mab935  (R&D Systems)

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: ADAM15 knockdown affects necroptosis but not apoptosis, NFκB, and MAPK signaling in U937 cells. a CRISPR Cas-9 mediated knockout of ADAM15 was monitored by WB using two different antibodies (R&D: MAB935 and HPA: HPA011633). Knockout (ko) cells are further referred to as ΔADAM15. Actin served as a loading control. n = 3 experiments performed. b ADAM15 knockout was validated by flow cytometry. The green curve represents staining using an anti-ADAM15 antibody (upper panel) or an isotype control (lower panel) in U937 wt cells. The red curve represents staining in U937 ΔADAM15 cells. The dashed non-coloured curves represent unstained cells. Right-shifted curves indicate higher fluorescence intensity. Representative data of n = 3 experiments are shown. c The degradation of IκB was monitored by WB. Band densities were quantified, and IkB:actin ratios are shown (green: U937 wt; red: U937 ΔADAM15). Representing n = 3 independent experiments. d The activation/phosphorylation of MAPK was monitored by WB. Band densities were quantified, and MAPK:actin ratios are shown (green: U937 wt; red: U937 ΔADAM15). Representative data of n = 3 experiments are shown. e Representative scatter plots of flow cytometry-based cell death analyses. The x-axis shows changes in fluorescence intensity due to increased Annexin V-FITC binding. The y-axis indicates increased fluorescence of 7AAD due to binding to DNA. Multiple ( n = 9) assays were quantified (right panel; green bars: WT; red bars: ΔADAM15). *: p = 0,05; ** p = 0,01; *** p = 0,001. f WB was used to monitor TC-mediated apoptosis (PARP-1 and caspases-3 and −8) and TCz-mediated necroptosis (MLKL oligomer). n = 3 experiments performed. Actin serves as a loading control

Article Snippet: ADAM15 (MAB935, R&D Systems), ADAM15 (HPA011633, Sigma-Aldrich).

Techniques: Knockdown, CRISPR, Knock-Out, Control, Flow Cytometry, Staining, Fluorescence, Activation Assay, Phospho-proteomics, Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: ADAM15 knockdown affects necroptosis but not apoptosis induction in U937 cells mediated by TRAIL, FasL, TL1a, and Obatoclax. a-c Representative scatter plots of flow cytometry-based cell death analyses upon incubation with TRAIL (a), FasL (b), or TL1a ( c ) The x-axis shows changes in fluorescence intensity due to increased Annexin V-FITC binding. The y-axis indicates increased fluorescence of 7AAD due to binding to DNA. Multiple ( n = 3 per ligand) assays were quantified (right panels; green bars: WT; red bars: ΔADAM15) d Obatoclax mediated apoptosis (Oba) and necroptosis (Obaz) compared to TNF/BV-6 (TB: apoptosis) and TNF/BV-6/zVAD (TBz: necroptosis) were monitored by WB in U937 wt (left panel) and U937 ΔADAM15 cells (right panel). Represents n = 3 independent experiments. Tubulin serves as a loading control

Article Snippet: ADAM15 (MAB935, R&D Systems), ADAM15 (HPA011633, Sigma-Aldrich).

Techniques: Knockdown, Flow Cytometry, Incubation, Fluorescence, Binding Assay, Control

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: Shotgun proteome analysis reveals regulated proteins upon ADAM15 knockout in U937 wt and U937 ΔADAM15 cells. a Volcano plot (p-value: 0.01; fdr: 0.01; fold-change cutoff 1: 0.3; fold-change cutoff 2: −0.3; min. samples for significance 0.75) shows proteins enriched in wt cells (red) versus U937 ΔADAM15 cells. The top 25 modulated proteins are indicated along with the selected proteins. The top annotated GSEA groups are shown: b ‘Regulation of endocytosis’, c ‘Regulation of autophagy’, d ‘Macroautophagy’, e ‘Organelle fusion’, f ‘Vacuole organization’, g ‘Regulation of mitochondrion organization’, h ‘Cell redox homeostasis’, i ‘Epigenetic regulation of gene expression’, and j ‘Mitotic cell cycle phase transition’. The upper panel shows the respective GO-termini, encircled by the involved proteins (Fold change is color-coded). The lower panels show the respective proteins as STRING-DB (V12.0) based networks. ADAM15 is highlighted for each network (dashed red circle)

Article Snippet: ADAM15 (MAB935, R&D Systems), ADAM15 (HPA011633, Sigma-Aldrich).

Techniques: Knock-Out, Gene Expression, Sublimation

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: Analysis of differential protein expression by WB and caspase-8 activity. a Depicts the validation of up- and down-modulation of selected proteins from the proteome analysis. b Representative (of n = 3) WB for RIPK1 probed with two different antibodies (cell signaling: #3493S and BD: 610,459). c Representative (of n = 3) WB analysis of various cell death-associated and non-related proteins. d Caspase-8 appears partially active in U937 ΔADAM15 compared to wt cells, indicated by reduced p55/44 and increased p43/41 and p18 (blue box – enhanced contrast). e Validation of increased basal Caspase-8 activity by flow cytometry. Dashed colorless curves indicate no staining. The green curve indicates wt cells stained with IETD-FITC, and the red curve indicates U937 ADAM15 cells with IETD-FITC. X-axis shift to the right side indicates increased fluorescence due to binding of IETD to active caspase-8 (p-18). Representative of n = 3 experiments. f Flow cytometry-based analysis of death receptor and ADAM15 surface expression. The non-coloured curves represent unstained and Strep-AF488-stained cells, the green curve WT, and the red curve ADAM15 cells. Representative data of n = 3 experiments

Article Snippet: ADAM15 (MAB935, R&D Systems), ADAM15 (HPA011633, Sigma-Aldrich).

Techniques: Expressing, Activity Assay, Biomarker Discovery, Flow Cytometry, Staining, Fluorescence, Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: ADAM15 knockout in Jurkat cells results in abrogation of necroptosis induction and enhanced basal caspase-8 activity. a ADAM15 knockout was monitored by WB and b flow cytometry. The green curve represents staining using an anti-ADAM15 antibody (upper panel) or an isotype control (lower panel) in U937 wt cells. The red curve represents staining in Jurkat ΔADAM15 cells. The dashed non-coloured curves represent unstained cells. Right-shifted curves indicate higher fluorescence intensity. c degradation of IκB and d phosphorylation of MAPK are not affected by ADAM15 knockout. Band densities were quantified, and IκB:actin or MAPK:actin ratios are shown (green: Jurkat wt; red: Jurkat ΔADAM15). e WB analysis of cell death in Jurkat cells. f Representation of multiple ( N = 4) flow cytometry-based cell death analyses (green bars: WT; red bars: ΔADAM15). g WB analysis of Obatoclax (Oba) mediated cell death in Jurkat cells. TNF/BV-6 or TNF/BV-6/zVAD treatment served as control. h WB was probed for cell death-related and unrelated proteins, revealing reduced amounts of full-length RIPK1 (third panel, left) and pre-activated caspase-8 (first panel, right). i The enhanced basal activation of caspase-8 was validated using flow cytometry. The dashed colorless curves indicate no staining. The green curve indicates wt cells stained with IETD-FITC, and the red curve indicates U937 ADAM15 cells with IETD-FITC. X-axis shift to the right side indicates increased fluorescence due to binding of IETD to active caspase-8 (p-18). In a, c, d, e, and f, actin or tubulin served as loading controls. Where not stated otherwise, representative data of n = 3 experiments are shown

Article Snippet: ADAM15 (MAB935, R&D Systems), ADAM15 (HPA011633, Sigma-Aldrich).

Techniques: Knock-Out, Activity Assay, Flow Cytometry, Staining, Control, Fluorescence, Phospho-proteomics, Activation Assay, Binding Assay

Journal: Cell Communication and Signaling : CCS

Article Title: Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation

doi: 10.1186/s12964-025-02530-3

Figure Lengend Snippet: Exogenously expressed RIPK1 is degraded in U937 ΔADAM15 cells, and ADAM15 is partially located in lysosome-like organelles. a WB analysis of exogenously expressed RIPK1: accumulation of full-length RIPK1 in U937 wt cells, and moderately in U937 ΔADAM15 cells (black arrowhead). In U937 ΔADAM15 cells, RIPK1 is directly cleaved (grey arrowhead). Actin serves as a loading control. b Lamp-2, Cathepsin D, and also ADAM15 are enriched in the lysosome-containing fraction (LysIP), compared to total lysate or soluble proteins (SNT). nM represents the lysosome-depleted non-magnetic fraction remaining after the isolation procedure. p8 and p10 represent two different homogenization procedures. Nucleoporin p62 and actin serve as loading/purity controls. c Fluorescence microscopy monitoring ADAM15 (red) and Lamp-1 (green) reveals partial co-localization (arrowheads) of both proteins in U937 cells. Manders’ tM1/tM2 values are: 0.495/0.619 (upper left); 0.403/: 0.362 (upper right), (lower left) 0.434/0.377; (lower right) 0.302/0.371 (lower right). Values of tM1/tM2 > 0.5 are considered moderate, > 0.7 strong colocalized. DNA (blue) is stained with DAPI. Scale bar indicates 10 µm. Where not stated otherwise, representative data of n = 3 experiments are shown. d Working model of ADAM15-mediated control of necroptosis induction (Model created in BioRender)

Article Snippet: ADAM15 (MAB935, R&D Systems), ADAM15 (HPA011633, Sigma-Aldrich).

Techniques: Control, Isolation, Homogenization, Fluorescence, Microscopy, Staining

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 1. ADAM15-dependent mechano-induced downregulation of lncRNA H19 is affected by inhibition of p21-activated kinases (PAKs). (A, B) Synovial fibroblasts either silenced with an ADAM15 siRNA or a non-silencing negative siRNA were mechanically strained (1 Hz and 15% elongation) for 1–9 h and H19 levels determined by RT-qPCR. (A) Fold changes of H19 in ADAM15-expressing versus non-expressing cells were calculated using the 2−ΔΔCt. Shown is the mean ± SD of 6 different RASFs. (B) time course of GAPDH- normalized Ct values for H19 upon mechanical strain, showing increase of Ct values (i.e. lower H19 amounts) in ADAM15 expressing cells (black dots) compared to ADAM15 non-expressing cells (open circle) in one representative RASF cell line. (C) RT-qPCR for H19 of RASFs stimulated for 1 and 3 h in the presence of either DMEM medium, or inhibitors for JNK (SP600125), Src family kinases (dasatinib), CAMKII (KN- 93), calmodulin (TFP) and PAKs (IPA-3). **p < 0.005, ***p < 0.0005, Student’s t-test, comparing ADAM15- expressing versus non-expressing cells or inhibitor versus DMEM.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Inhibition, Quantitative RT-PCR, Expressing

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 2. ADAM15- and N-cadherin (NCAD) dependent activation of PAK2 upon mechanical strain. (A–D) Immunoblots for pPAK2. (A) of RASFs seeded at different cell densities and mechanically strained for 30 and 60 min. (B) from strained RASFs with PAK2 silencing (si) and treated with a negative control siRNA (neg). (C, D) immunoblots for pPAK2, ADAM15 and NCAD from RASFs treated with ADAM15 and NCAD siRNA; right panels, showing the mean ± SD of densitometric analysis of 6 different RASF cell lines. ***p < 0.0005, Student’s t-test. GAPDH served as a loading control.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Activation Assay, Western Blot, Negative Control, Control

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 3. Interaction of ADAM15 with N-cadherin (NCAD) in synovial fibroblasts. (A) Co- immunoprecipitations (IP) of RASFs with prior silencing of ADAM15 using siRNA (I) and negative control siRNA (N) using NCAD antibodies (upper panels) or ADAM15 antibodies (lower panels) and detection of ADAM15 or NCAD with the respective antibodies. (B) Analogous to (A) Co-IPs using NCAD and ADAM15 antibodies in chondrocyte cell lines transfected with full length ADAM15 plasmid (+) or with ADAM15 lacking the cytoplasmic tail (Δcyto) and an empty vector (-). Mouse IgG served as a control. Input: 10% total lysate. (C) confocal microscopy of RASFs double immunofluorescently stained for NCAD (green) and ADAM15 (red). White inset indicates area of the magnified merged image. (D) In situ proximity ligation assays for ADAM15 and NCAD, showing direct interaction of both molecules in densely seeded cells only (arrows). Cell nuclei were counterstained with DAPI. Objective 40x, scale bar = 10 μm.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Negative Control, Transfection, Plasmid Preparation, Control, Confocal Microscopy, Staining, In Situ, Ligation

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 5. Binding of PAK2 to ADAM15/NCAD complex at cell membrane is crucially dependent on ADAM15. (A) IPs of strained RASFs using ADAM15 or NCAD antibodies and detection of PAK2 and Nck. TL = total lysate. IgG, mouse IgG served as background control. (B) cell surface biotinylation and enrichment of membrane fractions on streptavidin beads of strained cells with ADAM15-silenced or nonsilenced (N). Contr: non biotinylated cell lysates enriched on streptavidin beads served as background control. (C, D) IPs using ADAM15 antibodies in (C) RASFs with silenced and nonsilenced ADAM15 expression (N) and (D) in chondrocyte cell lines transfected with full length ADAM15 (full-A15) or ADAM15 lacking the cytoplasmic domain (Δcyto). (E, F) analogous to (C, D) IPs using N-cadherin antibodies, showing precipitates of PAK2 and Nck in ADAM15-expressing cells only. (E) right, densitometric evaluation of PAK2 from experiments obtained from 4 donors.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Binding Assay, Membrane, Control, Expressing, Transfection

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 6. Cadherin-11, but not Cadherin-2 (NCAD) is a target of mechano-downregulated H19. (A, B) RASFs with ADAM15-nonsilenced (N) or silenced (I) were mechanically strained and (A) RT-qPCR, fold changes of CDH11 or NCAD from 5 different RASFs and (B) immunoblots for CDH11 and NCAD, right, densitometry for CDH11 and NCAD from 4 different RASFs. (C, D) unstimulated RASFs with H19 silenced versus nonsilenced, (C) RT-qPCR, fold changes of CDH11 and NCAD from 5 different RASFs, (D) immunoblots for CDH11 and NCAD, right, densitometry from 4 different RASFs. (E) RT-qPCR for CDH11 and NCAD from mechanically strained (1 h) RASFs incubated with PAK inhibitor IPA-3 or DMEM medium. (F) densitometric evaluation of immunoblots for CDH11 and NCAD from 4 different RASFs (mean ± SD) treated with DMEM or IPA-3 for 48 h. GAPDH served as loading control. **p < 0.005, ***p < 0.0005, Student’s t-test, comparing DMEM versus inhibitor.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Quantitative RT-PCR, Western Blot, Incubation, Control

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 7. ADAM15/H19-dependent downregulation of miR-130a-3p, which binds to 3’ UTR of cadherin-11 and regulates its expression. (A) RNA pull-downs using transfected miR-130a-3p or scrambled mimics, purification on streptavidin beads and detection of binding using qPCR of H19, CDH11 and NCAD, showing Ct values of 5 different RASFs (mean ± SD). (B) RT-qPCR of miR-130a-3p in ADAM15-expressing or silenced RASFs, showing the mean ± SD of fold changes from 5 different RASFs. (C) RT-qPCR for miR-130a-3p in RASFs silenced with two different H19 siRNAs (I and II) vs. negative control siRNA (N). (D, E) RASFs prior transfected with 130a-3p mimics or scramble were strained and (D) RT-qPCR for CDH11 and NCAD and (E) immunoblots for CDH11 and NCAD; untreated = strained without any treatment; right panel, densitometry for CDH11 from 4 different RASFs. GAPDH served as loading control. **p < 0.005, ***p < 0.0005, Student’s t-test.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Expressing, Transfection, Purification, Binding Assay, Quantitative RT-PCR, Negative Control, Western Blot, Control

Journal: Scientific reports

Article Title: Mechanical forces trigger invasive behavior in synovial fibroblasts through N-cadherin/ADAM15 -dependent modulation of LncRNA H19.

doi: 10.1038/s41598-025-94012-2

Figure Lengend Snippet: Fig. 8. CDH11-mediated increased cell invasion can be blocked by CDH11 silencing and transfection with miR-130a-3p mimics. (A, B) RASFs were treated with H19 siRNA or negative nonsilencing siRNA (N) and (A) MTT-based cell viability assays and (B) cells transmigrated through matrigel were stained with DAPI, the whole transwell photographed and all cells counted. (C) upper panel, invaded cells prior transfected with 130a- 3p mimics, CDH11 siRNA or scramble control, shown is the mean ± SD from 5 different RASFs. (C) lower panel, immunoblots for CDH11 from cells transfected and strained as in upper panel. *p < 0.05, **p < 0.005, ***p < 0.0005, Student’s test. (D) diagram of summarized results: mechanical strain results in NCAD/ADAM15- mediated phosphorylation of PAK2, resulting in the downregulation of lncRNA H19 and miR-130a-3p and subsequent upregulation of CDH11, which in turn promotes an aggressive phenotype: increased cell invasion. Inhibition of PAK signaling by PAK inhibitor IPA-3 blocks mechano-induced H19 downregulation and subsequently CDH11 upregulation. In addition, mechano-induced PAK2 phosphorylation is accompanied by recruitment of SH2/SH3 adapter Nck and PAK2 to the NCAD/ADAM15 complex, but binding of Nck/PAK2 is restricted to the cytoplasmic domain of ADAM15. The mechano-induced redistribution of PAK2 to the cell membrane does not occur when Nck is silenced.

Article Snippet: For detection of ADAM15 and NCAD, cells (1 × 104) were grown on 8-chamberslides for 48 h, fixed with 4% PFA, permeabilized with PBS/0.1% Triton X-100 for 5 min, blocked with 1% horse serum and incubated with mouse ADAM15 (R&D Systems, #MAB935, 1:50) and sheep-anti N-cadherin antibodies.

Techniques: Transfection, Staining, Control, Western Blot, Phospho-proteomics, Inhibition, Binding Assay, Membrane

Journal: Cell reports

Article Title: PAI-1-Dependent Inactivation of SMAD4-Modulated Junction and Adhesion Complex in Obese Endometrial Cancer

doi: 10.1016/j.celrep.2020.108253

Figure Lengend Snippet: (A–C) Expression profiles of SMAD4 and JAC based on CyTOF were classified into five categories: I, II, III, IV, and V. Violin plots show ordered SMAD4 expression level (low to high) and distribution in the individual subpopulations (A). Expression heatmaps of JAC were aligned according to SMAD4 expression levels (in descending order) in different cellular subpopulations (B). Area of circle denotes relative cell proportion of a subpopulation within each sample and ordered in the aforementioned five categories in cellular subpopulations of EME6/7t lines and primary tumors (C). Tumors were ordered from top to bottom based on increased patients’ BMIs and histology classes. (D) Balloon plots of subpopulation distributions of endometrial tumors in the five categories based on histology and BMI. Circle area indicates the size of each subpopulation. Categories IV and V were associated with relatively high expression levels of SMAD4 and JAC, whereas low levels of SMAD4 and JAC were noted in categories I, II, and III. (E) Violin plots showing the average expression levels of four JAC markers—ADAM15, ROCK1, Cx43, and Gas1—based on patients’ tumor histology: papillary serous and endometrioid. (F) Balloon plots of subpopulation distributions in the five categories stratified by BMI into three groups: normal weight (NW), obesity (OB), and morbid obesity (MOB). (G) Violin plots showing the average expression levels of ADAM15, ROCK1, Cx43, and Gas1, based on three BMI groups: NW, OB, and MOB. Lower JAC expressions corresponded with patients with higher BMIs. ****p < 0.0001. See also .

Article Snippet: ADAM15 (clone 23G9) , Novus Biologicals , Cat# MAB935-100.

Techniques: Expressing

Journal: Cell reports

Article Title: PAI-1-Dependent Inactivation of SMAD4-Modulated Junction and Adhesion Complex in Obese Endometrial Cancer

doi: 10.1016/j.celrep.2020.108253

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: ADAM15 (clone 23G9) , Novus Biologicals , Cat# MAB935-100.

Techniques: Ubiquitin Proteomics, Recombinant, Multiplex Assay, Reverse Transcription, SYBR Green Assay, In Situ, shRNA, Software