Journal: bioRxiv

Article Title: Ångström Resolution with Flow Immunofluorescence Localization Microscopy (FILM)

doi: 10.64898/2025.12.16.694546

Figure Lengend Snippet: (A) FILM acquisition of anti-TOM22-APC in PFA-fixed and permeabilized HeLa cells. (B) Zoom-in of respective boxed region in A. (C) Zoom-in of boxed region in B. (D) Zoom-in of respective boxed region in A. (E) Zoom-in of boxed region in D. Panels A, B, and D use 10 nm pixels with 3-pixel Gaussian blurring. In panels C and E, localizations are represented as peak-normalized Gaussians with color-coded precision according to the colorbar.

Article Snippet: α-tubulin (REA1136 REAfinityTM, h, APC, #130-119-541, Miltenyi Biotec), CD2 (REA972 REAfinityTM, h, APC, #130-116-150, Miltenyi Biotec), CD20 (REA780 REAfinityTM, h, APC, #130-111-339, Miltenyi Biotec), CD28 (REA612 REAfinityTM, h, APC, #130-118-343, Miltenyi Biotec), CD45 (REA1023 REAfinityTM, h/nhp, APC, #130-117-191, Miltenyi Biotec), CD54/ICAM-1 (REA266 REAfinityTM, h, APC, #130-120-711, Miltenyi Biotec), CD81 (REA513 REAfinityTM, h, APC, #130-119-787, Miltenyi Biotec), CD107a/LAMP1 (REA792 REAfinityTM, h, APC, #130-111-847, Miltenyi Biotec), IgD (REA740 REAfinityTM, h, APC, #130-110-644, Miltenyi Biotec), IgM (REAL689 REAdye_leaseTM, h, PE, #130-125-786, Miltenyi Biotec), Pan-Cytokeratin (REA1141 REAfinityTM, h, APC, #130-120-096, Miltenyi Biotec), β-catenin (REA480 REAfinityTM, h, APC, #130-124-444, Miltenyi Biotec), TCRα/β (REA652 REAfinityTM, h, APC, #130-113-535, Miltenyi Biotec), TOM22 (REA1185 REAfinityTM, APC, h/ms, #130-122-079, Miltenyi Biotec), DAPI Staining Solution (#130-111-570, Miltenyi Biotec), and ATTO 643 phalloidin (ATT-AD643-81, ATTO-TEC).

Techniques:

Journal: Nature Communications

Article Title: Mitochondria-targeted gene delivery using fluorinated lipid nanoparticles to alleviate Leber’s hereditary optic neuropathy

doi: 10.1038/s41467-025-65874-x

Figure Lengend Snippet: A Formulation of 6F-M-LNPs via microfluidic mixing and thiol-maleimide coupling. B Cellular uptake capacity of 6F-M-LNPs with different proportions of MTS ( n = 3 biologically independent samples). C Mitochondrial GFP transfection efficiency of 6F-M-LNPs with different proportions of MTS ( n = 3 biologically independent samples). D Physicochemical characterization of 6F-LNPs before and after MTS grafting ( n = 3 biologically independent samples), EE encapsulation efficiency. E TEM image of 6F-M-LNPs. Scale bar: 200 nm. F Mitochondrial gene delivery of different F-LNPs detected by CLSM. Scale bar: 10 μm. Mitochondria (Mitotracker Green probe): green; gene cargo (Cy5-pDNA): red. White arrows: Cy5-pDNA in the cytosol. G Pearson’s correlation coefficient between Cy5-pDNA and mitochondria ( n = 3 biologically independent samples). H The mitochondrial targeting of different F-LNPs detected by MFI of Cy5-pDNA in extracted mitochondria ( n = 3 biologically independent samples). I Detection on key mitochondrial membrane proteins (representative images from n = 3 independent experiments). J The mtGFP transfection after gene silencing of Tomm20 and Tomm22 ( n = 3 biologically independent samples). K Mitochondrial colocalization of 6F-M-LNP/Cy5-pDNA observed by Multi-SIM (representative images from n = 3 independent experiments). Outer mitochondrial membranes were labeled by Tomm20-mEmerald transfection. Inner mitochondrial membranes were labeled by Mitotracker Red probe. L CLSM images showing 6F-M-LNP/Cy3-pDNA localization inside the mitochondria (representative images from n = 3 independent samples). Outer mitochondrial membranes (mouse mAb to TOMM20): green; mitochondrial matrix proteins (rabbit pAb to SDHA): red; Cy3-pDNA: blue. M Schematic illustration of mitochondrial targeting behavior of 6F-M-LNPs. A and M was created with BioRender.com. Data are presented as mean ± SD. One-way ANOVA with Tukey’s multiple comparisons test (two-tailed; B , C , G , H , J ) was used to calculate the statistical significance.

Article Snippet: To investigate MTS-mediated interactions between 6F-M-LNPs and mitochondrial proteins, mitochondrial protein lysates were prepared and incubated with either 6F-M-LNPs or 6F-LNPs for 12 h. Key mitochondrial membrane proteins, including TOMM20, TOMM22, TOMM40, and TOMM70, were further validated through western blot analysis [Mouse mAb to TOMM20, 1:5000, ABclonal, #A27799; Rabbit mAb to TOMM22, 1:1000, ABclonal, #A9666; Rabbit mAb to TOMM40, 1:3000, ABclonal, #A24644; Rabbit mAb to TOMM70, 1:1000, ABclonal, #A21210].

Techniques: Formulation, Transfection, Encapsulation, Membrane, Labeling, Two Tailed Test

Journal: Antioxidants

Article Title: Culture of Bovine Aortic Endothelial Cells in Galactose Media Enhances Mitochondrial Plasticity and Changes Redox Sensing, Altering Nrf2 and FOXO3 Levels

doi: 10.3390/antiox13070873

Figure Lengend Snippet: Effect of glucose- or galactose-containing medium on mitochondrial dynamic and intercellular variability in BAEC (P4-6). ( A ) Representative image of immunofluorescence from Tomm22 (green) and DAPI (blue) in BAEC for 24 h; the white bars represent 50 μm. ( B ) Quantification of mitochondrial total for ( C ) Mitochondrial fission. Intercellular variability was performed by standard deviation for ( D ) mitochondrial total and ( E ) mitochondrial fission. Each independent experiment was performed using cells in the same cell passage exposed to glucose or galactose media. Data in graphs represent mean ± SEM (n = 4). * p < 0.05, ** p < 0.01 indicates a statistical difference between the groups of glucose (Glu or dashed line) and galactose (Gal or black bars), # p < 0.05, ## p < 0.01 indicates time-dependent statistical difference between the responses to Glu and Gal by two-way ANOVA, followed by Bonferroni’s post-hoc test.

Article Snippet: Immunofluorescence (IF)—BAEC were grown on coverslips in 24-well culture (1 × 105 cells/well) plates and submitted to the glycolytic (glucose) or the oxidative (galactose) protocol for 3, 6, 12, 24, or 48 h. At the end of the incubation period, the cells were fixed with 3.7% formaldehyde, permeabilized with 0.1% Triton, and then incubated consecutively with a primary antibody directed against Tomm22 (1:200, HPA003037, MERCK, Darmstadt, Germany) for mitochondrial dynamics analysis and Nrf2 (1:200, PA1-38312, Thermo Fisher, Waltham, MA, USA) and FOXO3 (1:100, #9467, Cell signaling) redox-related transcription factors, and then incubated with a secondary antibody (−IgG rabbit ALEXA-488 conjugate, 1:2500).

Techniques: Immunofluorescence, Standard Deviation

Journal: Autophagy

Article Title: In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy

doi: 10.1080/15548627.2017.1403716

Figure Lengend Snippet: CSNK2 phosphorylates TOMM22 and the absence of Csnk2b compromises CSNK2 catalytical activity and protein amount, but neither is required for TOMM complex biogenesis nor mitochondrial protein import. (A) Mouse TOMM22 was purified and used for in vitro radio-isotope-assisted phosphorylation with different kinases. The image of the autoradiogram shows that mouse TOMM22 was only phosphorylated in the presence of protein kinase CSNK2 and is not phosphorylated by any of the other kinases used. The amount of histidine-tagged TOMM22 served as loading control. (B) In vitro radio-isotope-assisted phosphorylation of TOMM22 is less efficient by muscle lysates of csnk2b∆/∆, HSA-Cre mice in comparison with muscles of control litters. The amount of recombinant TOMM22 was adjusted by measuring the total protein amount and verified by Coomassie-stained SDS-PAGE. (C) Alignment of mouse and yeast TOMM22/Tom22 primary structure stretches. Potential mouse TOMM22 phosphosites in comparison with phosphosites in yeast Tom22 are depicted by asterisks. The panel also depicts kinase prediction scores for mouse phosphosites serine 15, threonine 43 and serine 45, obtained as potential CSNK2 target sites with ScanSite 3, Disphos 1.3, NetPhosK 1.0 and NetPhos 2. The target sequence of CSNK2 is known to be represented by [S-X-X-(D/E/pS/pY)].39 (D) In vitro phosphorylation experiments were performed with purified mouse TOMM22 wild-type protein and its alanine mutants together with recombinant CSNK2 using radiolabeled ATP. (E) T7 tagged TOMM22 wild-type and alanine-mutant expression plasmids were transfected into cultured cells, protein lysates immunprecipitated by a T7-specific antibody, precipitates were resolved by SDS-PAGE, and western blot membranes incubated with either a T7 or a TOMM22-p-S15-specific antibody. Note, the TOMM22-p-S15-specific antibody detects wild-type TOMM22, but not the TOMM22S15A or TOMM22S15A,T43A mutants. (F) The amount of catalytic activity-containing CSNK2A1 and CSNK2A2 subunits was determined in the absence of Csnk2b in skeletal muscle fiber lysates. Skeletal muscles soleus and tibialis anterior were used from approximately 2- (n = 3 mice per genotype) and 6- to 8-mo-old (n = 3 mice per genotype) mice. Obviously, CSNK2B protein is absent in csnk2b∆/∆, HSA-Cre muscle lysates. ACTN2 served as loading control. (G and H) Graphs represent protein amounts of CSNK2 subunits which were analyzed before by western blot (F). Note, in response to the absence of Csnk2b, protein amounts of CSNK2A1 and CSNK2A2 subunits are delicately balanced and seem to be adjusted in a muscle-type specific manner. (I) To determine the capacity of mitochondria for importing precursor proteins the in organello import assay with radiolabeled precursor proteins was used.72 [35S]-radiolabeled yeast proteins Cox4, Mdh1 and Atp2 were individually imported into mitochondria (Δψ, membrane potential). Mitochondria were treated with proteinase K and analyzed by SDS-PAGE. p, precursor; m, mature. Import into mitochondria after the longest import time was set to 100% (control). Note, all mitochondrial precursor (p) proteins are imported into mitochondria and processed to shorter mature (m) size with similar time kinetic between control and the csnk2b∆/∆, HSA-Cre indicating mitochondrial protein import in vitro being unaffected. (J) Mitochondria were isolated from skeletal muscles of adult wild-type or csnk2b∆/∆, HSA-Cre mice and equal amounts of native TOMM complexes were resolved by blue-native gels (BN) which are used to separate native protein complexes. After western blot, different TOMM family members within native TOMM complexes were detected by specific antibodies as shown by representative images. The amount of these TOMM family members is similar between TOMM complexes from mitochondria of wild-type or csnk2b∆/∆, HSA-Cre muscles, indicating proper biogenesis of TOMM complexes.

Article Snippet: Additionally used antibodies: from Santa Cruz Biotechnology Inc.: TOMM20 (sc-11415; 1:3,000), TOMM40 (sc-11414), SLC25A31/ANT4 (detects in mouse also SLC25A4 / ANT1, SLC25A5 / ANT2) (sc-11433), PRKN/PARK2 (sc-32282); from Sigma-Aldrich Chemie; ACTN2 (A 7811; 1:10,000); from Abcam: PRKN/PARK2 (ab15954), SQSTM1 (ab56416; 1:5,000), MFN2 (ab56889; 1:5,000), VDAC1/2/3 (ab15895; 1:5,000), SDHA (ab14715; 1:20,000); from Abnova/Biozol: TOMM22 (H00056993-M01); from Novus Biologicals: PINK1 (BC100-494); from Proteintech: OPTN (10837-1-AP); from Merck: anti-phospho-S65 Ubiquitin (ABS1513); from Enzo Life Sciences: Mono- and polyubiquitinated conjugates (FK2); from Novagen: T7 (69522; 1.10,000); anti-p-S15-AA (generated in the lab of Dr. Michael Marber, UK); anti-CSNK2A1 (1:500) and anti-CSNK2A2 (1:100), both generated in the lab of Dr. Olaf-Georg Issinger (Odense, Denmark).

Techniques: Activity Assay, Purification, In Vitro, Recombinant, Staining, SDS Page, Sequencing, Mutagenesis, Expressing, Transfection, Cell Culture, Western Blot, Incubation, Isolation

Journal: Autophagy

Article Title: In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy

doi: 10.1080/15548627.2017.1403716

Figure Lengend Snippet: PINK1 accumulates as a full-length 65-kDa protein in csnk2b∆/∆, HSA-Cre diaphragms and preferentially binds to phosphomimetic TOMM22. (A) Representative immunoblot images showing that diaphragms of csnk2b∆/∆, HSA-Cre mice in comparison with controls contain less of processed PINK1 (53 kDa) and more of the full-length PINK1 (65 kDa). (B) Protein levels of unprocessed and processed PINK1 as shown in (A) were quantified by ImageJ and normalized to ACTN2. N = 3 mice per genotype. SDS-PAGE and western blot was repeated 3 to 5 times per protein lysate. (C) Representative western blot membrane images demonstrated interaction of PINK1 with all TOMM receptors, TOMM20, 22, 70, and the import channel TOMM40. GFP-T7 was used as a negative control. (D) Western blot membrane image demonstrated that the mitochondrial targeting sequence (MTS, spanning the area from amino acid 1 to 94) of PINK1 interacts with TOMM22. (E) Representative TOMM22 immunoblot images of GST affinity isolations. GST-PINK1-MTS was utilized to affinity isolate individually wild-type, inactive alanine- or phosphomimetic-TOMM22 mutants. Note, TOMM22S15D,T43D or TOMM22S15E,T43E bound significantly stronger to PINK1-MTS in comparison with wild-type TOMM22 or TOMM22S15A,T43A. N = 3 independent experiments. (F) Protein levels of wild-type and mutant TOMM22 as shown in (E) were quantified using ImageJ, normalized to 1/10 input. Note, PINK1 bound significantly more phosphomimetic TOMM22, than wild-type or alanine-mutant TOMM22 proteins.

Article Snippet: Additionally used antibodies: from Santa Cruz Biotechnology Inc.: TOMM20 (sc-11415; 1:3,000), TOMM40 (sc-11414), SLC25A31/ANT4 (detects in mouse also SLC25A4 / ANT1, SLC25A5 / ANT2) (sc-11433), PRKN/PARK2 (sc-32282); from Sigma-Aldrich Chemie; ACTN2 (A 7811; 1:10,000); from Abcam: PRKN/PARK2 (ab15954), SQSTM1 (ab56416; 1:5,000), MFN2 (ab56889; 1:5,000), VDAC1/2/3 (ab15895; 1:5,000), SDHA (ab14715; 1:20,000); from Abnova/Biozol: TOMM22 (H00056993-M01); from Novus Biologicals: PINK1 (BC100-494); from Proteintech: OPTN (10837-1-AP); from Merck: anti-phospho-S65 Ubiquitin (ABS1513); from Enzo Life Sciences: Mono- and polyubiquitinated conjugates (FK2); from Novagen: T7 (69522; 1.10,000); anti-p-S15-AA (generated in the lab of Dr. Michael Marber, UK); anti-CSNK2A1 (1:500) and anti-CSNK2A2 (1:100), both generated in the lab of Dr. Olaf-Georg Issinger (Odense, Denmark).

Techniques: Western Blot, SDS Page, Negative Control, Sequencing, Mutagenesis

Journal: Autophagy

Article Title: In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy

doi: 10.1080/15548627.2017.1403716

Figure Lengend Snippet: Phosphomimetic and inactive TOMM22 proteins correlate with the number of SQSTM1-associated accumulations and oxygen consumption rates in Csnk2b ablated muscle cells. (A) Representative images of SQSTM1 immunostain of longitudinal sections of soleus muscle which were electroporated in vivo with phosphomimetic TOMM22 and shRNA transcribing plasmids to knockdown endogenous Tomm22. Note, a higher number of SQSTM1-associated accumulations was visible in csnk2b∆/∆, HSA-Cre soleus muscle fibers. This number decreased in csnk2b∆/∆, HSA-Cre muscle fibers which were electroporated with a phosphomimetic TOMM22 mutant (TOMM22S15E,T43E); but not after electroporation with wild-type TOMM22. Contemporary electroporation of an RFP-nuclear localization signal (nls) expression plasmid served for identification of the electroporated muscle fiber areas. (B) Quantification of the number of SQSTM1-associated accumulations in control or csnk2b∆/∆, HSA-Cre muscle cells which were electroporated with either wild-type or phosphomimetic TOMM22. N = 3 mice per genotype. Note that expression of phosphomimetic TOMM22 lowered the number of SQSTM1-associated accumulations in csnk2b∆/∆, HSA-Cre muscle fibers to almost wild-type levels. (C and D) Cultured C2C12 muscle cells were transfected with shRNA to knock down endogenous Tomm22 expression and with either wild-type or inactive Tomm22 expression plasmids. Cells were then immunostained for SQSTM1, DAPI and monitored for GFP expression encoded by shRNA transcribing plasmids. N = 3 independent experiments. (C). Note, the number of SQSTM1-associated aggregates is significantly higher in muscle cells expressing TOMM22S15A,T43A in comparison with wild-type TOMM22 (C). Number of SQSTM1-associated aggregates per cell was quantified and is depicted as graph (D). (E) Cultured primary muscle cells were untransfected or transfected with Tomm22 wild-type or Tomm22S15E,T43E expression plasmids, both together with shRNA plasmid to reduce endogenous Tomm22 expression, lysed, resolved by SDS-PAGE, western blotted, and membranes were immunostained with antibodies specific for different mitochondrial proteins. Representative images of immunostains demonstrated that the decreased mitochondrial protein amount in csnk2b∆/∆, HSA-Cre muscle cells, in comparison with controls, was rescued to normal values by transfection of a phosphomimetic TOMM22 mutant. (F) Quantification of protein bands as seen in (E) using ImageJ. All numbers were normalized to ACTN2. N = 3 independent experiments. (G) Graphs show oxygen consumption rates (OCR) in C2C12 cells which were transfected with expression plasmids encoding wild-type Tomm22 or inactive Tomm22S15A,T43A, together with GFP, and FACS sorted prior to OCR measurement by Seahorse methodology. N = 3 independent experiments. (H) OCRs measured with cultured primary muscle cells from wild-type or csnk2b∆/∆, HSA-Cre mice. Cells were transfected with expression plasmids as indicated, together with a GFP expression plasmid. Like in (G), transfected cells were FACS sorted by their fluorophore prior to Seahorse measurements. Note, constitutively expressed Cre recombinase was transfected to all cells to ensure deletion of floxed Csnk2b in csnk2b∆/∆, HSA-Cre muscle cells which occurred 48 to 72 h prior to the seahorse measurements.

Article Snippet: Additionally used antibodies: from Santa Cruz Biotechnology Inc.: TOMM20 (sc-11415; 1:3,000), TOMM40 (sc-11414), SLC25A31/ANT4 (detects in mouse also SLC25A4 / ANT1, SLC25A5 / ANT2) (sc-11433), PRKN/PARK2 (sc-32282); from Sigma-Aldrich Chemie; ACTN2 (A 7811; 1:10,000); from Abcam: PRKN/PARK2 (ab15954), SQSTM1 (ab56416; 1:5,000), MFN2 (ab56889; 1:5,000), VDAC1/2/3 (ab15895; 1:5,000), SDHA (ab14715; 1:20,000); from Abnova/Biozol: TOMM22 (H00056993-M01); from Novus Biologicals: PINK1 (BC100-494); from Proteintech: OPTN (10837-1-AP); from Merck: anti-phospho-S65 Ubiquitin (ABS1513); from Enzo Life Sciences: Mono- and polyubiquitinated conjugates (FK2); from Novagen: T7 (69522; 1.10,000); anti-p-S15-AA (generated in the lab of Dr. Michael Marber, UK); anti-CSNK2A1 (1:500) and anti-CSNK2A2 (1:100), both generated in the lab of Dr. Olaf-Georg Issinger (Odense, Denmark).

Techniques: In Vivo, shRNA, Mutagenesis, Electroporation, Expressing, Plasmid Preparation, Cell Culture, Transfection, SDS Page, Western Blot

Journal: Autophagy

Article Title: In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy

doi: 10.1080/15548627.2017.1403716

Figure Lengend Snippet: Sketch hypothesizes a mechanism for impaired mitochondrial homeostasis and mitophagy in wild type and csnk2b∆/∆, HSA-Cre muscle fibers. (Left) TOMM22 in its phosphorylated state facilitates import of PINK1 into the inner mitochondrial membrane. PINK1 in the inner membrane will be degraded by PARL, but also lead via phosphorylation of NDUFA10 to the stimulation of oxidative phosphorylation (OXPHOS) activity. Note, it remains to be determined whether PINK1 directly phosphorylates NDUFA10. (Right) In csnk2b∆/∆, HSA-Cre cells, lack of phosphorylated TOMM22 impairs PINK1 import and induce PARK2-mediated mitophagy. In addition, the lack of NDUFA10 phosphorylation will reduce OXPHOS activity and therefore lower the membrane potential of mitochondria. We speculate that accordingly loss of TOMM22 phosphorylation fosters PINK1 to accumulate on the outer membrane of mitochondria.

Article Snippet: Additionally used antibodies: from Santa Cruz Biotechnology Inc.: TOMM20 (sc-11415; 1:3,000), TOMM40 (sc-11414), SLC25A31/ANT4 (detects in mouse also SLC25A4 / ANT1, SLC25A5 / ANT2) (sc-11433), PRKN/PARK2 (sc-32282); from Sigma-Aldrich Chemie; ACTN2 (A 7811; 1:10,000); from Abcam: PRKN/PARK2 (ab15954), SQSTM1 (ab56416; 1:5,000), MFN2 (ab56889; 1:5,000), VDAC1/2/3 (ab15895; 1:5,000), SDHA (ab14715; 1:20,000); from Abnova/Biozol: TOMM22 (H00056993-M01); from Novus Biologicals: PINK1 (BC100-494); from Proteintech: OPTN (10837-1-AP); from Merck: anti-phospho-S65 Ubiquitin (ABS1513); from Enzo Life Sciences: Mono- and polyubiquitinated conjugates (FK2); from Novagen: T7 (69522; 1.10,000); anti-p-S15-AA (generated in the lab of Dr. Michael Marber, UK); anti-CSNK2A1 (1:500) and anti-CSNK2A2 (1:100), both generated in the lab of Dr. Olaf-Georg Issinger (Odense, Denmark).

Techniques: Activity Assay

Journal: Autophagy

Article Title: In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2/CK2 controls mitophagy

doi: 10.1080/15548627.2017.1403716

Figure Lengend Snippet: Plasmids, primers, mutagenesis

Article Snippet: Additionally used antibodies: from Santa Cruz Biotechnology Inc.: TOMM20 (sc-11415; 1:3,000), TOMM40 (sc-11414), SLC25A31/ANT4 (detects in mouse also SLC25A4 / ANT1, SLC25A5 / ANT2) (sc-11433), PRKN/PARK2 (sc-32282); from Sigma-Aldrich Chemie; ACTN2 (A 7811; 1:10,000); from Abcam: PRKN/PARK2 (ab15954), SQSTM1 (ab56416; 1:5,000), MFN2 (ab56889; 1:5,000), VDAC1/2/3 (ab15895; 1:5,000), SDHA (ab14715; 1:20,000); from Abnova/Biozol: TOMM22 (H00056993-M01); from Novus Biologicals: PINK1 (BC100-494); from Proteintech: OPTN (10837-1-AP); from Merck: anti-phospho-S65 Ubiquitin (ABS1513); from Enzo Life Sciences: Mono- and polyubiquitinated conjugates (FK2); from Novagen: T7 (69522; 1.10,000); anti-p-S15-AA (generated in the lab of Dr. Michael Marber, UK); anti-CSNK2A1 (1:500) and anti-CSNK2A2 (1:100), both generated in the lab of Dr. Olaf-Georg Issinger (Odense, Denmark).

Techniques: Sequencing, shRNA