rabbit anti ido Search Results


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Sino Biological ido ido1 r sino biological 11650 t58
Ido Ido1 R Sino Biological 11650 T58, 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
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Cusabio 3 dioxygenase 1
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GeneTex ido1 gt273 mouse antibody
Antibodies used in immunostaining.
Ido1 Gt273 Mouse Antibody, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Adipogen mb11 ag-27b-0009-c100
Fixation alters SH signals and tubulin conformations. a Recordings of SH signals before and after fixation with acetone (Ac, n = 16 cells from three independent experiments), methanol (Meth, n = 20 cells from three independent experiments) and paraformaldehyde (PFA, n = 19 cells from three independent experiments), which all lead to a loss of the SH signal while ethylene glycol bis succinimidyl succinate (EGS, n = 27 cells from three independent experiments) fixation preserves the SH signal intensity compared to the controls before fixation (CTRL; n = 94 cells from six independent experiments; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). b <t>MB11</t> staining and quantification for GTP-bound tubulin dimers after fixation shows lack of epitope recognition in aceton, methanol, and paraformaldehyde fixed cells, but positive staining in EGS fixed samples ( n = 9 cells from three independent experiments; *** p < 0.001 one-way ANOVA Bonferroni multiple comparison). c To control for immunohistochemical processing, staining with α-tubulin was performed simultaneously and shows positive staining after aceton, methanol, PFA, and EGS fixation. Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file
Mb11 Ag 27b 0009 C100, supplied by Adipogen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Washington Biotechnology Inc polyclonal anti ido antibody
Fixation alters SH signals and tubulin conformations. a Recordings of SH signals before and after fixation with acetone (Ac, n = 16 cells from three independent experiments), methanol (Meth, n = 20 cells from three independent experiments) and paraformaldehyde (PFA, n = 19 cells from three independent experiments), which all lead to a loss of the SH signal while ethylene glycol bis succinimidyl succinate (EGS, n = 27 cells from three independent experiments) fixation preserves the SH signal intensity compared to the controls before fixation (CTRL; n = 94 cells from six independent experiments; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). b <t>MB11</t> staining and quantification for GTP-bound tubulin dimers after fixation shows lack of epitope recognition in aceton, methanol, and paraformaldehyde fixed cells, but positive staining in EGS fixed samples ( n = 9 cells from three independent experiments; *** p < 0.001 one-way ANOVA Bonferroni multiple comparison). c To control for immunohistochemical processing, staining with α-tubulin was performed simultaneously and shows positive staining after aceton, methanol, PFA, and EGS fixation. Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file
Polyclonal Anti Ido Antibody, supplied by Washington Biotechnology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Incyte corporation anti-ido rabbit antiserum
Fixation alters SH signals and tubulin conformations. a Recordings of SH signals before and after fixation with acetone (Ac, n = 16 cells from three independent experiments), methanol (Meth, n = 20 cells from three independent experiments) and paraformaldehyde (PFA, n = 19 cells from three independent experiments), which all lead to a loss of the SH signal while ethylene glycol bis succinimidyl succinate (EGS, n = 27 cells from three independent experiments) fixation preserves the SH signal intensity compared to the controls before fixation (CTRL; n = 94 cells from six independent experiments; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). b <t>MB11</t> staining and quantification for GTP-bound tubulin dimers after fixation shows lack of epitope recognition in aceton, methanol, and paraformaldehyde fixed cells, but positive staining in EGS fixed samples ( n = 9 cells from three independent experiments; *** p < 0.001 one-way ANOVA Bonferroni multiple comparison). c To control for immunohistochemical processing, staining with α-tubulin was performed simultaneously and shows positive staining after aceton, methanol, PFA, and EGS fixation. Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file
Anti Ido Rabbit Antiserum, supplied by Incyte corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Abnova rabbit anti-ido1 monoclonal antibody mab
The relationship between <t> IDO1 </t> expression and clinicopathological characteristic in Lung cancer patients
Rabbit Anti Ido1 Monoclonal Antibody Mab, supplied by Abnova, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Enzo Biochem polyclonal rabbit anti-murine ido antibody
The relationship between <t> IDO1 </t> expression and clinicopathological characteristic in Lung cancer patients
Polyclonal Rabbit Anti Murine Ido Antibody, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Enzo Biochem rabbit anti-ido
The relationship between <t> IDO1 </t> expression and clinicopathological characteristic in Lung cancer patients
Rabbit Anti Ido, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Enzo Biochem ido-1 monoclonal antibody
a Immunostaining <t>IDO-1</t> and E-cadherin antibodies in human PDACs. IDO-1 expression patterns in normal pancreatic ducts and precursor lesions (panINs) and early invasive lesions (white arrowheads, ducts; the lower panel in the left panel, E-cadherin staining, and nuclear morphology in the boxed region). b IDO-1 expression in the neoplastic duct, invasive lesions, and metastatic lymph lesions of PDACs (the upper panel, the split channels of the boxed region; the lower left in the right panel, the magnification of the boxed region). c Comparing the IDO-1 staining intensity in the neoplastic cells in PDAC or invasive lesions (sample size, n > 15) with lymph metastatic neoplastic cells and normal/precursors ducts (sample size, n = 4). Data, mean ± SD. One-way ANOVA. ** P < 0.01. d Immunostaining IDO-1 and E-cadherin antibodies in human PDACs revealed IDO-1 is also exclusively upregulated in the cells with apical or basal extrusion (the lower panels, single channel of the boxed region). The 3D-rendered image revealed the morphology of basal extruding cells. e , f Significant fraction of IDO-1 + neoplastic cells in PDAC have discontinuous or uneven E-cadherin membrane staining. The circled area in the right and left panels (yellow arrowheads, IDO-1 high , and E-cadherin low neoplastic cells). The graph showed the counts of IDO-1 high and E-cadherin low cells and IDO-1 low and E-cadherin high cells in PDAC tissues.
Ido 1 Monoclonal Antibody, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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NewLink Genetics polyclonal rabbit anti-mouse ido-2 antibody
a Immunostaining <t>IDO-1</t> and E-cadherin antibodies in human PDACs. IDO-1 expression patterns in normal pancreatic ducts and precursor lesions (panINs) and early invasive lesions (white arrowheads, ducts; the lower panel in the left panel, E-cadherin staining, and nuclear morphology in the boxed region). b IDO-1 expression in the neoplastic duct, invasive lesions, and metastatic lymph lesions of PDACs (the upper panel, the split channels of the boxed region; the lower left in the right panel, the magnification of the boxed region). c Comparing the IDO-1 staining intensity in the neoplastic cells in PDAC or invasive lesions (sample size, n > 15) with lymph metastatic neoplastic cells and normal/precursors ducts (sample size, n = 4). Data, mean ± SD. One-way ANOVA. ** P < 0.01. d Immunostaining IDO-1 and E-cadherin antibodies in human PDACs revealed IDO-1 is also exclusively upregulated in the cells with apical or basal extrusion (the lower panels, single channel of the boxed region). The 3D-rendered image revealed the morphology of basal extruding cells. e , f Significant fraction of IDO-1 + neoplastic cells in PDAC have discontinuous or uneven E-cadherin membrane staining. The circled area in the right and left panels (yellow arrowheads, IDO-1 high , and E-cadherin low neoplastic cells). The graph showed the counts of IDO-1 high and E-cadherin low cells and IDO-1 low and E-cadherin high cells in PDAC tissues.
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Affinity Biosciences rabbit anti-ido1
a Immunostaining <t>IDO-1</t> and E-cadherin antibodies in human PDACs. IDO-1 expression patterns in normal pancreatic ducts and precursor lesions (panINs) and early invasive lesions (white arrowheads, ducts; the lower panel in the left panel, E-cadherin staining, and nuclear morphology in the boxed region). b IDO-1 expression in the neoplastic duct, invasive lesions, and metastatic lymph lesions of PDACs (the upper panel, the split channels of the boxed region; the lower left in the right panel, the magnification of the boxed region). c Comparing the IDO-1 staining intensity in the neoplastic cells in PDAC or invasive lesions (sample size, n > 15) with lymph metastatic neoplastic cells and normal/precursors ducts (sample size, n = 4). Data, mean ± SD. One-way ANOVA. ** P < 0.01. d Immunostaining IDO-1 and E-cadherin antibodies in human PDACs revealed IDO-1 is also exclusively upregulated in the cells with apical or basal extrusion (the lower panels, single channel of the boxed region). The 3D-rendered image revealed the morphology of basal extruding cells. e , f Significant fraction of IDO-1 + neoplastic cells in PDAC have discontinuous or uneven E-cadherin membrane staining. The circled area in the right and left panels (yellow arrowheads, IDO-1 high , and E-cadherin low neoplastic cells). The graph showed the counts of IDO-1 high and E-cadherin low cells and IDO-1 low and E-cadherin high cells in PDAC tissues.
Rabbit Anti Ido1, supplied by Affinity Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Antibodies used in immunostaining.

Journal: Frontiers in Immunology

Article Title: Colorectal Cancer-Associated Immune Exhaustion Involves T and B Lymphocytes and Conventional NK Cells and Correlates With a Shorter Overall Survival

doi: 10.3389/fimmu.2021.778329

Figure Lengend Snippet: Antibodies used in immunostaining.

Article Snippet: IDO1 , GT273 , Mouse , GTX634652 , Genetex, Irvine, CA, USA.

Techniques: Immunostaining

Fixation alters SH signals and tubulin conformations. a Recordings of SH signals before and after fixation with acetone (Ac, n = 16 cells from three independent experiments), methanol (Meth, n = 20 cells from three independent experiments) and paraformaldehyde (PFA, n = 19 cells from three independent experiments), which all lead to a loss of the SH signal while ethylene glycol bis succinimidyl succinate (EGS, n = 27 cells from three independent experiments) fixation preserves the SH signal intensity compared to the controls before fixation (CTRL; n = 94 cells from six independent experiments; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). b MB11 staining and quantification for GTP-bound tubulin dimers after fixation shows lack of epitope recognition in aceton, methanol, and paraformaldehyde fixed cells, but positive staining in EGS fixed samples ( n = 9 cells from three independent experiments; *** p < 0.001 one-way ANOVA Bonferroni multiple comparison). c To control for immunohistochemical processing, staining with α-tubulin was performed simultaneously and shows positive staining after aceton, methanol, PFA, and EGS fixation. Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file

Journal: Nature Communications

Article Title: Molecular understanding of label-free second harmonic imaging of microtubules

doi: 10.1038/s41467-019-11463-8

Figure Lengend Snippet: Fixation alters SH signals and tubulin conformations. a Recordings of SH signals before and after fixation with acetone (Ac, n = 16 cells from three independent experiments), methanol (Meth, n = 20 cells from three independent experiments) and paraformaldehyde (PFA, n = 19 cells from three independent experiments), which all lead to a loss of the SH signal while ethylene glycol bis succinimidyl succinate (EGS, n = 27 cells from three independent experiments) fixation preserves the SH signal intensity compared to the controls before fixation (CTRL; n = 94 cells from six independent experiments; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). b MB11 staining and quantification for GTP-bound tubulin dimers after fixation shows lack of epitope recognition in aceton, methanol, and paraformaldehyde fixed cells, but positive staining in EGS fixed samples ( n = 9 cells from three independent experiments; *** p < 0.001 one-way ANOVA Bonferroni multiple comparison). c To control for immunohistochemical processing, staining with α-tubulin was performed simultaneously and shows positive staining after aceton, methanol, PFA, and EGS fixation. Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file

Article Snippet: In brief, cells were treated with 0.05% Triton in GPEM buffer (3 min, 37 °C) before incubation with MB11 (1:250, cat. number AG-27B-0009-C100 Adipogen) diluted in GPEM buffer supplemented with 2% BSA (15 min, 37 °C).

Techniques: Comparison, Staining, Control, Immunohistochemical staining

SH signals originate from the GTP-bound tubulin dimer conformation. a SH signals positively correlate with MB11 (GTP-bound tubulin conformation) staining intensity ( n = 81 cells from three independent experiments; p < 0.001 Spearman r = 0.5642). b Increased SH signal intensities in untreated (DMSO) and taxol (10 nM, 4 h incubation)-treated hippocampal neurons ( n = 27 cells from three independent experiments *** p < 0.001 two-tailed Mann–Whitney test) and HEK293T ( n = 27 cells from three independent experiments; *** p < 0.001 Welch two-tailed t -test) cells. c SH signals were significantly increased upon addition of epothilone B (10 nM, 6 h) in neuronal cultures ( n = 27 cells from three independent experiments; ** p < 0.01 two-tailed Mann–Whitney test). d Schematic representation of how increased tubulin dimers in the GTP-bound conformation (yellow compared to blue GDP-bound tubulin conformation) could impact microtubule organization and SH signal intensity. The GTP-bound conformation leads to more rigid, less bendable microtubules, which in turn lead to a more parallel organization. e Because of the molecular alterations between GDP- and GTP-bound tubulin dimers, the dipolar hyperpolarisability tensor element β zzz (arrow) can be different, which directly affects SH signal intensities. Note that the arrows here represent the hyperpolarizability tensor element. f HRS shows a larger β zzz for GTP-bound tubulin dimers ( β zzz = 190 ± 30 × 10 −30 esu) compared to GDP-bound tubulin dimers ( β zzz = 100 ± 10 × 10 −30 esu), as calculated from the slope and intercept of the concentration dependency of the HRS peak amplitude. n = 10 measurements per concentration (mean ± standard deviation). Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file

Journal: Nature Communications

Article Title: Molecular understanding of label-free second harmonic imaging of microtubules

doi: 10.1038/s41467-019-11463-8

Figure Lengend Snippet: SH signals originate from the GTP-bound tubulin dimer conformation. a SH signals positively correlate with MB11 (GTP-bound tubulin conformation) staining intensity ( n = 81 cells from three independent experiments; p < 0.001 Spearman r = 0.5642). b Increased SH signal intensities in untreated (DMSO) and taxol (10 nM, 4 h incubation)-treated hippocampal neurons ( n = 27 cells from three independent experiments *** p < 0.001 two-tailed Mann–Whitney test) and HEK293T ( n = 27 cells from three independent experiments; *** p < 0.001 Welch two-tailed t -test) cells. c SH signals were significantly increased upon addition of epothilone B (10 nM, 6 h) in neuronal cultures ( n = 27 cells from three independent experiments; ** p < 0.01 two-tailed Mann–Whitney test). d Schematic representation of how increased tubulin dimers in the GTP-bound conformation (yellow compared to blue GDP-bound tubulin conformation) could impact microtubule organization and SH signal intensity. The GTP-bound conformation leads to more rigid, less bendable microtubules, which in turn lead to a more parallel organization. e Because of the molecular alterations between GDP- and GTP-bound tubulin dimers, the dipolar hyperpolarisability tensor element β zzz (arrow) can be different, which directly affects SH signal intensities. Note that the arrows here represent the hyperpolarizability tensor element. f HRS shows a larger β zzz for GTP-bound tubulin dimers ( β zzz = 190 ± 30 × 10 −30 esu) compared to GDP-bound tubulin dimers ( β zzz = 100 ± 10 × 10 −30 esu), as calculated from the slope and intercept of the concentration dependency of the HRS peak amplitude. n = 10 measurements per concentration (mean ± standard deviation). Neuronal cultures were imaged at 7 DIV. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file

Article Snippet: In brief, cells were treated with 0.05% Triton in GPEM buffer (3 min, 37 °C) before incubation with MB11 (1:250, cat. number AG-27B-0009-C100 Adipogen) diluted in GPEM buffer supplemented with 2% BSA (15 min, 37 °C).

Techniques: Staining, Incubation, Two Tailed Test, MANN-WHITNEY, Concentration Assay, Standard Deviation

Biomedical applications for SH imaging of microtubules. a SH recordings of primary neuronal cultures from the substantia nigra treated with DMSO as control (CTRL), rotenone (Rt 100 nM, 4 h) or a combination of rotenone (100 nM, 4 h) and taxol (100 nM, 4 h). The significant reduction in the SH signal upon incubation with rotenone (arrowheads) was no longer detected in neurons treated with both rotenone and taxol to counteract the destabilizing effect ( n = 27 biologically independent cells; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). Neuronal cultures were imaged at 7 DIV. b SH signals from hippocampal neuronal cultures prepared from wild-type (TAU +/+ ), heterozygous (TAU +/− ) and TAU knock-out (TAU −/− ) mice. The SH signal intensity is significantly lower in TAU-deficient neurons compared to control and heterozygous cells ( n = 27 cells from three independent experiments; ** p < 0.01 *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). Neuronal cultures were imaged at 7 DIV. c Hippocampal neurons were cultured for 4, 7, or 10 days in vitro (DIV) before SH recordings and MB11 staining to localize GTP-tubulin dimer conformations. The SH signal and MB11 staining intensity was plotted over the entire length of the fiber to detect regional differences along the fiber during neuronal maturation in vitro. At early stages of development (4 DIV), both the SH and MB11 signal intensity were mainly localized at the proximal region of the processes (arrowhead) while later stages (7, 10 DIV) show increased signal intensity at the distal end (arrow) of the fiber ( n = 27 cells from three independent experiments; *** p < 0.001 two-way ANOVA Bonferroni post-hoc test). d SHG recordings in acute brain slices treated with taxol (10 µM, 4 h; n = 36 fibers from three independent experiments), epothilone B (100 nM, 4 h; n = 31 fibers from three independent experiments) or DMSO ( n = 36 fibers from three independent experiments) as control show increased SH signal intensities in both taxol (*** p < 0.001, one-way ANOVA Bonferroni multiple comparison) and epothilone B (** p < 0.01, one-way ANOVA Bonferroni multiple comparison) treated slices. SP: stratum pyramidale, SR: stratum radiatum. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file

Journal: Nature Communications

Article Title: Molecular understanding of label-free second harmonic imaging of microtubules

doi: 10.1038/s41467-019-11463-8

Figure Lengend Snippet: Biomedical applications for SH imaging of microtubules. a SH recordings of primary neuronal cultures from the substantia nigra treated with DMSO as control (CTRL), rotenone (Rt 100 nM, 4 h) or a combination of rotenone (100 nM, 4 h) and taxol (100 nM, 4 h). The significant reduction in the SH signal upon incubation with rotenone (arrowheads) was no longer detected in neurons treated with both rotenone and taxol to counteract the destabilizing effect ( n = 27 biologically independent cells; *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). Neuronal cultures were imaged at 7 DIV. b SH signals from hippocampal neuronal cultures prepared from wild-type (TAU +/+ ), heterozygous (TAU +/− ) and TAU knock-out (TAU −/− ) mice. The SH signal intensity is significantly lower in TAU-deficient neurons compared to control and heterozygous cells ( n = 27 cells from three independent experiments; ** p < 0.01 *** p < 0.001 one-way ANOVA Dunn’s multiple comparison test). Neuronal cultures were imaged at 7 DIV. c Hippocampal neurons were cultured for 4, 7, or 10 days in vitro (DIV) before SH recordings and MB11 staining to localize GTP-tubulin dimer conformations. The SH signal and MB11 staining intensity was plotted over the entire length of the fiber to detect regional differences along the fiber during neuronal maturation in vitro. At early stages of development (4 DIV), both the SH and MB11 signal intensity were mainly localized at the proximal region of the processes (arrowhead) while later stages (7, 10 DIV) show increased signal intensity at the distal end (arrow) of the fiber ( n = 27 cells from three independent experiments; *** p < 0.001 two-way ANOVA Bonferroni post-hoc test). d SHG recordings in acute brain slices treated with taxol (10 µM, 4 h; n = 36 fibers from three independent experiments), epothilone B (100 nM, 4 h; n = 31 fibers from three independent experiments) or DMSO ( n = 36 fibers from three independent experiments) as control show increased SH signal intensities in both taxol (*** p < 0.001, one-way ANOVA Bonferroni multiple comparison) and epothilone B (** p < 0.01, one-way ANOVA Bonferroni multiple comparison) treated slices. SP: stratum pyramidale, SR: stratum radiatum. Bar plots presented as means ± standard error of the mean. All source data are provided as a Source Data file

Article Snippet: In brief, cells were treated with 0.05% Triton in GPEM buffer (3 min, 37 °C) before incubation with MB11 (1:250, cat. number AG-27B-0009-C100 Adipogen) diluted in GPEM buffer supplemented with 2% BSA (15 min, 37 °C).

Techniques: Imaging, Control, Incubation, Comparison, Knock-Out, Cell Culture, In Vitro, Staining

The relationship between  IDO1  expression and clinicopathological characteristic in Lung cancer patients

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: The relationship between IDO1 expression and clinicopathological characteristic in Lung cancer patients

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Expressing

(A) IDO1 expression of was determined by way of qRT-PCR in 64 paired human lung cancer and their corresponding nontumorous samples (NT) and normalized against an endogenous U6 RNA control. (B) IDO1expression in different clinical stages of lung cancer. Patients were staged in accordance with the 8th Edition of the TNM staging for lung cancer of UICC. (C) up-regulation of IDO1 in lung cancer was associated with lymph node-metastasis; patients were classified into lymph node-metastasis negative group (LN-negative) and positive group (LN-positive).

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: (A) IDO1 expression of was determined by way of qRT-PCR in 64 paired human lung cancer and their corresponding nontumorous samples (NT) and normalized against an endogenous U6 RNA control. (B) IDO1expression in different clinical stages of lung cancer. Patients were staged in accordance with the 8th Edition of the TNM staging for lung cancer of UICC. (C) up-regulation of IDO1 in lung cancer was associated with lymph node-metastasis; patients were classified into lymph node-metastasis negative group (LN-negative) and positive group (LN-positive).

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Expressing, Quantitative RT-PCR, Control

(A) The expression levels of IDO1 were determined by qRT-PCR in lung cancer cell lines. U6 RNA served as an internal control. (B) And (C) Successful over-expression of IDO1 was confirmed by qRT-PCR after infection with IDO1-expressing lentivirus or vector control lentivirus. The values of IDO1 expression were calculated as fold change relative to the vector control.

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: (A) The expression levels of IDO1 were determined by qRT-PCR in lung cancer cell lines. U6 RNA served as an internal control. (B) And (C) Successful over-expression of IDO1 was confirmed by qRT-PCR after infection with IDO1-expressing lentivirus or vector control lentivirus. The values of IDO1 expression were calculated as fold change relative to the vector control.

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Expressing, Quantitative RT-PCR, Control, Over Expression, Infection, Plasmid Preparation

Overexpression of IDO1 significantly enhanced abilities of cell migration (A) and invasion (B) in NCI-H292 and HCC827 Lung cancer cell after infection with IDO1-expressing or vector lentivirus.

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: Overexpression of IDO1 significantly enhanced abilities of cell migration (A) and invasion (B) in NCI-H292 and HCC827 Lung cancer cell after infection with IDO1-expressing or vector lentivirus.

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Over Expression, Migration, Infection, Expressing, Plasmid Preparation

Downregulation of IDO1 significantly suppressed cell migration and invasion in NCI-H1299 Lung cancer cell

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: Downregulation of IDO1 significantly suppressed cell migration and invasion in NCI-H1299 Lung cancer cell

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Migration

(A) The distribution of p53 protein expression in lung cancer and corresponding nontumorous tissue (B) Correlation between p53 expression and IDO1 levels in the 64 lung cancer tissue samples. The expression levels of p53 were classified into low (scores of 0 and 1) and high groups (scores of 2 and 3) according to the scores of p53 immunohistochemical staining.

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: (A) The distribution of p53 protein expression in lung cancer and corresponding nontumorous tissue (B) Correlation between p53 expression and IDO1 levels in the 64 lung cancer tissue samples. The expression levels of p53 were classified into low (scores of 0 and 1) and high groups (scores of 2 and 3) according to the scores of p53 immunohistochemical staining.

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Expressing, Immunohistochemical staining, Staining

(A) and (B) silencing of IDO 1 was confirmed by Western blot in NCI-H292 and HCC827 cells after transfection with specific si-IDO1. β-Actin served as an internal control. (C) and (D) migration and invasion assays were carried out in NCI-H292 and HCC827 cells after transfection with negative control (NC) or si-IDO1.

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: (A) and (B) silencing of IDO 1 was confirmed by Western blot in NCI-H292 and HCC827 cells after transfection with specific si-IDO1. β-Actin served as an internal control. (C) and (D) migration and invasion assays were carried out in NCI-H292 and HCC827 cells after transfection with negative control (NC) or si-IDO1.

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Western Blot, Transfection, Control, Migration, Negative Control

(A) Western blot analysis was used to detect the IDO1 expression in NCI-H1299 cells after transfection with si-p53, si-IDO1 or NC. β-Actin served as an internal control. (B) NCI-H1299 cells after transfection with si-p53, si-IDO1 or NC were subjected to migration and invasion assays.

Journal: Oncotarget

Article Title: P53 prevent tumor invasion and metastasis by down-regulating IDO in lung cancer

doi: 10.18632/oncotarget.17408

Figure Lengend Snippet: (A) Western blot analysis was used to detect the IDO1 expression in NCI-H1299 cells after transfection with si-p53, si-IDO1 or NC. β-Actin served as an internal control. (B) NCI-H1299 cells after transfection with si-p53, si-IDO1 or NC were subjected to migration and invasion assays.

Article Snippet: After blocking in 5% nonfat milk, the membranes were incubated with the following primary antibodies: rabbit anti-IDO1 monoclonal antibody (mAb; 1:100; Abnova), mouse anti-β-actin mAb (1:10,000; Sigma) [ ].

Techniques: Western Blot, Expressing, Transfection, Control, Migration

a Immunostaining IDO-1 and E-cadherin antibodies in human PDACs. IDO-1 expression patterns in normal pancreatic ducts and precursor lesions (panINs) and early invasive lesions (white arrowheads, ducts; the lower panel in the left panel, E-cadherin staining, and nuclear morphology in the boxed region). b IDO-1 expression in the neoplastic duct, invasive lesions, and metastatic lymph lesions of PDACs (the upper panel, the split channels of the boxed region; the lower left in the right panel, the magnification of the boxed region). c Comparing the IDO-1 staining intensity in the neoplastic cells in PDAC or invasive lesions (sample size, n > 15) with lymph metastatic neoplastic cells and normal/precursors ducts (sample size, n = 4). Data, mean ± SD. One-way ANOVA. ** P < 0.01. d Immunostaining IDO-1 and E-cadherin antibodies in human PDACs revealed IDO-1 is also exclusively upregulated in the cells with apical or basal extrusion (the lower panels, single channel of the boxed region). The 3D-rendered image revealed the morphology of basal extruding cells. e , f Significant fraction of IDO-1 + neoplastic cells in PDAC have discontinuous or uneven E-cadherin membrane staining. The circled area in the right and left panels (yellow arrowheads, IDO-1 high , and E-cadherin low neoplastic cells). The graph showed the counts of IDO-1 high and E-cadherin low cells and IDO-1 low and E-cadherin high cells in PDAC tissues.

Journal: Acta Pharmacologica Sinica

Article Title: IDO-1 inhibitor INCB24360 elicits distant metastasis of basal extruded cancer cells in pancreatic ductal adenocarcinoma

doi: 10.1038/s41401-022-01035-w

Figure Lengend Snippet: a Immunostaining IDO-1 and E-cadherin antibodies in human PDACs. IDO-1 expression patterns in normal pancreatic ducts and precursor lesions (panINs) and early invasive lesions (white arrowheads, ducts; the lower panel in the left panel, E-cadherin staining, and nuclear morphology in the boxed region). b IDO-1 expression in the neoplastic duct, invasive lesions, and metastatic lymph lesions of PDACs (the upper panel, the split channels of the boxed region; the lower left in the right panel, the magnification of the boxed region). c Comparing the IDO-1 staining intensity in the neoplastic cells in PDAC or invasive lesions (sample size, n > 15) with lymph metastatic neoplastic cells and normal/precursors ducts (sample size, n = 4). Data, mean ± SD. One-way ANOVA. ** P < 0.01. d Immunostaining IDO-1 and E-cadherin antibodies in human PDACs revealed IDO-1 is also exclusively upregulated in the cells with apical or basal extrusion (the lower panels, single channel of the boxed region). The 3D-rendered image revealed the morphology of basal extruding cells. e , f Significant fraction of IDO-1 + neoplastic cells in PDAC have discontinuous or uneven E-cadherin membrane staining. The circled area in the right and left panels (yellow arrowheads, IDO-1 high , and E-cadherin low neoplastic cells). The graph showed the counts of IDO-1 high and E-cadherin low cells and IDO-1 low and E-cadherin high cells in PDAC tissues.

Article Snippet: Following antibodies were used for immunostaining or immunoblotting: IDO-1 (Cell Signaling Technology, D5J4E TM , rabbit, mAb #86630, 1:1000), CD45RA (BD Pharmingen, Clone: L48, 1:200), Foxp3 (Abcam, ab20034, 1:200), human VEGFR2/KDR/Flk-1 antibody (R&D, AF357, 1:200), E-Cadherin antibody (R&D, AF748, 1:100), CD11b antibody (Abcam, ab34216, 1:10000), CD8 antibody (Abcam, ab4505, 1:1000), CD11b antibody (Abcam, ab133357, 1:10000), purified mouse anti-human CD16 antibody (BD Pharmingen, Clone GO22, 1:200), anti-glucose transporter GLUT1 antibody (Abcam, ab115730, 1:1000), purified mouse anti-human CD3 antibody (BD Pharmingen, Clone SP34-2, 556648, 1:500), recombinant anti-Cytokeratin 19 antibody (Abcam, EP1580Y, 1:1000), 6-diamidino-2-phenylindole (DAPI, Sigma, D9542, 1:1000), IDO monoclonal antibody (Sigma, Clone mIDO-48, 1:500), IDO-1 monoclonal antibody (Enzo Life Sciences, Clone 2E2, 1:200), Vimentin antibody (Thermo Fisher Scientific, MA5-11883, 1:1000), Ki67 (EPR3610, Abcam, 1:1000), E-cadherin (Abcam, Ab1416, 1:500).

Techniques: Immunostaining, Expressing, Staining

a CK-19, IDO-1, and vimentin antibodies immunostaining showed that IDO-1 + and vimentin + cells in the neoplastic cells of PDAC that localized on the basal domain of ducts expressed a lower level of CK-19 (white arrows, basal extruding cells with EMT). Scale bar, 20 µm. Student t test. ** P < 0.001. Data, mean ± SEM. b E-cadherin, IDO-1, and vimentin antibodies immunostaining showed that vimentin antibodies stained a few IDO-1 + and E-cadherin + cells in PDAC tissues. Student t test. * P < 0.05, ** P < 0.01. Data, mean ± SEM. c 1 ng/mL Abraxane and 5 ng/mL gemcitabine-treated KPIC cells for 12 h were stained by CK-19, E-cadherin, and vimentin antibodies. The results CK-19 immunostaining intensity in cells with higher vimentin levels and lower vimentin levels showed that KPIC cells with higher levels of vimentin also expressed higher levels of CK-19 and vice versa. Student’s t test. ** P < 0.01. Data, mean ± SEM. d 5 ng/mL and 10 ng/mL gemcitabine-treated KPIC cells with over 80% confluence in dishes were performed CK-19, vimentin, and TUNEL staining. The measurement of staining intensity showed that TUNEL + cells with intact cellular structure expressed higher levels of CK-19 compared to TUNEL - KPIC cells. Data, mean ± SD. t test, ** P < 0.01.

Journal: Acta Pharmacologica Sinica

Article Title: IDO-1 inhibitor INCB24360 elicits distant metastasis of basal extruded cancer cells in pancreatic ductal adenocarcinoma

doi: 10.1038/s41401-022-01035-w

Figure Lengend Snippet: a CK-19, IDO-1, and vimentin antibodies immunostaining showed that IDO-1 + and vimentin + cells in the neoplastic cells of PDAC that localized on the basal domain of ducts expressed a lower level of CK-19 (white arrows, basal extruding cells with EMT). Scale bar, 20 µm. Student t test. ** P < 0.001. Data, mean ± SEM. b E-cadherin, IDO-1, and vimentin antibodies immunostaining showed that vimentin antibodies stained a few IDO-1 + and E-cadherin + cells in PDAC tissues. Student t test. * P < 0.05, ** P < 0.01. Data, mean ± SEM. c 1 ng/mL Abraxane and 5 ng/mL gemcitabine-treated KPIC cells for 12 h were stained by CK-19, E-cadherin, and vimentin antibodies. The results CK-19 immunostaining intensity in cells with higher vimentin levels and lower vimentin levels showed that KPIC cells with higher levels of vimentin also expressed higher levels of CK-19 and vice versa. Student’s t test. ** P < 0.01. Data, mean ± SEM. d 5 ng/mL and 10 ng/mL gemcitabine-treated KPIC cells with over 80% confluence in dishes were performed CK-19, vimentin, and TUNEL staining. The measurement of staining intensity showed that TUNEL + cells with intact cellular structure expressed higher levels of CK-19 compared to TUNEL - KPIC cells. Data, mean ± SD. t test, ** P < 0.01.

Article Snippet: Following antibodies were used for immunostaining or immunoblotting: IDO-1 (Cell Signaling Technology, D5J4E TM , rabbit, mAb #86630, 1:1000), CD45RA (BD Pharmingen, Clone: L48, 1:200), Foxp3 (Abcam, ab20034, 1:200), human VEGFR2/KDR/Flk-1 antibody (R&D, AF357, 1:200), E-Cadherin antibody (R&D, AF748, 1:100), CD11b antibody (Abcam, ab34216, 1:10000), CD8 antibody (Abcam, ab4505, 1:1000), CD11b antibody (Abcam, ab133357, 1:10000), purified mouse anti-human CD16 antibody (BD Pharmingen, Clone GO22, 1:200), anti-glucose transporter GLUT1 antibody (Abcam, ab115730, 1:1000), purified mouse anti-human CD3 antibody (BD Pharmingen, Clone SP34-2, 556648, 1:500), recombinant anti-Cytokeratin 19 antibody (Abcam, EP1580Y, 1:1000), 6-diamidino-2-phenylindole (DAPI, Sigma, D9542, 1:1000), IDO monoclonal antibody (Sigma, Clone mIDO-48, 1:500), IDO-1 monoclonal antibody (Enzo Life Sciences, Clone 2E2, 1:200), Vimentin antibody (Thermo Fisher Scientific, MA5-11883, 1:1000), Ki67 (EPR3610, Abcam, 1:1000), E-cadherin (Abcam, Ab1416, 1:500).

Techniques: Immunostaining, Staining, TUNEL Assay

a The typical morphology of KPIC PDAC organoids taken by DIC microscopy and E-cadherin, CK-19, and vimentin antibodies co-immunostaining or Glut-1 and IDO-1 antibodies co-immunostaining at day 7. The spliced images in the middle panel from the boxed region showed that the PDAC KPIC organoids did not express vimentin. b–d Treating KPIC PDAC organoids with 0, 10, and 20 ng/mL IFN-γ for 24 h increases apical extrusion of IDO-1 + KPIC cells ( b ). IDO-1 expression levels in KPIC 2D culture after treatment with 0, 10, and 20 ng/mL IFN-γ and 20 µM 1-MT for 24 h ( c , d ). The intensity of the IDO-1 signal in each cell was measured by Imaris 9.7. One-way ANOVA, ** P < 0.01. e Treating KPIC PDAC organoids with 0, 1, 10, and 20 ng/mL IFN-γ for 24 h and 48 h increased the distorting of ductal structure. Counting the ratio of ductal shape changes at 24 h and 48 h (replicates, n = 5; black arrowheads, the protruding basal cells).

Journal: Acta Pharmacologica Sinica

Article Title: IDO-1 inhibitor INCB24360 elicits distant metastasis of basal extruded cancer cells in pancreatic ductal adenocarcinoma

doi: 10.1038/s41401-022-01035-w

Figure Lengend Snippet: a The typical morphology of KPIC PDAC organoids taken by DIC microscopy and E-cadherin, CK-19, and vimentin antibodies co-immunostaining or Glut-1 and IDO-1 antibodies co-immunostaining at day 7. The spliced images in the middle panel from the boxed region showed that the PDAC KPIC organoids did not express vimentin. b–d Treating KPIC PDAC organoids with 0, 10, and 20 ng/mL IFN-γ for 24 h increases apical extrusion of IDO-1 + KPIC cells ( b ). IDO-1 expression levels in KPIC 2D culture after treatment with 0, 10, and 20 ng/mL IFN-γ and 20 µM 1-MT for 24 h ( c , d ). The intensity of the IDO-1 signal in each cell was measured by Imaris 9.7. One-way ANOVA, ** P < 0.01. e Treating KPIC PDAC organoids with 0, 1, 10, and 20 ng/mL IFN-γ for 24 h and 48 h increased the distorting of ductal structure. Counting the ratio of ductal shape changes at 24 h and 48 h (replicates, n = 5; black arrowheads, the protruding basal cells).

Article Snippet: Following antibodies were used for immunostaining or immunoblotting: IDO-1 (Cell Signaling Technology, D5J4E TM , rabbit, mAb #86630, 1:1000), CD45RA (BD Pharmingen, Clone: L48, 1:200), Foxp3 (Abcam, ab20034, 1:200), human VEGFR2/KDR/Flk-1 antibody (R&D, AF357, 1:200), E-Cadherin antibody (R&D, AF748, 1:100), CD11b antibody (Abcam, ab34216, 1:10000), CD8 antibody (Abcam, ab4505, 1:1000), CD11b antibody (Abcam, ab133357, 1:10000), purified mouse anti-human CD16 antibody (BD Pharmingen, Clone GO22, 1:200), anti-glucose transporter GLUT1 antibody (Abcam, ab115730, 1:1000), purified mouse anti-human CD3 antibody (BD Pharmingen, Clone SP34-2, 556648, 1:500), recombinant anti-Cytokeratin 19 antibody (Abcam, EP1580Y, 1:1000), 6-diamidino-2-phenylindole (DAPI, Sigma, D9542, 1:1000), IDO monoclonal antibody (Sigma, Clone mIDO-48, 1:500), IDO-1 monoclonal antibody (Enzo Life Sciences, Clone 2E2, 1:200), Vimentin antibody (Thermo Fisher Scientific, MA5-11883, 1:1000), Ki67 (EPR3610, Abcam, 1:1000), E-cadherin (Abcam, Ab1416, 1:500).

Techniques: Microscopy, Immunostaining, Expressing

a Testing IDO-1 expression in KPIC and KPIC Ido-1 KO cells. b Representative images of Ki67 antibody immunostaining and count of Ki67 + cells in KPIC and KPIC Ido-1 KO cells. Data, mean ± SD. t test, ** P < 0.01. c Representative images of dextran uptake in KPIC and KPIC Ido-1 KO cells after starvation and count of dextran vesicles in SIM Z-stacked images. Data, mean ± SD. t test, ** P < 0.01. d , e Comparing the growth patterns and speeds of KPIC Ido-1 KO PDAC organoids with KPIC organoids. Data, CI 95%. Two-way ANOVA. f KPIC Ido-1 KO organoids did not form a subcutaneous tumor in C57/B6 mice after transplantation for 4 weeks ( n = 7; white circled region, subcutaneous tumor of KPIC organoids). LS-MS data of KPIC and KPIC Ido-1 KO cells showed that CD86 ( g ), CD276 ( h ), H2-K1 ( i ), CD74 ( j ), and H2-D1 ( k ) significantly changed after Ido-1 knockout. Data, mean ± SD. t test; ** P < 0.01. Repeats, 3 times.

Journal: Acta Pharmacologica Sinica

Article Title: IDO-1 inhibitor INCB24360 elicits distant metastasis of basal extruded cancer cells in pancreatic ductal adenocarcinoma

doi: 10.1038/s41401-022-01035-w

Figure Lengend Snippet: a Testing IDO-1 expression in KPIC and KPIC Ido-1 KO cells. b Representative images of Ki67 antibody immunostaining and count of Ki67 + cells in KPIC and KPIC Ido-1 KO cells. Data, mean ± SD. t test, ** P < 0.01. c Representative images of dextran uptake in KPIC and KPIC Ido-1 KO cells after starvation and count of dextran vesicles in SIM Z-stacked images. Data, mean ± SD. t test, ** P < 0.01. d , e Comparing the growth patterns and speeds of KPIC Ido-1 KO PDAC organoids with KPIC organoids. Data, CI 95%. Two-way ANOVA. f KPIC Ido-1 KO organoids did not form a subcutaneous tumor in C57/B6 mice after transplantation for 4 weeks ( n = 7; white circled region, subcutaneous tumor of KPIC organoids). LS-MS data of KPIC and KPIC Ido-1 KO cells showed that CD86 ( g ), CD276 ( h ), H2-K1 ( i ), CD74 ( j ), and H2-D1 ( k ) significantly changed after Ido-1 knockout. Data, mean ± SD. t test; ** P < 0.01. Repeats, 3 times.

Article Snippet: Following antibodies were used for immunostaining or immunoblotting: IDO-1 (Cell Signaling Technology, D5J4E TM , rabbit, mAb #86630, 1:1000), CD45RA (BD Pharmingen, Clone: L48, 1:200), Foxp3 (Abcam, ab20034, 1:200), human VEGFR2/KDR/Flk-1 antibody (R&D, AF357, 1:200), E-Cadherin antibody (R&D, AF748, 1:100), CD11b antibody (Abcam, ab34216, 1:10000), CD8 antibody (Abcam, ab4505, 1:1000), CD11b antibody (Abcam, ab133357, 1:10000), purified mouse anti-human CD16 antibody (BD Pharmingen, Clone GO22, 1:200), anti-glucose transporter GLUT1 antibody (Abcam, ab115730, 1:1000), purified mouse anti-human CD3 antibody (BD Pharmingen, Clone SP34-2, 556648, 1:500), recombinant anti-Cytokeratin 19 antibody (Abcam, EP1580Y, 1:1000), 6-diamidino-2-phenylindole (DAPI, Sigma, D9542, 1:1000), IDO monoclonal antibody (Sigma, Clone mIDO-48, 1:500), IDO-1 monoclonal antibody (Enzo Life Sciences, Clone 2E2, 1:200), Vimentin antibody (Thermo Fisher Scientific, MA5-11883, 1:1000), Ki67 (EPR3610, Abcam, 1:1000), E-cadherin (Abcam, Ab1416, 1:500).

Techniques: Expressing, Immunostaining, Transplantation Assay, Knock-Out