Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: Intrathrombotic expressions of HSP27 and HSP70 in mice. ( a and b ) Intrathrombotic gene expressions of Hspa1a and Hspb1 were examined by real-time RT-PCR in mice after inferior vena cava (IVC) ligation. Hspb1 : murine HSP27 gene; Hspa1a : murine HSP70 gene. n = 5 in each group. ( c ) Immunohistochemical analysis of HSP27 and HSP70 in mouse thrombi. Representative results were shown (n = 5).

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques: Quantitative RT-PCR, Ligation, Immunohistochemical staining

Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: Double-color immunofluorescence analysis of HSPs and F4/80 or CD11b in the 14-days-thrombi. ( a ) HSP27 (green), F4/80 (red) and DAPI (blue); ( b ) HSP70 (green), F4/80 (red) and DAPI (blue); ( c ) CD11b (green), F4/80 (red) and DAPI (blue); ( d ) CD11b (green), HSP27 (red) and DAPI (blue); ( e ) CD11b (green), HSP70 (red) and DAPI (blue).

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques: Immunofluorescence

Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: Double-color immunofluorescence analysis of HSPs and MPO, α-SMA, or CD31 in the thrombi at the indicated time points. ( a ) HSP27 (green), MPO (red) and DAPI (blue); ( b ) HSP27 (green), α-SMA (red) and DAPI (blue); ( c ) HSP27 (green), CD31 (red) and DAPI (blue); ( d ) HSP70 (green), MPO (red) and DAPI (blue); ( e ) HSP70 (green), α-SMA (red) and DAPI (blue); ( f ) HSP70 (green), CD31 (red) and DAPI (blue).

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques: Immunofluorescence

Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: Mean intrathrombotic HSP27 + cells and HSP70 + cell numbers (n = 5).

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques:

Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: Changes in intrathrombotic HSP27 + cell and HSP70 + cell numbers after IVC ligation. Both positive cell number of HSP27 and HSP70 showed maximum values on day 10, but HSP27 was significantly abundant than HSP70. n = 5 in each group.

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques: Ligation

Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: The effects of HSP27 and HSP70 inhibitor in murine thrombosis. ( a ) Macroscopic appearance of venous thrombi obtained from mice treated with HSP27 inhibitor or PBS as controls. Representative results from five independent animals are shown. Thrombus mass ( b ) and thrombosed blood flow ( c ) were measured at 5 days after IVC ligation. ( d ) Macroscopic appearance of venous thrombi obtained from mice treated with HSP70 inhibitor or PBS as controls. Representative results from six independent animals are shown. Thrombus mass ( e ) and thrombosed blood flow ( f ) were measured at 5 days after IVC ligation. All values represent the mean ± SEM (n = 5–6 animals). ** p < 0.01, * p < 0.05 vs. control.

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques: Ligation, Control

Journal: Scientific Reports

Article Title: Relationship between intrathrombotic appearance of HSP27 and HSP70 and thrombus ages in a  murine model of deep vein thrombosis

doi: 10.1038/s41598-023-48987-5

Figure Lengend Snippet: Determination of human thrombus age.

Article Snippet: For mice thrombi, immunostaining of HSP27 and HSP70 were performed by Ventana Discovery XT (Ventana Medical Systems, Inc., AZ, USA) using mouse anti-HSP27 monoclonal antibodies (mAbs) (sc-13132, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA), mouse anti-HSP70 mAb (sc-32239, Santa Cruz Biotechnology, Inc., Santa Cruz CA, USA).

Techniques:

Journal: Nature Communications

Article Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis

doi: 10.1038/s41467-018-03627-9

Figure Lengend Snippet: HSP27 downregulation impairs myelofibrosis progression in a TPO high murine model. a In vivo strategy of HSP27 inhibition using OGX-427, or a scrambled oligonucleotide control (CTL) injected intraperitoneally 3 times a week at a dose of 10 mg kg −1 in a TPO high murine model of myelofibrosis (MF). Mice were 2–4 months old. b Expression level of HSP27 proteins in the serum of TPO high mice ( n =9) compared with healthy mice (WT, n =10) measured by ELISA assay. P value was calculated using the Mann–Whitney test. * P < .05. Error bars represent ±s.e.m. c Western blot analysis of HSP27 in splenocytes (whole cell lysate) of MF mice treated with OGX-427 or CTL. Actin served as the loading control. Bar graphs show quantification of mean relative amount of the proteins ( n =2 per group). Uncropped blots presented in Supplementary Fig. d Spleen weight was evaluated in mice ( n =9 per group). Outcomes of the two treatments were compared using the Mann–Whitney test. * P < .05. Error bars represent ±s.e.m. e Representative picture of spleen size of MF mice treated with CTL or OGX-427. f Left panel, haematoxylin and eosin-stained spleen sections revealed hyperplasia of the red pulp (R) in MF mice and partial restoration of the white pulp (W) territories in OGX-427-treated mice. Right panel, assessment of the grade of extramedullary haematopoiesis (EMH), from spleen sections in 18 killed mice. Pie chart: Grade A (light pink): diffuse EMH invasion. Grade B (purple colour): diffuse EMH invasion with atrophy of white pulp. Images were obtained using a Nanozoomer scanner (Hamamatsu, France) at ×23 magnification and Calopics software. g Left panel, histology of bone marrow sections after haematoxylin and eosin staining. Right panel, Pie chart representing percentages of mice according to erythrocyte (right upper panel) and megakaryocyte counts (right lower panel) from bone marrow sections of 18 killed mice: very low cell number (dark blue), decreased cell number (azure blue), normal cell number (light blue) and increased cell number (pink). Arrows show erythrocyte foci and megakaryocytes. Images were obtained using a Nanozoomer scanner (Hamamatsu, France) at ×13 magnification and Calopics software

Article Snippet: Precleared cell lysates were subjected to immunoprecipitation for 3 h using an anti-mouse HSP27 antibody (2 µg, SPA-800, Enzo Life Sciences) or anti-STAT5 mouse (4 µg, clone A-9, sc-74442, Santa-Cruz) or a mouse IgG (I5381, Sigma-Aldrich) as a negative control that had been pre-incubated for 1 h at room temperature (RT) with Protein G UltraLink Resin beads (53132, Pierce).

Techniques: In Vivo, Inhibition, Injection, Expressing, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY, Western Blot, Staining, Software

Journal: Nature Communications

Article Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis

doi: 10.1038/s41467-018-03627-9

Figure Lengend Snippet: HSP27 downregulation impairs myelofibrosis progression in a JAK2V617F murine model. a In vivo strategy of HSP27 inhibition using OGX-427 or a vehicle, injected intraperitoneally 3 times a week at a dose of 10 mg kg −1 in a JAK2V617F murine model of myelofibrosis (MF). Mice were 2 months old. b Spleen weight was evaluated in mice ( n =5 per group). Outcomes of the two treatments were compared using the Mann–Whitney test. * P < .05. Error bars represent ±s.e.m. c Western blot analysis of HSP27 in bone marrow (whole cell lysate) of MF mice treated with OGX-427 or vehicle. Actin served as the loading control. Bar graphs show quantification of mean relative amount of the proteins ( n =3 per group). Uncropped blots presented in Supplementary Fig. . d Percentage of megakaryocytes progenitors (MkPs) present in the bone marrow or spleen, error bars represent ±s.e.m. ( n =5 per group). P values were calculated using the Mann–Whitney test. * P < .05. e Upper panel, Gordon and Sweet-stained bone marrow sections revealed reduced reticulin fibrosis in MF mice and in OGX-427-treated mice. Lower panel, assessment of the fibrosis grade from bone marrow sections of 5 mice per group. Pie chart: Grade 1 (light pink): few thin reticulin fibres. Grade 2 (light red): networks of thin reticulin fibres. Grade 3 (purple): dense network of thick reticulin fibres. Images were obtained using a Nanozoomer scanner (Hamamatsu, France) at ×23 magnification and Calopics software. f Blood cell parameters assessed in mice before and after OGX-427 ( n =5) or vehicle treatment ( n =5) and on the day of killing. WBC white blood cells. Error bars represent ±s.e.m. P values were calculated using the Mann–Whitney test. * P < .05; ** P < .01. *** P < .001

Article Snippet: Precleared cell lysates were subjected to immunoprecipitation for 3 h using an anti-mouse HSP27 antibody (2 µg, SPA-800, Enzo Life Sciences) or anti-STAT5 mouse (4 µg, clone A-9, sc-74442, Santa-Cruz) or a mouse IgG (I5381, Sigma-Aldrich) as a negative control that had been pre-incubated for 1 h at room temperature (RT) with Protein G UltraLink Resin beads (53132, Pierce).

Techniques: In Vivo, Inhibition, Injection, MANN-WHITNEY, Western Blot, Staining, Software

Journal: Nature Communications

Article Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis

doi: 10.1038/s41467-018-03627-9

Figure Lengend Snippet: HSP27 affects proliferation of JAK2V617F leukaemic cell lines. a HEL92.1.7, SET-2 and K562 cells were transfected with HSP27 siRNA, OGX-427 or an oligonucleotide control (CTL). Bars represent cell proliferation percentages relative to non-transfected cells (NT) from 9 independent experiments. P values were calculated using the Mann–Whitney test. ** P < .01. Error bars represent ±s.e.m. b HEL92.1.7, SET-2 and K562 cells were transfected with HSP27 siRNA, OGX-427 or CTL and lysed 48 h later in Laemmli Buffer. Protein expression was determined by western blot and compared to non-transfected cells (NT). Actin was used as the loading control ( n =3 independent experiments). See quantification of the blot in Supplementary Fig. . Uncropped blots presented in Supplementary Fig.

Article Snippet: Precleared cell lysates were subjected to immunoprecipitation for 3 h using an anti-mouse HSP27 antibody (2 µg, SPA-800, Enzo Life Sciences) or anti-STAT5 mouse (4 µg, clone A-9, sc-74442, Santa-Cruz) or a mouse IgG (I5381, Sigma-Aldrich) as a negative control that had been pre-incubated for 1 h at room temperature (RT) with Protein G UltraLink Resin beads (53132, Pierce).

Techniques: Transfection, MANN-WHITNEY, Expressing, Western Blot

Journal: Nature Communications

Article Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis

doi: 10.1038/s41467-018-03627-9

Figure Lengend Snippet: HSP27 affects de-phosphorylation of STAT5. a The phosphorylation of STAT5 by JAK2 is HSP27 independent. An in vitro kinase assay was performed using the recombinant protein JAK2 and STAT5 (produced in reticulocyte lysate) in the presence or absence of HSP27 (produced in reticulocyte lysate). The level of STAT5 phosphorylation, and the amount of JAK2 and STAT5 proteins were determined by western blot ( n =3 independent experiments). Uncropped blots presented in Supplementary Fig. . b HSP27 impairs the in vitro de-phosphorylation of STAT5 induced by SHP2. Following an in vitro kinase assay using the recombinant protein JAK2 and STAT5 (same batch produced in reticulocyte lysate), samples were incubated or not with the recombinant phosphatase, SHP2, in the presence or absence of HSP27 (produced in reticulocyte lysate). The level of phosphorylated STAT5 was detected by western blot using an antibody specific for Ph-STAT5. The expressions of JAK2, SHP2 and HSP27 are also shown. Bar graphs show normalized ratios of Ph-STAT5_SHP2/Ph-STAT5 bands quantified from the western blots ( n =4 independent experiments), error bars represent the ±s.d. P values were calculated using the Student’s t test. ** P < .01. Uncropped blots presented in Supplementary Fig. . c HEL92.1.7 cells were transfected with HSP27 siRNA or CTL for 48 h. Then, cells were treated or not with the JAK2 inhibitor, AG490 (100 μM), at indicated times and lysed in Laemmli Buffer. Level of STAT5 phosphorylation was determined by western blot. Actin was used as the loading control ( n =3 independent experiments). Uncropped blots presented in Supplementary Fig.

Article Snippet: Precleared cell lysates were subjected to immunoprecipitation for 3 h using an anti-mouse HSP27 antibody (2 µg, SPA-800, Enzo Life Sciences) or anti-STAT5 mouse (4 µg, clone A-9, sc-74442, Santa-Cruz) or a mouse IgG (I5381, Sigma-Aldrich) as a negative control that had been pre-incubated for 1 h at room temperature (RT) with Protein G UltraLink Resin beads (53132, Pierce).

Techniques: De-Phosphorylation Assay, In Vitro, Kinase Assay, Recombinant, Produced, Western Blot, Incubation, Transfection

Journal: Nature Communications

Article Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis

doi: 10.1038/s41467-018-03627-9

Figure Lengend Snippet: HSP27 interacts with JAK2/STAT5. a The binding of recombinant JAK2 and STAT5a/b at 125 nM to immobilized biotinylated HSP27 was determined by biolayer interferometry Crystallin alpha B and the CBP RING domain serves as a positive control and negative control, respectively (Supplementary Fig. ) ( n =3 independent experiments). b Immunoprecipitation from HEL92.1.7 cell extracts of endogenous HSP27 was followed by immunodetection of endogenous STAT5 and JAK2. CTL: unstimulated cells starved for 16 h; +SVF: Cells starved for 16 h and then stimulated with SVF (10%) for 30 min. Inputs: proteins in total cell lysates. IP IgG: immunoprecipitation with a non-relevant antibody (IgG mouse) ( n =2 independent experiments). Uncropped blots presented in Supplementary Fig. . c Immunoprecipitation of endogenous STAT5 was followed by immunodetection of endogenous HSP27 and JAK2. Inputs: proteins in total cell lysates. IP IgG: immunoprecipitation with a non-relevant antibody (IgG mouse) ( n =2 independent experiments). Uncropped blots presented in Supplementary Fig. . d Immunofluorescence analysis of the endogenous interaction (red foci) of JAK2 (upper panel) or STAT5 (middle panel) with HSP27 visualized in situ by PLA in HEL92.1.7 cells transfected or not (NT) with a HSP27 siRNA. Nuclei are stained with DAPI. Images were taken randomly and obtained using an Axio Imager 2 at ×40 magnification and analysed using ICY software. Cells were segmented manually, and the number of interaction foci in each cell was counted using the spot detector plugin. Right panel, graphs represent quantification of the interaction of JAK2 or STAT5 with HSP27 visualized in situ by PLA. Each data point corresponds to an analysed cell, placed according to the number of detected interaction foci (lower panel). Immunofluorescence analysis of the endogenous interaction (red foci) of JAK2 with STAT5 visualized in situ by PLA in HEL92.1.7 cells transfected with a scramble (CTL) or a HSP27 siRNA (siHSP27). Nuclei are stained with DAPI. Images were obtained using an Axio Imager 2 at ×63 magnification and analysed using ICY software as in upper panel. Right panel, graphs represent quantification of the interaction of endogenous JAK2 with STAT5 visualized by PLA. P values were calculated using the Mann–Whitney test. **** P < .0001. Scale bar 10 µm

Article Snippet: Precleared cell lysates were subjected to immunoprecipitation for 3 h using an anti-mouse HSP27 antibody (2 µg, SPA-800, Enzo Life Sciences) or anti-STAT5 mouse (4 µg, clone A-9, sc-74442, Santa-Cruz) or a mouse IgG (I5381, Sigma-Aldrich) as a negative control that had been pre-incubated for 1 h at room temperature (RT) with Protein G UltraLink Resin beads (53132, Pierce).

Techniques: Binding Assay, Recombinant, Positive Control, Negative Control, Immunoprecipitation, Immunodetection, Immunofluorescence, In Situ, Transfection, Staining, Software, MANN-WHITNEY

Journal: Nature Communications

Article Title: HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis

doi: 10.1038/s41467-018-03627-9

Figure Lengend Snippet: HSP27 is overexpressed in patients with MPN-associated MF. a Flow cytometry analysis of HSP27, HSP70 and HSP90 in circulating hematopoietic progenitor CD34 + cells from patients with myelofibrosis (MF) and healthy control donors (HDs) (number of samples analysed; MF: n =11–18; HD: n =10–12). P values were calculated by using the unpaired t test with Welch’s correction. ** P < .01; n.s. not significant. Expression levels of HSP27, HSP70 and HSP90 from MF patients were plotted as median fluorescence intensities. b Analysis of HSP27, HSP70 and HSP90 levels in the serum of patients with MF ( n =24-27) compared with HDs ( n =15) measured by ELISA. P values were calculated using the Mann–Whitney test. **** P < .0001. c Representative histological sections of bone marrow from MF patients. Images were obtained using Cell Observer (Zeiss, France) at two different magnifications (×23, scale bar 20 µm and ×63, scale bar 10 µm) and Axiovision software. Arrows show megakaryocytes

Article Snippet: Precleared cell lysates were subjected to immunoprecipitation for 3 h using an anti-mouse HSP27 antibody (2 µg, SPA-800, Enzo Life Sciences) or anti-STAT5 mouse (4 µg, clone A-9, sc-74442, Santa-Cruz) or a mouse IgG (I5381, Sigma-Aldrich) as a negative control that had been pre-incubated for 1 h at room temperature (RT) with Protein G UltraLink Resin beads (53132, Pierce).

Techniques: Flow Cytometry, Expressing, Fluorescence, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY, Software

Journal: Clinical immunology (Orlando, Fla.)

Article Title: Occurrence of Major Anti-retinal Autoantibodies Associated with Paraneoplastic Autoimmune Retinopathy

doi: 10.1016/j.clim.2019.108317

Figure Lengend Snippet: List of control proteins and antibodies used in the study

Article Snippet: Only patients whose sera were verified for antibody specificity have been the focus of this study. table ft1 table-wrap mode="anchored" t5 Table 1: caption a7 Antigen Molecular Mass Protein Name Source Control Antibody Source 23-kDa Recombinant Recoverin Purified in the lab Rat MAb anti-recoverin Made in the lab 23-kDa Recombinant HSP27 R&D Mouse anti-human HSP27 Thermo Fisher Scientific 23-kDa Recombinant Rab6A NOVUS Rabbit anti-human Rab6A NOVUS 30-kDa Purified CAII Sigma Sheep anti-human CAII Invitrogen 34-kDa Recombinant CRALBP NOVUS Rabbit anti-human CRALBP Thermo Fisher 36-kDa Purified GADPH Sigma Rabbit anti-human GADPH Sigma 40-kDa Aldolase C MP Biomedical Rabbit anti-aldolase C Cell Signaling Technology 46-kDa Purified retinal α-Enolase Purified in the lab Rat MAb anti-α-enolase Made in the lab 48-kDa Purfied retinal Arrestin Purified in the lab Mouse MAb anti-arrestin Made in the lab 52-kDa Purified Tubulin-α Sigma Goat anti-human tubulin-α Santa Cruz 56-kDa Recombinant PKM2 NOVUS Rabbit anti-human PKM2 Invitrogen 62-kDa Recombinant HSP60 StressMarq Rabbit anti-human HSP60 Cell signaling Technology Open in a separate window List of control proteins and antibodies used in the study

Techniques: Recombinant, Purification

Journal: Clinical immunology (Orlando, Fla.)

Article Title: Occurrence of Major Anti-retinal Autoantibodies Associated with Paraneoplastic Autoimmune Retinopathy

doi: 10.1016/j.clim.2019.108317

Figure Lengend Snippet: Frequency of anti-retinal autoantibodies against 12 autoantigens in normal individuals and patients with cancer and vision loss

Article Snippet: Only patients whose sera were verified for antibody specificity have been the focus of this study. table ft1 table-wrap mode="anchored" t5 Table 1: caption a7 Antigen Molecular Mass Protein Name Source Control Antibody Source 23-kDa Recombinant Recoverin Purified in the lab Rat MAb anti-recoverin Made in the lab 23-kDa Recombinant HSP27 R&D Mouse anti-human HSP27 Thermo Fisher Scientific 23-kDa Recombinant Rab6A NOVUS Rabbit anti-human Rab6A NOVUS 30-kDa Purified CAII Sigma Sheep anti-human CAII Invitrogen 34-kDa Recombinant CRALBP NOVUS Rabbit anti-human CRALBP Thermo Fisher 36-kDa Purified GADPH Sigma Rabbit anti-human GADPH Sigma 40-kDa Aldolase C MP Biomedical Rabbit anti-aldolase C Cell Signaling Technology 46-kDa Purified retinal α-Enolase Purified in the lab Rat MAb anti-α-enolase Made in the lab 48-kDa Purfied retinal Arrestin Purified in the lab Mouse MAb anti-arrestin Made in the lab 52-kDa Purified Tubulin-α Sigma Goat anti-human tubulin-α Santa Cruz 56-kDa Recombinant PKM2 NOVUS Rabbit anti-human PKM2 Invitrogen 62-kDa Recombinant HSP60 StressMarq Rabbit anti-human HSP60 Cell signaling Technology Open in a separate window List of control proteins and antibodies used in the study

Techniques:

Journal: Clinical immunology (Orlando, Fla.)

Article Title: Occurrence of Major Anti-retinal Autoantibodies Associated with Paraneoplastic Autoimmune Retinopathy

doi: 10.1016/j.clim.2019.108317

Figure Lengend Snippet: Analysis of Contingency Table: Overview

Article Snippet: Only patients whose sera were verified for antibody specificity have been the focus of this study. table ft1 table-wrap mode="anchored" t5 Table 1: caption a7 Antigen Molecular Mass Protein Name Source Control Antibody Source 23-kDa Recombinant Recoverin Purified in the lab Rat MAb anti-recoverin Made in the lab 23-kDa Recombinant HSP27 R&D Mouse anti-human HSP27 Thermo Fisher Scientific 23-kDa Recombinant Rab6A NOVUS Rabbit anti-human Rab6A NOVUS 30-kDa Purified CAII Sigma Sheep anti-human CAII Invitrogen 34-kDa Recombinant CRALBP NOVUS Rabbit anti-human CRALBP Thermo Fisher 36-kDa Purified GADPH Sigma Rabbit anti-human GADPH Sigma 40-kDa Aldolase C MP Biomedical Rabbit anti-aldolase C Cell Signaling Technology 46-kDa Purified retinal α-Enolase Purified in the lab Rat MAb anti-α-enolase Made in the lab 48-kDa Purfied retinal Arrestin Purified in the lab Mouse MAb anti-arrestin Made in the lab 52-kDa Purified Tubulin-α Sigma Goat anti-human tubulin-α Santa Cruz 56-kDa Recombinant PKM2 NOVUS Rabbit anti-human PKM2 Invitrogen 62-kDa Recombinant HSP60 StressMarq Rabbit anti-human HSP60 Cell signaling Technology Open in a separate window List of control proteins and antibodies used in the study

Techniques: