Journal: Cellular & molecular biology letters

Article Title: Reciprocal negative feedback between Prrx1 and miR-140-3p regulates rapid chondrogenesis in the regenerating antler.

doi: 10.1186/s11658-024-00573-x

Figure Lengend Snippet: Fig. 4 Characteristics of tissue layers of the antler growth center and isolated RM cells. A Immunofluorescence assay of CD73, CD90, Nestin, CD34, and Prrx1 (red color) in the RM, PC, and CA layers, respectively. B Third passage of cultured cells from the RM layer were identified using mesenchymal stem cell markers: CD73 and CD90 (red), Nestin and CD34 (green), respectively; nuclei were stained blue with DAPI. C Chondrogenic differentiation of RM cells, Alcian blue, and Col II immunofluorescence staining. D Osteogenic differentiation of RM cells with Alizarin red staining. E Adipogenic differentiation of RM cells with Oil Red O staining (scale bars, 125 μm and magnification ×200)

Article Snippet: The cells and tissues were fixed, permeabilized, blocked, and incubated overnight with primary antibodies: CD90 (1:300, proteintech, USA, 66766-1-lg), CD73 (1:1000, proteintech, USA, 12231- 1-AP), Nestin (1:300, BIOSS, China, bs-0008R), CD34 (1:300, proteintech, USA, 14486- 1-AP), and Prrx1 (1:200, Absin, China, abs134576).

Techniques: Isolation, Immunofluorescence, Cell Culture, Staining

Journal: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology

Article Title: Differential expression of ORAI channels and STIM proteins in renal cell carcinoma subtypes: implications for metastasis and therapeutic targeting

doi: 10.4196/kjpp.24.126

Figure Lengend Snippet: (A, C) FPKM for Orai3 according to normal and RCC grades (Stage I, II, III, and IV) in clear cell RCC (ccRCC) and papillary RCC (pRCC), respectively. Box whisker plots express the minimum, median, and maximum values of FPKM (expressed as log(expr + 1)), where FPKM was adjusted using a scaling factor instead of total mapped reads to remove a million units. ***p ≤ 0.001 of one-way ANOVA (normal vs . tumor stages). (B, D) Kaplan–Meler survival analysis comparing females (left) and males (right) in the low and high mRNA levels of Orai3 in ccRCC and pRCC, respectively. The cut-off value for Orai3 in ccRCC is 13.5, and in pRCC is 16.87. (E, G) Correlation analysis between gene copy number (log2-transformed values) of STIM2 and Orai3 in ccRCC (total n = 355) and pRCC (total n = 241), respectively. The linear regression line with a 95% confidence interval and the Spearman r correlation coefficient. (F, H) Kaplan–Meler survival analysis comparing males and females with high Orai3 and low STIM2 mRNA levels in ccRCC and pRCC, respectively. The cut-off value for Orai3 is 13, and for STIM2 is 4.5. p-values were determined by a log-rank test (B, D, F, and H).

Article Snippet: The primary antibodies used for immunoblotting were: β-actin (1:3,000, #sc-47778) and Cyclin D1 (1:200, #sc-246) from Santa Cruz Biotechnology; STIM1 (1:1,000, #S6072) from Sigma Aldrich; p-FAK (Tyr397) (1:1,000, #8556) and t-FAK (1:1,000, #13009) from Cell Signaling Technology Inc.; and STIM2 (1:500, #21192-1-AP) from ProteinTech.

Techniques: Whisker Assay, Transformation Assay

Journal: Journal of Neuroinflammation

Article Title: VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses

doi: 10.1186/s12974-025-03645-7

Figure Lengend Snippet: VSIG2 expression on immune cells. Splenocytes from C57BL/6 mice were freshly harvested and stained with anti-VSIG2 monoclonal antibody (mAb) or isotype control, as well as antibodies targeting CD4, CD8, CD19, B220, CD11c, F4/80, or CD11b to identify different immune cell populations. To activate B cells, dendritic cells (DCs), monocytes, and macrophages, splenocytes were incubated with LPS (5 µg/ml) for 3 days. For T cell activation, splenocytes were incubated with anti-CD3 (1 µg/ml) and anti-CD28 (0.5 µg/ml) antibodies for 24 h. a Representative flow cytometry profiles showing mVSIG2 protein expression on resting and activated immune cells. b Statistical analysis of VSIG2 protein expression on resting and activated immune cells ( n = 3 independent experiments). Data are presented as mean ± SD. Statistical significance was assessed by two-way ANOVA with Tukey’s test (a-d) or two-sided Student’s t test (e, f)

Article Snippet: Tissue sections were incubated overnight at 4 °C with the following primary antibodies: anti-occludin (1:200; 66378-1-Ig, Proteintech), anti-GFAP (1:200; 60190-1-Ig, Proteintech), anti-IBA1(1:200; 10904-1-AP, Proteintech), anti-CD3 (1:200; 17617-1-AP, Proteintech), anti-CD4(1:200; 67786-1-Ig, Proteintech), anti-CD8 (1:200; 0108-7, Huabio).

Techniques: Expressing, Staining, Control, Incubation, Activation Assay, Flow Cytometry

Journal: Journal of Neuroinflammation

Article Title: VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses

doi: 10.1186/s12974-025-03645-7

Figure Lengend Snippet: The effects of hVSIG2-Ig protein on T cell activation and proliferation in vitro. a , Splenic cells from C57BL/6 mice were stimulated with anti-CD3 (1 µg/ml) and anti-CD28 (0.5 µg/ml) antibodies in the presence of graded doses of hVSIG2-Ig (1600 ng/ml, 3200 ng/ml, and 6400 ng/ml) or equimolar amounts of control Ig for 24–72 h. b , Representative flow cytometric analysis of CD69, CD25, and CD40L expression in CD4 + and CD8 + T cells, and ( c ) statistical analysis of T cell activation ( n = 3 independent experiments). d , Representative flow cytometric analysis of CFSE dilution in CD4 + and CD8 + T cells, and ( e ) statistical analysis of T cell proliferation ( n = 3 independent experiments). f , Representative flow cytometric analysis of naïve and effector T cells, with ( g ) statistical analysis of CD44loCD62Lhi naïve T cells and CD44hiCD62Llo effector T cells for both CD4 + /CD8 + T cells ( n = 3 independent experiments). Data are presented as mean ± SD. Statistical significance was assessed by two-way ANOVA with Tukey’s test ( a-g )

Article Snippet: Tissue sections were incubated overnight at 4 °C with the following primary antibodies: anti-occludin (1:200; 66378-1-Ig, Proteintech), anti-GFAP (1:200; 60190-1-Ig, Proteintech), anti-IBA1(1:200; 10904-1-AP, Proteintech), anti-CD3 (1:200; 17617-1-AP, Proteintech), anti-CD4(1:200; 67786-1-Ig, Proteintech), anti-CD8 (1:200; 0108-7, Huabio).

Techniques: Activation Assay, In Vitro, Control, Expressing

Journal: Journal of Neuroinflammation

Article Title: VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses

doi: 10.1186/s12974-025-03645-7

Figure Lengend Snippet: Role of GBP2 in VSIG2-mediated T cell activation. Purified CD4 + T cells were isolated from splenocytes of C57BL/6 mice using magnetic bead sorting. Cells were then plated on anti-CD3 antibody (1 µg/ml) and anti-CD28 (0.5 µg/ml) antibodies pre-coated plates and incubated for 24 h in the presence of hVSIG2-Ig (6400 ng/ml) or an equimolar concentration of control Ig. After incubation, the cells were harvested for RNA-Seq and DIA proteomic sequencing ( n = 3 independent experiments). a CD4⁺ T cells were isolated from C57BL/6 mouse spleens by magnetic bead sorting, transduced with lentiviral vectors for GBP2 knockdown or overexpression, and cultured for 48 h. Cells were then transferred to 96-well plates pre-coated with anti-CD3/CD28 antibodies and hVSIG2-Ig for an additional 24 h. b Immunoblot analysis of GBP2 knockdown efficiency in CD4⁺ T cells ( n = 3 independent experiments). c Representative flow cytometry analysis of CD69 expression in CD4⁺ T cells, with statistical quantification of T cell activation ( n = 3 independent experiments). d Immunoblot analysis of p-STAT1, IRF1, and CD69 protein levels in GBP2 knockdown CD4⁺ T cells, with ( e ) semiquantitative analysis ( n = 3 independent experiments). f Immunoblot analysis of GBP2 overexpression in CD4⁺ T cells ( n = 3 independent experiments). g Representative flow cytometry analysis of CD69 expression in CD4⁺ T cells, with statistical quantification of T cell activation ( n = 3 independent experiments). h Immunoblot analysis of p-STAT1, IRF1, and CD69 protein levels in GBP2 overexpressing CD4⁺ T cells, with ( i ) densitometric quantification ( n = 3 independent experiments). Data are presented as mean ± SD. Statistical significance was assessed by two-way ANOVA with Tukey’s test

Article Snippet: Tissue sections were incubated overnight at 4 °C with the following primary antibodies: anti-occludin (1:200; 66378-1-Ig, Proteintech), anti-GFAP (1:200; 60190-1-Ig, Proteintech), anti-IBA1(1:200; 10904-1-AP, Proteintech), anti-CD3 (1:200; 17617-1-AP, Proteintech), anti-CD4(1:200; 67786-1-Ig, Proteintech), anti-CD8 (1:200; 0108-7, Huabio).

Techniques: Activation Assay, Purification, Isolation, Incubation, Concentration Assay, Control, RNA Sequencing, Sequencing, Transduction, Knockdown, Over Expression, Cell Culture, Western Blot, Flow Cytometry, Expressing

Journal: Journal of Neuroinflammation

Article Title: VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses

doi: 10.1186/s12974-025-03645-7

Figure Lengend Snippet: hVSIG2-Ig alleviates experimental autoimmune encephalomyelitis (EAE) severity in mice. 6–8 weeks old female C57BL/6 mice were immunized with 200 µg of MOG₃₅‒₅₅ emulsified in complete Freund’s adjuvant (CFA) and 500 ng of purified pertussis toxin. Mice received intraperitoneal injections of 25 µg hVSIG2-Ig or control Ig three times weekly for 5 weeks, with EAE progression monitored over 42 days. a Western blot analysis of VSIG2 expression i n spleen and spinal cord tissues from wild-type (WT) and EAE mice ( n = 3 independent experiments). b Mean clinical scores of EAE model mice ( n = 12 mice each group). c H&E and LFB staining of spinal cord sections, with ( d ) quantitative histopathological scoring ( n = 6 mice). e Immunofluorescence staining of spinal cord tissues (GFAP: green, Iba1: red, CD4: red, CD8: red). f, Quantification of GFAP, Iba1, CD4, and CD8 immunofluorescence intensity ( n = 6 mice). g Representative flow cytometric analysis of CD69, CD25, CD40L expression in spinal cord CD4⁺ and CD8⁺ T cells, with statistical analysis of T cell activation ( n = 6 mice). h Representative flow cytometry analysis of Ki67 expression in spinal cord CD4⁺ and CD8⁺ T cells, with statistical analysis of T cell proliferation ( n = 6 mice). i Flow cytometry analysis and quantification of CD45⁺CD4⁺CD25⁺FoxP3⁺ and CD45⁺CD4⁺FoxP3⁺ regulatory T cells (Tregs) ( n = 6 mice). j Intracellular cytokine staining and statistical analysis of TNF-α, IFN-γ, IL-17 A, and IL-4 in CD4⁺ T cells ( n = 6 mice). k Cytokine microsphere array (CBA) analysis of TNF-α, IFN-γ, IL-17 A, and IL-4 in serum ( n = 6 mice). l Kaplan-Meier survival curves comparing survival rates between the two groups ( n = 12 mice each group). Data are presented as mean ± SD. Statistical significance was assessed by two-sided Student’s t test

Article Snippet: Tissue sections were incubated overnight at 4 °C with the following primary antibodies: anti-occludin (1:200; 66378-1-Ig, Proteintech), anti-GFAP (1:200; 60190-1-Ig, Proteintech), anti-IBA1(1:200; 10904-1-AP, Proteintech), anti-CD3 (1:200; 17617-1-AP, Proteintech), anti-CD4(1:200; 67786-1-Ig, Proteintech), anti-CD8 (1:200; 0108-7, Huabio).

Techniques: Adjuvant, Purification, Control, Western Blot, Expressing, Staining, Immunofluorescence, Activation Assay, Flow Cytometry

Journal: Journal of Neuroinflammation

Article Title: VSIG2 as a novel immunosuppressive ligand interacts with Nectin-2 to regulate T cell responses

doi: 10.1186/s12974-025-03645-7

Figure Lengend Snippet: Anti-VSIG2 VHH antibody suppresses pancreatic cancer progression in mice. C57BL/6 mice were subcutaneously inoculated with 1 × 10⁶ Pan02 pancreatic cancer cells. When tumor volume reached ~ 100 mm³, mice were intratumorally injected with anti-VSIG2 VHH nanoantibody or control antibody (200 µg/dose, 3 times weekly). Tumor growth was monitored daily by caliper measurements, and tumors were harvested on day 12 for analysis. a Representative images of tumors from both groups ( n = 7 mice). b Tumor volume kinetics over time, with comparisons of tumor volume at day 12 and tumor weight between groups ( n = 13 mice). c H&E and immunofluorescence staining of tumor sections (CD4: green, CD8: red), with d quantitative analysis of immune cell infiltration ( n = 6 mice). e Representative flow cytometry analysis of CD69, CD25, and CD40L expression in tumor-infiltrating CD4⁺ and CD8⁺ T cells, with statistical analysis of T cell activation ( n = 13 mice). f Representative flow cytometry analysis of Ki67 expression in tumor-infiltrating CD4⁺ and CD8⁺ T cells, with statistical analysis of T cell proliferation ( n = 13 mice). g Flow cytometry analysis and quantification of CD45⁺CD4⁺CD25⁺FoxP3⁺ and CD45⁺CD4⁺FoxP3⁺ regulatory T cells (Tregs) in tumors ( n = 13 mice). h Cytokine microsphere array (CBA) analysis of TNF-α, IFN-γ, IL-17 A, IL-2, and IL-4 in serum ( n = 9 mice). Data are presented as mean ± SD. p values were determined by two-sided Student’s t test

Article Snippet: Tissue sections were incubated overnight at 4 °C with the following primary antibodies: anti-occludin (1:200; 66378-1-Ig, Proteintech), anti-GFAP (1:200; 60190-1-Ig, Proteintech), anti-IBA1(1:200; 10904-1-AP, Proteintech), anti-CD3 (1:200; 17617-1-AP, Proteintech), anti-CD4(1:200; 67786-1-Ig, Proteintech), anti-CD8 (1:200; 0108-7, Huabio).

Techniques: Injection, Control, Immunofluorescence, Staining, Flow Cytometry, Expressing, Activation Assay

Journal: PLoS Genetics

Article Title: Asymmetry of the Budding Yeast Tem1 GTPase at Spindle Poles Is Required for Spindle Positioning But Not for Mitotic Exit

doi: 10.1371/journal.pgen.1004938

Figure Lengend Snippet: A-C: Bacterially purified GST-Bub2 or GST-Bub2-Q132L, MBP-Bfa1 and 6xHis-Tem1 proteins were used to measure the kinetics of hydrolysis+dissociation (γ[ 32 P]GTP) or dissociation only (γ[ 35 S]GTP) using a filter binding assay (see ). Graphs show average values and standard deviations from three independent experiments. D: Exponentially growing cultures of the indicated strains were shifted to nocodazole containing medium at t = 0. Cell samples were withdrawn at the indicated time for FACS analysis of DNA contents. E: The percentage of cells with binucleate cell bodies accompanied or not by a checkpoint defect (indicated by re-budding in the absence of proper chromosome segregation) was scored in cycling cultures of the indicated strains shifted either to 14°C for 16h (left graph) or to 37°C for 3h (right graph). F-G: Exponentially growing cells with the indicated genotypes were arrested in G1 by α-factor and released into fresh medium at time 0. At 70’ after release α-factor was re-added to prevent cells from entering a second cell cycle. Cell samples were collected for FACS analysis of DNA contents (F) and for tubulin staining by indirect immunofluorescence (G). H: Cells were treated as in (F-G). TCA extracts were prepared from cell samples at the indicated time points to monitor kinetics of Bfa1-HA6 phosphorylation and Clb2 accumulation and degradation by western blot analysis. Pgk1 was used as loading control. I: Protein extracts from cells expressing the indicated tagged proteins were used for immunoprecipitation with an anti-HA affinity resin. Western blot analysis was then performed with anti-GFP and anti-HA antibodies. The input represents 1/25 th of the total extract used for each IP. J-K: Localization of eGFP- tagged Bub2/Bub2-Q132L, Tem1, Bfa1 (J) and Cdc15-GFP (K) was analysed by fluorescence microscopy after formaldehyde fixation.

Article Snippet: Proteins transferred to Protran membranes (Schleicher & Schuell) were probed with anti-PK mouse monoclonal antibodies for PK-tagged Bub2, with anti-GFP rat monoclonal antibodies for GFP-tagged Tem1, Bub2 and Bfa1 (Chromotek) and with an anti-HA monoclonal antibody (12CA5).

Techniques: Purification, Filter-binding Assay, Staining, Immunofluorescence, Western Blot, Expressing, Immunoprecipitation, Fluorescence, Microscopy

Journal: PLoS Genetics

Article Title: Asymmetry of the Budding Yeast Tem1 GTPase at Spindle Poles Is Required for Spindle Positioning But Not for Mitotic Exit

doi: 10.1371/journal.pgen.1004938

Figure Lengend Snippet: A-B: Cycling cells co-expressing Spc72-Bfa1-eGFPand Spc42-mCherry to mark the SPB (upper panel) or co-expressing Tem1-eGFP and Tub1-GFP (to mark microtubules, lower panel) were analysed to study the distribution of Spc72-Bfa1-eGFP (A) and Tem1-eGFP (B) at SPBs in SPC72-BFA1 bfa1Δ cells. C-D: Cycling cells with the indicated genotypes were shifted into nocodazole containing medium (t = 0). Cell samples were withdrawn at the indicated times for FACS analysis of DNA contents. E: The percentage of cells with binucleate cell bodies accompanied or not by a SPOC defect was scored after propidium iodide staining of cycling cultures of cells with the indicated genotypes after shift to 14°C for 16h. The histograms on the right side represent the DNA contents of the same cells as measured by FACS analysis. F: Percentage of metaphase cells with Cdc15-GFP at 0, 1 or 2 SPBs was scored in the indicated strains after formaldehyde fixation. Metaphases were identified by means of the Tub1-mCherry co-expressed marker. G: Serial dilutions of stationary phase cultures of the indicated strains were spotted on YPD and incubated at the indicated temperature. H: Serial dilutions of stationary phase cultures of the indicated strains were spotted on YP medium containing either glucose or galactose and incubated at 25°C for 48h.

Article Snippet: Proteins transferred to Protran membranes (Schleicher & Schuell) were probed with anti-PK mouse monoclonal antibodies for PK-tagged Bub2, with anti-GFP rat monoclonal antibodies for GFP-tagged Tem1, Bub2 and Bfa1 (Chromotek) and with an anti-HA monoclonal antibody (12CA5).

Techniques: Expressing, Staining, Marker, Incubation

Journal: PLoS Genetics

Article Title: Asymmetry of the Budding Yeast Tem1 GTPase at Spindle Poles Is Required for Spindle Positioning But Not for Mitotic Exit

doi: 10.1371/journal.pgen.1004938

Figure Lengend Snippet: A: Bacterially purified 6XHis-Tem1 and 6XHis-Tem1-Q79L were loaded with γ[ 32 P]GTP either in the absence or in the presence of recombinant MBP-Bfa1 and incubated at 30°C for 10 minutes. The mixture was then added to GST-Bub2 or buffer alone and kinetics of GTP hydrolysis and dissociation was followed by a filter-binding assay (see details in ). Graphs show average values and standard deviations from three independent experiments. B: Wild type and TEM1-Q79L cells were arrested in G1 by α-factor and then released into fresh medium at 25°C (t = 0). Cell samples were withdrawn every 10’ to measure kinetics of budding and spindle formation/elongation after in situ immunostaining of tubulin. C: Actomyosin ring contraction has been visualized by live cell imaging of wild type and TEM1-Q79L expressing Myo1-GFP (n = 30). D: Logarithmically growing cultures of cells with the indicated genotypes were shifted into nocodazole containing medium (t = 0). DNA contents were analysed by flow cytometry at the indicated times. E: The percentage of cells with binucleate cell bodies accompanied or not by SPOC defect was scored after DAPI staining of cycling cells of the indicated strains shifted to 14°C for 16h. F: Logarithmically growing cultures of strains with the indicated genotypes were shifted to nocodazole containing medium (t = 0). DNA contents were analysed by flow cytometry at the indicated times. G: Serial dilutions of stationary phase cultures of the indicated strains were spotted on YPD or YP galactose plates and incubated at 30°C for 48h.

Article Snippet: Proteins transferred to Protran membranes (Schleicher & Schuell) were probed with anti-PK mouse monoclonal antibodies for PK-tagged Bub2, with anti-GFP rat monoclonal antibodies for GFP-tagged Tem1, Bub2 and Bfa1 (Chromotek) and with an anti-HA monoclonal antibody (12CA5).

Techniques: Purification, Recombinant, Incubation, Filter-binding Assay, In Situ, Immunostaining, Live Cell Imaging, Expressing, Flow Cytometry, Staining

Journal: PLoS Genetics

Article Title: Asymmetry of the Budding Yeast Tem1 GTPase at Spindle Poles Is Required for Spindle Positioning But Not for Mitotic Exit

doi: 10.1371/journal.pgen.1004938

Figure Lengend Snippet: List of non-essential genes implicated in microtubules dynamics or spindle positioning identified in the SGA screen with TEM1-Q79L .

Article Snippet: Proteins transferred to Protran membranes (Schleicher & Schuell) were probed with anti-PK mouse monoclonal antibodies for PK-tagged Bub2, with anti-GFP rat monoclonal antibodies for GFP-tagged Tem1, Bub2 and Bfa1 (Chromotek) and with an anti-HA monoclonal antibody (12CA5).

Techniques: Migration

Journal: PLoS Genetics

Article Title: Asymmetry of the Budding Yeast Tem1 GTPase at Spindle Poles Is Required for Spindle Positioning But Not for Mitotic Exit

doi: 10.1371/journal.pgen.1004938

Figure Lengend Snippet: A-B: Protein extracts from cells expressing the indicated tagged proteins were used for immunoprecipitation with an anti-HA affinity resin. Western blot analysis was then performed with anti-PK, anti-GFP and anti-HA antibodies. The input represents 1/25 th of the total extract used for each IP. C-F: Localization of eGFP- tagged Tem1 and Tem1-Q79L (C-D) or Bfa1-eGFP (E-F) was analysed in the indicated strains by fluorescence microscopy after formaldehyde fixation. Metaphase and anaphase cells were identified by means of the Tub1-mCherry co-expressed marker. Micrographs show representative cells of each strain in anaphase. G: Fluorescence intensity ratios were calculated between the two SPBs in anaphase cells of the indicated strains (see details in ).

Article Snippet: Proteins transferred to Protran membranes (Schleicher & Schuell) were probed with anti-PK mouse monoclonal antibodies for PK-tagged Bub2, with anti-GFP rat monoclonal antibodies for GFP-tagged Tem1, Bub2 and Bfa1 (Chromotek) and with an anti-HA monoclonal antibody (12CA5).

Techniques: Expressing, Immunoprecipitation, Western Blot, Fluorescence, Microscopy, Marker

Journal: PLoS Genetics

Article Title: Asymmetry of the Budding Yeast Tem1 GTPase at Spindle Poles Is Required for Spindle Positioning But Not for Mitotic Exit

doi: 10.1371/journal.pgen.1004938

Figure Lengend Snippet: A-B: Distribution of Cdc15-GFP (A) or Mob1-GFP (B) was analysed in the indicated strains by fluorescence microscopy after formaldehyde fixation. Metaphase and anaphase cells were identified by means of the Tub1-mCherry co-expressed marker. Micrographs show representative wild type and TEM1-Q79L cells expressing Cdc15-GFP in metaphase. C: Serial dilutions of stationary phase cells with the indicated genotypes were spotted on YPD and incubated at the indicated temperatures for 48h.

Article Snippet: Proteins transferred to Protran membranes (Schleicher & Schuell) were probed with anti-PK mouse monoclonal antibodies for PK-tagged Bub2, with anti-GFP rat monoclonal antibodies for GFP-tagged Tem1, Bub2 and Bfa1 (Chromotek) and with an anti-HA monoclonal antibody (12CA5).

Techniques: Fluorescence, Microscopy, Marker, Expressing, Incubation