absolute TER values were reduced in both Tie2-deleted groups as compared to control ECs at basal condition. mTie2 overexpression successfully rescued the basal leakiness. ( B ) Quantification of TER values of wild-type (control), transduced cells (sgRNA Tie2-1, sgRNA Tie2-2) and rescued cells (HuTie2KO + mTie2) at basal (−1 h), thrombin-stimulated (0.5 h) and post-recovery (3 h) condition. Differences were calculated using two-way ANOVA. P values less than 0.05 are indicated in the graph. n = 3. ( C ) Serum-starved confluent control or Tie2-deleted HLMVECs were challenged by PBS or 1 U/ml of thrombin, and subjected for VE-cadherin immunostaining at the indicated time-points and analyzed by confocal microscopy. The marked disruption of VE-cadherin junctions seen in wild-type HLMVEC monolayer (control) at the 30 min post thrombin (white arrows) was reversed by 2 h; however, the defective VE-cadherin junctions were present in Tie2-deleted HLMVECs 2 h post-thrombin. White arrows are used to identify areas of adherens junction disruption where neighboring cells lack cell membrane localization of VE-cadherin. Results are representative of 3 independent experiments.

    Journal: Scientific Reports

    Article Title: Method for Dual Viral Vector Mediated CRISPR-Cas9 Gene Disruption in Primary Human Endothelial Cells

    doi: 10.1038/srep42127

    Figure Lengend Snippet: Tie2 deletion by CRISPR-Cas9 in primary ECs increases endothelial permeability and mitigates recovery of permeability in response to thrombin challenge. ( A ) Basal TER and post-thrombin (1 U/ml) TER were studied in confluent control, Tie2-deleted HLMVECs and mTie2 overexpressing cells in which Tie2 had been deleted. Absolute TER values were reduced in both Tie2-deleted groups as compared to control ECs at basal condition. mTie2 overexpression successfully rescued the basal leakiness. ( B ) Quantification of TER values of wild-type (control), transduced cells (sgRNA Tie2-1, sgRNA Tie2-2) and rescued cells (HuTie2KO + mTie2) at basal (−1 h), thrombin-stimulated (0.5 h) and post-recovery (3 h) condition. Differences were calculated using two-way ANOVA. P values less than 0.05 are indicated in the graph. n = 3. ( C ) Serum-starved confluent control or Tie2-deleted HLMVECs were challenged by PBS or 1 U/ml of thrombin, and subjected for VE-cadherin immunostaining at the indicated time-points and analyzed by confocal microscopy. The marked disruption of VE-cadherin junctions seen in wild-type HLMVEC monolayer (control) at the 30 min post thrombin (white arrows) was reversed by 2 h; however, the defective VE-cadherin junctions were present in Tie2-deleted HLMVECs 2 h post-thrombin. White arrows are used to identify areas of adherens junction disruption where neighboring cells lack cell membrane localization of VE-cadherin. Results are representative of 3 independent experiments.

    Article Snippet: Rescue of Tie2 expression in HLMVECs following Tie-2 deletion Mouse Tie2 (mTie2) cDNA plasmids was purchased from Sino Biological Inc. (# MG51087-G).

    Techniques: CRISPR, Permeability, Over Expression, Immunostaining, Confocal Microscopy

    Intravital Microscopy. Tie2 reporter mouse, with implanted dorsal skin chambers, were injected with Reb-TMR (20 mg/kg, tail vein I.V.). About 1 hour after injection, select sites in the vascularized region were imaged. The two sites above show Reb-TMR lining the endothelia of the blood vessels, overlaying Tie2.

    Journal: ACS chemical biology

    Article Title: Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand

    doi: 10.1021/acschembio.9b00724

    Figure Lengend Snippet: Intravital Microscopy. Tie2 reporter mouse, with implanted dorsal skin chambers, were injected with Reb-TMR (20 mg/kg, tail vein I.V.). About 1 hour after injection, select sites in the vascularized region were imaged. The two sites above show Reb-TMR lining the endothelia of the blood vessels, overlaying Tie2.

    Article Snippet: TIE2 plasmid was obtained from SinoBiological (HG10700-NY).

    Techniques: Intravital Microscopy, Injection

    Quantitative binding data and inhibition of Reb-TMR (a) Representative images of Reb-TMR in HUVEC cells in the presence (below) or absence (top) of unlabeled rebastinib (10 uM). (b) Quantification of Reb-TMR fluorescent intensity as a function of increasing concentration of unlabeled rebastinib. Reported is the mean single cell fluorescent intensity per well, N = 2 wells. Error bars correspond to S.D. (c) Biochemical fluorescent polarization assay of rebastinib-bodipy TMR (0.8 uM) on enzymatic domain of Tie2. Leftmost point corresponds to polarization of Reb-TMR in PBS, and right points correspond to polarization of Reb-TMR with Tie2, and in increasing concentrations of unlabeled rebastinib (0,0.1,1,10 uM). Reported is mean over N = 2 wells. Error bars correspond to S.D.

    Journal: ACS chemical biology

    Article Title: Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand

    doi: 10.1021/acschembio.9b00724

    Figure Lengend Snippet: Quantitative binding data and inhibition of Reb-TMR (a) Representative images of Reb-TMR in HUVEC cells in the presence (below) or absence (top) of unlabeled rebastinib (10 uM). (b) Quantification of Reb-TMR fluorescent intensity as a function of increasing concentration of unlabeled rebastinib. Reported is the mean single cell fluorescent intensity per well, N = 2 wells. Error bars correspond to S.D. (c) Biochemical fluorescent polarization assay of rebastinib-bodipy TMR (0.8 uM) on enzymatic domain of Tie2. Leftmost point corresponds to polarization of Reb-TMR in PBS, and right points correspond to polarization of Reb-TMR with Tie2, and in increasing concentrations of unlabeled rebastinib (0,0.1,1,10 uM). Reported is mean over N = 2 wells. Error bars correspond to S.D.

    Article Snippet: TIE2 plasmid was obtained from SinoBiological (HG10700-NY).

    Techniques: Binding Assay, Inhibition, Concentration Assay

    Co-localization (a) High resolution imaging of HUVECs. Treatment of HUVECs with Reb-TMR (100 nM) followed by a stain for Tie2 shows colocalization of the two markers in the cytoplasm (b) Correlation of Reb-TMR and Tie2 immunofluorescence signals (Pearson r 2 = 0.88)

    Journal: ACS chemical biology

    Article Title: Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand

    doi: 10.1021/acschembio.9b00724

    Figure Lengend Snippet: Co-localization (a) High resolution imaging of HUVECs. Treatment of HUVECs with Reb-TMR (100 nM) followed by a stain for Tie2 shows colocalization of the two markers in the cytoplasm (b) Correlation of Reb-TMR and Tie2 immunofluorescence signals (Pearson r 2 = 0.88)

    Article Snippet: TIE2 plasmid was obtained from SinoBiological (HG10700-NY).

    Techniques: Imaging, Staining, Immunofluorescence

    Modeling. Addition of a linker to the amide of rebastinib allows for coupling of a fluorophore to the small molecule. Based on a previously published structure of rebastinib in complex with Tie2 (PDB: 6MWE), we predicted this addition should not interfere with binding of rebastinib to Tie2.

    Journal: ACS chemical biology

    Article Title: Imaging of Tie2 with a fluorescently labeled small molecule affinity ligand

    doi: 10.1021/acschembio.9b00724

    Figure Lengend Snippet: Modeling. Addition of a linker to the amide of rebastinib allows for coupling of a fluorophore to the small molecule. Based on a previously published structure of rebastinib in complex with Tie2 (PDB: 6MWE), we predicted this addition should not interfere with binding of rebastinib to Tie2.

    Article Snippet: TIE2 plasmid was obtained from SinoBiological (HG10700-NY).

    Techniques: Binding Assay