Journal: bioRxiv

Article Title: Comparison of immunohistochemistry methods in embryonic chicken corneal tissue

doi: 10.64898/2026.03.30.715369

Figure Lengend Snippet: (A–C) Limbal region, showing TAP1 signal primarily associated with the stromal compartment, with marked differences in signal intensity and continuity across processing methods. (D–F) Central cornea, showing background or negative staining across all processing methods. (G–I) Kidney tissue, serving as a TAP1-positive control, showing robust TAP1 expression with clear cellular and subcellular definition in Wax and Wax AR sections and reduced structural resolution in cryo-embedded tissue. * marks one positive cell in stroma

Article Snippet: Slides were then incubated with monoclonal primary antibodies Rb P40 (Abcam AB203826, 1:200), Rb Cd68 (Abcam AB213363, 1:100), Rb Pax6 (Abcam AB195045, 1:500), Ms Pax6 (Abcam AB78545, 1:100), Ms CD11c (Abcam AB254183, 1:250), Ms Actin (DSHB AB_528068, 1:8.5), Ms Pax6-S (DSHB AB_528427, 1:12), and Ms TAP1 (DSHB AB_531780, 1:55).

Techniques: Negative Staining, Positive Control, Expressing

Journal: Nature

Article Title: Identification of essential genes for cancer immunotherapy

doi: 10.1038/nature23477

Figure Lengend Snippet: a–c, Kaplan-Meier survival plots of patient overall survival with the expression of antigen presentation genes B2M (a), TAP1 (b) and TAP2 (c) after ipilimumab immunotherapy. Patients were categorized into ‘High’ and ‘Low’ groups according to the highest and the lowest quartiles of each individual gene expression (RPKM). Reported P-values have been penalized by multiplying the unadjusted P-value by 3 to account for the comparison of the two extreme quartiles. Hazard ratio (HR) was calculated using Mantel-Haenszel test; with HR ranges: B2M (0.02–0.31), TAP1 (0.04–0.52) and TAP2 (0.12–1.07). Data is derived from 42 melanoma patients from the Van-Allen et al. cohort3. d, Schematic of the 2CT-CRISPR assay to identify essential genes for EFT. e, NY-ESO-1 antigen specific lysis of melanoma cells after 24 h of co-culture of ESO T cells with NY-ESO-1− SK23, NY-ESO-1+ SK23 and NY-ESO-1+ Mel624 cells (n = 3 biological replicates) at E:T ratio of 1. f, Survival of Mel624 cells modified through lentiviral CRISPR targeting of MHC class I antigen presentation/processing genes after introduction of ESO T cells. CRISPR-modified Mel624 cells were co-cultured with ESO T cells at E:T ratio of 0.5 for 12 h. Live cell survival (%) was calculated from control cells unexposed to T cell selection. Data is from 3 independent infection replicates. All values are mean ± s.e.m. ***P < 0.001 as determined by Student’s t-test.

Article Snippet: Gene expression was quantified using TaqMan RNA-to-Ct 1-Step Kit (Thermo Fisher) and Taqman assay probes (Invitrogen): Aplnr (Mm00442191_s1), Actb (Mm00607939_s1), APLN (Hs00936329), ACTB (Hs01060665_g1), IRF1 (Hs00971965_m1), IFI30 (Hs00173838_m1), TAP1 (Hs00388675_m1), TAP2 (Hs00241060_m1), TAPBP (Hs00917451_g1) and JAK1 (Hs01026983_m1).

Techniques: Expressing, Immunopeptidomics, Gene Expression, Comparison, Derivative Assay, CRISPR, Lysis, Co-Culture Assay, Modification, Cell Culture, Control, Selection, Infection

Journal: Cancer Research

Article Title: Parkin Deficiency Suppresses Antigen Presentation to Promote Tumor Immune Evasion and Immunotherapy Resistance

doi: 10.1158/0008-5472.CAN-22-2499

Figure Lengend Snippet: Parkin deficiency in human ccRCC is associated with poor clinical outcome, limited antigen presentation capabilities, and impacts immunotherapy efficacy. Parkin ( PRKN ) downregulation in patients with KIRC is significantly associated with overall survival and tumor stage. A, PRKN gene expression is significantly downregulated in patient tumor samples vs. matched controls ( N = 72 matches samples, P value = 3E−07 via paired Student t test; FPKMs mapped reads data from GDC HTSeq-FPKM pipeline was used). Dashed lines represent cutoffs used to bin patients with KIRC into low, mid, high PRKN gene expression levels. B, PRKN gene expression levels are significantly associated with overall survival ( N = 538 tumor samples, P < 0.0001 via log-rank test for trend). C, PRKN expression is significantly associated with overall survival in patients with stage 4 tumors (log-rank P < 0.007). D, mRNA expression levels of PRKN on HEK293, 786-O, CAKI-I, and A498 cells cultured overnight in growth media. E, mRNA and protein expression levels of A498 Parkin KO or EV cells. F, A498 Parkin KO or EV cells were stimulated with IFNγ (10 ng/mL) for 18 hours. Then, immunoblotting analysis was performed on Parkin, HLA-A, TAP1, and PSMB8. Data represent two to three independent experiments. Immunoblot data represent two to three independent experiments. G, IFNγ ELISA analysis was performed on donor-derived NY-ESO-1-specific T cells (5 × 10 4 ) cocultured in a 1:1 ratio overnight with A498 Parkin KO or EV cells. Tumor cells were prestimulated with IFNγ (10 ng/mL) or mock-treated for 18 hours before the assay. Data are represented as mean ± SD. ***, P < 0.001; unpaired, two-tailed t test.

Article Snippet: The primary antibodies for TAP1, PSMB8, β2-microglobulin (D8P1H), HSP90 (C45G5), β-actin (E4D9Z), Vinculin (VCL; E1E9V), Parkin, PTEN, AMPKa, phospho-AMPKa (Thr172; 40H9), Akt, phospho-Akt (Ser473; D9E), phospho-GSK-3β (Ser9, D85E12), and GSK-3β (D5C5Z) were purchased from Cell Signaling Technology; HLA-A was purchased from Thermo Fisher Scientific; and MHC-I (ER-HR52) was obtained from Santa Cruz Biotechnology.

Techniques: Immunopeptidomics, Gene Expression, Expressing, Cell Culture, Western Blot, Enzyme-linked Immunosorbent Assay, Derivative Assay, Two Tailed Test

Journal: Cancer Research

Article Title: Parkin Deficiency Suppresses Antigen Presentation to Promote Tumor Immune Evasion and Immunotherapy Resistance

doi: 10.1158/0008-5472.CAN-22-2499

Figure Lengend Snippet: Parkin regulates the MHC-I-associated tumor APM and fosters tumor progression. A and B, mRNA expression levels of Prkn , H2-k1 , Tap1 , Psmb8 , and B2m in RENCA cells stably transfected with sh Prkn _1 (sh#1), sh Prkn _3 (sh#3), and empty vector control (pLKO.1) lentiviral vectors. Data are represented as mean ± SD. ***, P < 0.001; unpaired, two-tailed t test. C, Protein expression analyses of Parkin, Tap1, Psmb8, and B2m (immunoblotting) and Parkin vs. MHC-I (intracellular staining, flow cytometry) of pLKO.1 controls, sh#1, and sh#3 RENCA cells. Data represent two to three independent experiments. D, IFNγ ELISPOT analysis was performed on T cells isolated from the spleens of pLKO.1 RENCA tumor-bearing mice at day 25 after challenge. T cells were cocultured overnight with stimulator Parkin-positive (pLKO.1) or -negative (sh#1, sh#3) RENCA cells (5:1 ratio). E, Parkin-positive (pLKO.1) or -negative (sh#1, sh#3) RENCA cells (10 6 ) were injected in the back of BALB/c mice and tumor growth was monitored. Data are represented as mean ± SEM. *, P < 0.05; ***, P < 0.001; two-way ANOVA.

Article Snippet: The primary antibodies for TAP1, PSMB8, β2-microglobulin (D8P1H), HSP90 (C45G5), β-actin (E4D9Z), Vinculin (VCL; E1E9V), Parkin, PTEN, AMPKa, phospho-AMPKa (Thr172; 40H9), Akt, phospho-Akt (Ser473; D9E), phospho-GSK-3β (Ser9, D85E12), and GSK-3β (D5C5Z) were purchased from Cell Signaling Technology; HLA-A was purchased from Thermo Fisher Scientific; and MHC-I (ER-HR52) was obtained from Santa Cruz Biotechnology.

Techniques: Expressing, Stable Transfection, Transfection, Plasmid Preparation, Control, Two Tailed Test, Western Blot, Staining, Flow Cytometry, Enzyme-linked Immunospot, Isolation, Injection

Journal: Cancer Research

Article Title: Parkin Deficiency Suppresses Antigen Presentation to Promote Tumor Immune Evasion and Immunotherapy Resistance

doi: 10.1158/0008-5472.CAN-22-2499

Figure Lengend Snippet: Parkin regulates cytosolic tumor antigen processing and presentation and facilitates effector CD8 + T-cell cancer immunity. A–C, Mouse melanoma B16-OVA Prkn knockout (KO, CRISPr/Cas9) or EV control cells were stimulated for 18 hours with IFNγ (10 ng/mL) or mock-stimulated before the analyses. A, mRNA expression levels of Prkn , H2-k1 , Psmb8 , and Tap1 in B16-OVA Parkin KO or EV cells. Data are represented as mean ± SD. ** P < 0.01; *** P < 0.001; unpaired, two-tailed t test. B, Protein expression analyses of Parkin, Tap1, and Psmb8 (immunoblotting) and SIINFEKL-bound to H-2Kb (MHCi-OVA; intracellular staining, flow cytometry) of B16-OVA KO and EV cells. Data represent two to three independent experiments. C, IFNγ ELISPOT analysis was performed on OT.1 T cells (10 5 ) cocultured overnight with B16-OVA KO and EV cells in a 5:1 ratio. D, B16-OVA Parkin KO or EV cells (10 6 ) were injected in the back of C57BL/6 mice and tumor growth was monitored. Five mice per group were treated with anti-CD8 blocking antibody (aCD8) or isotype (ISO) control. E, Percentage of CD45 − /MHC-OVA + cells present in B16-OVA Parkin KO or EV isotype-treated tumors analyzed by flow cytometry. F, SIINFEKL-specific CD8 + T-cell tumor infiltration present in B16-OVA Parkin KO or EV isotype-treated tumors. G, mRNA expression levels of IFNγ in B16-OVA Parkin KO or EV isotype-treated tumors. E–G, Data are represented as mean ± SEM. ns, not significant; *, P < 0.05; **, P < 0.01; unpaired, two-tailed t test. H, B16-OVA Parkin KO or EV cells (10 6 ) were injected in the back of C57BL/6-Tg(TcraTcrb)1100Mjb/J (OT.1) mice (5 per group) and tumor growth was monitored. I, Survival rate analysis (Kaplan–Meier, log-rank test) was performed by day 25 posttumor challenge, including five mice per group. D and H, Data are represented as mean ± SEM. ***, P < 0.001; two-way ANOVA.

Article Snippet: The primary antibodies for TAP1, PSMB8, β2-microglobulin (D8P1H), HSP90 (C45G5), β-actin (E4D9Z), Vinculin (VCL; E1E9V), Parkin, PTEN, AMPKa, phospho-AMPKa (Thr172; 40H9), Akt, phospho-Akt (Ser473; D9E), phospho-GSK-3β (Ser9, D85E12), and GSK-3β (D5C5Z) were purchased from Cell Signaling Technology; HLA-A was purchased from Thermo Fisher Scientific; and MHC-I (ER-HR52) was obtained from Santa Cruz Biotechnology.

Techniques: Knock-Out, CRISPR, Control, Expressing, Two Tailed Test, Western Blot, Staining, Flow Cytometry, Enzyme-linked Immunospot, Injection, Blocking Assay

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 1. Molecular model of the heterodimeric human TAP complex including SNP’s of TAP1 and TAP2. The structure of TAP1 including its cytosolic nucleotide binding domain (NBD1) and its six transmembrane regions forming the core transmembrane domain (TMD1) is depicted in green. The structure of the NBD2 and TMD2 of TAP2 is shown in purple. Non-synonymous SNPs in TAP1 evaluated in this study are shown in orange (left). G17R is not shown because it occurs in the N- terminal TMD not present in the model. The TAP2 SNPs included in this study are shown in yellow (right). (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Binding Assay

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 2. Confirmation of the knock-out phenotype of TAP1/2 KO MJS cells. (A) Lysates from MJS WT cells and TAP1/2 KO MJS cells stained for TAP1 and TAP2 by immunoblotting (IB) with specific antibodies. β-actin was used as a loading control. (B) Surface expression of MHC I molecules of TAP1/2 KO MJS cells (green), TAP1/2 KO MJS cells reconstituted with TAP1/2 (red), MJS WT cells (blue) and unstained MJS WT cells (orange) was assessed by flow cyto- metry. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Knock-Out, Staining, Western Blot, Control, Expressing

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 3. Expression and function of TAP1 and TAP2 variants introduced into TAP1/2 KO MJS cells. Expression of TAP1 variant-TAP2 reference pairs (A) and TAP2 variant-TAP1 reference pairs (B) in MJS cells was analyzed by immunoblotting (IB) of lysates with specific antibodies. TAP expression was compared to that of TAP WT cells; lysates of TAP KO cells served as negative control. β-actin was used as a loading control. (C and D) TAP-dependent peptide translocation in MJS cells transduced with the different variant-reference pairs, displayed as changes in mean fluorescence intensity (MFI), normalized to that of MJS WT cells. MJS WT cells incubated with ADP were used to verify that transport is ATP dependent. TAP1/2 KO cells transduced with an empty vector (EV) were used as a control. (E and F) Relative surface expression levels of MHC I molecules on MJS containing the different TAP variants compared to MJS WT, assessed by flow cytometry. MJS without antibody and TAP1/2 KO MJS were included as controls. Error bars indicate the SD, N = 3.

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Expressing, Variant Assay, Western Blot, Negative Control, Control, Translocation Assay, Transduction, Incubation, Plasmid Preparation, Cytometry

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 4. Inhibition of TAP function by the viral inhibitor US6. Expression of US6 in MJS containing the TAP1 variant-TAP2 reference pairs (A) and TAP2 variant-TAP1 reference pairs (B) was analyzed by immunoblotting (IB) of lysates with a mouse-anti-myc antibody. Lysates of TAP KO and untransduced WT cells served as controls. TfR was used as a loading control. (C and D) TAP-dependent peptide translocation in MJS cells transduced with the viral inhibitor US6 and different variant-reference pairs, displayed as changes in MFI, normalized to that of MJS WT cells. MJS WT cells incubated with ADP were used to verify that transport is ATP dependent. TAP1/ 2 KO cells transduced with the inhibitor US6 were used as a control. (E and F) Relative surface expression levels of MHC I molecules on MJS containing the different TAP variants and US6 compared to MJS WT cells, assessed by flow cytometry. MJS without antibody and TAP1/2 KO MJS cells + US6 were used as controls. Error bars indicate the SD, N = 3.

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Inhibition, Expressing, Variant Assay, Western Blot, Control, Translocation Assay, Transduction, Incubation, Cytometry

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 5. Inhibition of TAP function by the viral inhibitor BNLF2a. Expression of BNLF2a in MJS cells containing the TAP1 variant-TAP2 reference pairs (A) and TAP2 variant-TAP1 reference pairs (B) was analyzed by immunoblotting (IB) of lysates with a mouse-anti-myc antibody. Lysates of TAP KO cells served as negative control. β-actin was used as a loading control. (C and D) TAP-dependent peptide translocation in MJS cells transduced with the viral inhibitor BNLF2a and different variant- reference pairs, displayed as changes in MFI, normalized to that of MJS WT cells. MJS WT cells incubated with ADP were used to verify that transport is ATP dependent. TAP1/2 KO cells transduced with the inhibitor BNLF2a were used as a control. (E and F) Relative surface expression levels of MHC I molecules on MJS containing the different TAP variants and BNLF2a compared to MJS WT cells, assessed by flow cytometry. MJS without antibody and TAP1/2 KO MJS cells + BNLF2a were used as controls. Error bars indicate the SD, N = 3.

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Inhibition, Expressing, Variant Assay, Western Blot, Negative Control, Control, Translocation Assay, Transduction, Incubation, Cytometry

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 6. Inhibition of TAP function by the viral inhibitor ICP47. (A and B) TAP-dependent peptide translocation in MJS cells transduced with the viral inhibitor ICP47 and different variant-reference pairs, displayed as changes in MFI, normalized to that of MJS WT cells. MJS WT cells incubated with ADP were used to verify that transport is ATP dependent. TAP1/2 KO cells transduced with the inhibitor ICP47 were used as a control. (C and D) Relative surface expression levels of MHC I molecules on MJS containing the different TAP variants and ICP47 compared to MJS WT cells, assessed by flow cytometry. MJS without antibody and TAP1/2 KO MJS cells + ICP47 were used as controls. Error bars indicate the SD, N = 3.

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Inhibition, Translocation Assay, Transduction, Variant Assay, Incubation, Control, Expressing, Cytometry

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 7. Molecular model of the TAP1-TAP2-ICP47 complex. The viral inhibitor ICP47 (red) forms a helix-loop-helix structure and blocks TAP by obstructing the peptide translocation pathway with a helical hairpin. The SNPs S286F and A370V from TAP1 and A374T from TAP2 are located in close proximity to ICP47. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Translocation Assay

Journal: Molecular immunology

Article Title: The influence of TAP1 and TAP2 gene polymorphisms on TAP function and its inhibition by viral immune evasion proteins.

doi: 10.1016/j.molimm.2018.05.025

Figure Lengend Snippet: Fig. 8. Schematic representation of the interaction between the TAP complex and the viral inhibitors BNLF2a and US6. (A) Upon binding of the tail anchored transmembrane protein BNLF2a to TAP, peptide binding as well as ATP binding are inhibited. (B) In contrast to BNLF2a, the inhibitor US6 interferes with ATP binding to TAP1 while interacting with the ER-luminal loops of TAP1 and TAP2.

Article Snippet: The following primary and secondary antibodies were used for IB: mouse-anti-human TAP1 148.3 C-terminus mAb (1:200) (Plewnia et al., 2007), mouse-anti-human TAP2 435.4 mAb (1:200) (van Endert et al., 1994), mouse-anti-myc 9E10 mAb (1:1000), mouse-anti-actin mAb (Millipore MAB1501R, 1:10,000), mouse-anti-transferrin receptor mAb (Santa Cruz sc-7327, 1:1000), goat-anti-mouse conjugate-HRP pAb (Jackson #115-035-174, 1:5000) and goat-anti-rat-HRP (Jackson #112-035-175,1:5000).

Techniques: Binding Assay

Journal: Immunology

Article Title: Interferon-α promotes MHC I antigen presentation of islet β cells through STAT1-IRF7 pathway in type 1 diabetes.

doi: 10.1111/imm.13468

Figure Lengend Snippet: FIGURE 5 Differential gene expression in NOD mice pancreas after IFN-α treatment. Representative images (40×) of frozen sections of mice pancreas stained for Insulin, DAPI and (a) STAT1, (b) IRF7, (c) TAP1, (d) MHC I from NOD mice with or without IFN-α treatment

Article Snippet: Phospho- STAT1, STAT1, Phospho- STAT2, STAT2, TAP1 and β- actin antibodies were purchased from Cell Signaling Technology company, USA; IRF7 antibody was purchased from NOVUS company, USA; B2M, PSMB8 and NLRC5 antibodies were purchased from Abcam company, UK; PhosphoSTAT3, STAT3 and Phospho- STAT5 antibodies were purchased from Abclonal company, China; STAT5 and IRF9 antibodies were purchased from company, China.

Techniques: Gene Expression, Staining

Journal: Immunology

Article Title: Interferon-α promotes MHC I antigen presentation of islet β cells through STAT1-IRF7 pathway in type 1 diabetes.

doi: 10.1111/imm.13468

Figure Lengend Snippet: FIGURE 8 IFN-α induce β cells autoimmunity by promoting MHC I antigen presentation. In β cells, IFN-α binds to the IFNRs and lead to the nuclear translocation of STAT1 and IRF7, which in turn activates the STAT1-IRF7 axis to increase expression of antigen presenting molecules (TAP1, PSMB8 and MHC I). These actions create positive feedback through IRF7-STAT2 cascade amplifying signals and promote the proliferation of CD8+ T cells and insulitis. Figure was created with BioRender.com (Agreement number: TX23NA2XMH)

Article Snippet: Phospho- STAT1, STAT1, Phospho- STAT2, STAT2, TAP1 and β- actin antibodies were purchased from Cell Signaling Technology company, USA; IRF7 antibody was purchased from NOVUS company, USA; B2M, PSMB8 and NLRC5 antibodies were purchased from Abcam company, UK; PhosphoSTAT3, STAT3 and Phospho- STAT5 antibodies were purchased from Abclonal company, China; STAT5 and IRF9 antibodies were purchased from company, China.

Techniques: Immunopeptidomics, Translocation Assay, Expressing

Journal: Clinical Cancer Research

Article Title: Multidrug Resistance-Linked Gene Signature Predicts Overall Survival of Patients With Primary Ovarian Serous Carcinoma

doi: 10.1158/1078-0432.CCR-12-0056

Figure Lengend Snippet: MDR-linked gene signature that predicts overall survival

Article Snippet: Then the left out sample is classified as low or high risk depending on whether its log-hazard is higher than or lower than the threshold (see Materials and Methods section). table ft1 table-wrap mode="anchored" t5 caption a7 Genes TaqMan Assay ID p-value a % CV Support b Mean Expression in Low Risk Group Mean Expression in High Risk Group GPX3 Hs00173566_m1 0.0003 100 −0.47 1.16 APC Hs00181051_m1 0.0009 100 −0.15 −0.09 BAG3 Hs00188713_m1 0.0012 100 −1.35 −1.14 S100A10 Hs00237010_m1 0.0013 100 2.47 3.35 EGFR Hs00193306_m1 0.0023 98.75 −1.24 −0.62 ITGAE Hs00559580_m1 0.0038 98.75 −3.02 −4.64 MAPK3 Hs00385075_m1 0.0053 93.75 0.72 0.87 TAP1/ABCB2 Hs00388682_m1 0.0056 96.25 3.09 1.90 BNIP3 Hs00969291_m1 0.0063 90 2.05 2.53 MMP9 Hs00234579_m1 0.0074 86.25 0.43 −0.83 FASLG Hs00181225_m1 0.0085 66.25 −4.08 −5.49 Open in a separate window a The p-value is the correlation of the gene to overall survival based on the samples on which the Cox PH model is fitted. b Percent of times when the gene was used in the predictor for the leave-one-out cross-validation procedure.

Techniques: TaqMan Assay, Expressing

Journal: Clinical Cancer Research

Article Title: Multidrug Resistance-Linked Gene Signature Predicts Overall Survival of Patients With Primary Ovarian Serous Carcinoma

doi: 10.1158/1078-0432.CCR-12-0056

Figure Lengend Snippet: Genes included in the gene signature, their functions and association with ovarian cancer

Article Snippet: Then the left out sample is classified as low or high risk depending on whether its log-hazard is higher than or lower than the threshold (see Materials and Methods section). table ft1 table-wrap mode="anchored" t5 caption a7 Genes TaqMan Assay ID p-value a % CV Support b Mean Expression in Low Risk Group Mean Expression in High Risk Group GPX3 Hs00173566_m1 0.0003 100 −0.47 1.16 APC Hs00181051_m1 0.0009 100 −0.15 −0.09 BAG3 Hs00188713_m1 0.0012 100 −1.35 −1.14 S100A10 Hs00237010_m1 0.0013 100 2.47 3.35 EGFR Hs00193306_m1 0.0023 98.75 −1.24 −0.62 ITGAE Hs00559580_m1 0.0038 98.75 −3.02 −4.64 MAPK3 Hs00385075_m1 0.0053 93.75 0.72 0.87 TAP1/ABCB2 Hs00388682_m1 0.0056 96.25 3.09 1.90 BNIP3 Hs00969291_m1 0.0063 90 2.05 2.53 MMP9 Hs00234579_m1 0.0074 86.25 0.43 −0.83 FASLG Hs00181225_m1 0.0085 66.25 −4.08 −5.49 Open in a separate window a The p-value is the correlation of the gene to overall survival based on the samples on which the Cox PH model is fitted. b Percent of times when the gene was used in the predictor for the leave-one-out cross-validation procedure.

Techniques: Cell Differentiation, Membrane, Marker, Activation Assay, Transduction