mouse monoclonal anti human cyclin d1  (Proteintech)

Journal: iScience

Article Title: Prognostic value of BTG1 for predicting decitabine sensitivity in de novo acute myeloid leukemia

doi: 10.1016/j.isci.2025.114327

Figure Lengend Snippet: Downstream signaling pathway of BTG1 in AML cell lines (A) Top three signaling pathways in terms of Gene Ratio were EBV infection (0.037), Wnt signaling pathway (0.035), and hematopoietic lineage (0.023) of KEGG pathway enrichment. (B) Effect of BTG1 on the mRNA expression of β-catenin, Cyclin D1, and C-Myc. (C) Effect of BTG1 on the protein expression of β-catenin and Cyclin D1. (D) The relative viability of AML cells after interference of BTG1 and treatment with FH535. (E) Apoptosis of AML cells after interference of BTG1 and treatment with FH535. Data are presented as mean ± standard deviation (SD). (ns, p > 0.05; ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001).

Article Snippet: Mouse monoclonal anti-human Cyclin D1 , Proteintech , Cat# 60186-1-Ig RRID: AB_10793718.

Techniques: Protein-Protein interactions, Infection, Expressing, Standard Deviation

Journal: Animal Bioscience

Article Title: Transcriptomic analysis identifies CXCL12 as a novel candidate gene for litter size in rabbits

doi: 10.5713/ab.24.0640

Figure Lengend Snippet: CXCL12 overexpression and knockdown in GCs. (A,B) Changes in the expression of CXCL12 after its overexpression and knockdown in GCs. (C,D) The mRNA expression level of PCNA , CCND1 , CDK2 , Bcl-2 and Bax was detected after overexpressing or knocking down CXCL12 in GCs. (E) The protein expression levels of CCND1, PCNA, Bcl-2 and Bax were detected after overexpressing and knocking down CXCL12 in GCs. H, high-litter size group; L, low-itter size group; GAPDH was selected as the internal reference gene (The t test was used for the above analyses comparing two individual samples. * p<0.05; ** p<0.01; *** p<0.001; ns, not significant). GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GC, granulosa cells.

Article Snippet: Protein detection was achieved using the following antibodies: anti-CCND1 mouse monoclonal antibody (1:250, Proteintech), anti-PCNA rabbit polyclonal antibody (1:250, Proteintech), anti-Bcl2 rabbit polyclonal antibody (1:250, Proteintech), anti-Bax rabbit polyclonal antibody (1:250, Proteintech), anti-CITED1 rabbit polyclonal antibody (1:50, Proteintech), anti-WNT10B mouse monoclonal polyclonal antibody (1:250, Proteintech), anti-CXCR4 mouse monoclonal polyclonal antibody (1:250, Proteintech), anti-phospho-JAK2 rabbit monoclonal polyclonal antibody (1:250, Abcam, Cambridge, UK), anti-JAK2 rabbit monoclonal polyclonal antibody (1:250, Abcam), anti-phospho-STAT1 rabbit polyclonal antibody (1:250, Proteintech), anti-STAT1 rabbit polyclonal antibody (1:250, Proteintech), anti-GAPDH mouse monoclonal antibody (1:2,500, Proteintech), 1:1,000 goat anti-rabbit secondary antibody IgG (Proteintech) and 1:1,000 goat anti-mouse secondary antibody IgG (Proteintech).

Techniques: Over Expression, Knockdown, Expressing

Journal: Acta Pharmaceutica Sinica. B

Article Title: Elevated SNHG15 empowers keratinocytes hyperproliferation through activation of STAT3/Cyclin D1 axis in psoriasis

doi: 10.1016/j.apsb.2025.10.010

Figure Lengend Snippet: SNGH15 promotes keratinocytes hyperproliferation through activation of STAT3–Cyclin D1 signaling pathway. (A) The heatmap of RNA-seq data for HaCaT cells treated with control, IL-6 (50 ng/mL), IL-6+si-NC and IL-6+si-SNHG15 for 48 h. (B) Bubble plots showed that the differential expression genes were majorly enriched in several Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway. (C) SNHG15 was enriched in p-STAT3-precipitated complex relative to IgG control by RIP assay ( n = 3). (D) The protein level of p-STAT3/STAT3 and Cyclin D1 in HaCaT cells transfected with control, IL-6 (50 ng/mL), IL-6+si-NC and IL-6+si-SNHG15 for 72 h ( n = 3). (E) The protein level of Cyclin D1 in HaCaT cells treated with IL-6 (50 ng/mL) and IL-6+Stattic (10 μmol/L) for 48 h ( n = 3). (F) HaCaT cells were transfected with plasmid (empty vector control plasmid or EF.STAT3C.Ubc.GFP) for 24 h. And then cells were treated with control, IL-6 (50 ng/mL), IL-6+si-NC and IL-6+si-SNHG15 for 72 h. Finally, the protein expression of p-STAT3/STAT3 were detected by WB. (G) Cell viability was measured after transfection with plasmid (empty vector control plasmid or EF.STAT3C.Ubc.GFP) and treatment with IL-6 (50 ng/mL), IL-6+si-NC and IL-6+si-SNHG15 for 72 h by MTT ( n = 3). (H) HaCaT cells were transfected with plasmid (empty vector control plasmid or Exp-Cyclin D1 plasmid) for 48 h. Then, the protein expression of Cyclin D1 were detected by WB ( n = 3). (I) Cell viability was measured after transfection with plasmid (empty vector control plasmid or Exp-Cyclin D1 plasmid) and treatment with IL-6 (50 ng/mL), IL-6+si-NC and IL-6+si-SNHG15 for 72 h by MTT ( n = 3). Student's t test was used in C. One-way ANOVA with Student Newman–Keuls method was used for G and I. ∗∗ P < 0.01, ∗∗∗ P < 0.001, N.S. , non-significant. Data represent the mean ± SEM.

Article Snippet: Subsequently, the skin sections were perforated (Saponin, Beyotime, 30 min), blocked with 5% goat serum for 1 h, and then incubated with monoclonal Cyclin D1 antibody (1:100, 60186-1-Ig, Proteintech, Wuhan, China) overnight at 4 °C.

Techniques: Activation Assay, RNA Sequencing, Control, Quantitative Proteomics, Transfection, Plasmid Preparation, Expressing

Journal: Acta Pharmaceutica Sinica. B

Article Title: Elevated SNHG15 empowers keratinocytes hyperproliferation through activation of STAT3/Cyclin D1 axis in psoriasis

doi: 10.1016/j.apsb.2025.10.010

Figure Lengend Snippet: Inhibition of SNHG15 alleviates the IMQ-induced psoriasis-like epidermis hyperplasia in mice. (A) Strategies for the animal experiment. (B) The SNHG15 expression upon treatment with Vaseline/IMQ/IMQ + DEX/IMQ + si-NC/IMQ + si-SNHG15 ( n = 3–6). (C) Representative photos and H&E staining of the mice back of the Control/IMQ/IMQ + DEX/IMQ + si-NC/IMQ + si-SNHG15 groups (scale bar = 150 μm). (D) The PASI scores of the Control/IMQ/IMQ + DEX/IMQ + si-NC/IMQ + si-SNHG15 groups from Days 1–7. (E) Histological analysis of epidermal thickness in each group ( n = 3–6). (F) The protein level of p-STAT3 and STAT3 in the Control/IMQ/IMQ + si-NC/IMQ + si-SNHG15/IMQ + DEX groups. (G) Representative fluorescence staining of Cyclin D1 in the Control/IMQ/IMQ + DEX/IMQ + si-NC/IMQ + si-SNHG15 groups. The statistical relative fluorescence intensity expressions of Cyclin D1 in these groups are presented in the right. One-way ANOVA with Student Newman–Keuls method was used for B, D, E and G. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, N.S. , non-significant. Data represent the mean ± SEM.

Article Snippet: Subsequently, the skin sections were perforated (Saponin, Beyotime, 30 min), blocked with 5% goat serum for 1 h, and then incubated with monoclonal Cyclin D1 antibody (1:100, 60186-1-Ig, Proteintech, Wuhan, China) overnight at 4 °C.

Techniques: Inhibition, Expressing, Staining, Control, Fluorescence

Journal: bioRxiv

Article Title: CDKN1A (p21 Cip/Waf1 ) stabilizes Cyclin D3 by inhibiting its phosphorylation-dependent nuclear export following butyrate treatment

doi: 10.1101/2025.06.19.660543

Figure Lengend Snippet: Structural comparison of the crystallographic (PDB ID: 6P8H) and AlphaFold2-predicted (AF2) CDKN1A–CCND1/3–CDK4 complexes. Each subunit (CDKN1A, CCND1/CCND3, and CDK4) was predicted separately by AF2 and then overlaid onto the experimentally determined partial complex. Shown are the reassembled AF2-predicted CDKN1A–CCND3–CDK4 (left) and CDKN1A–CCND1–CDK4 (right) structures, highlighting how unresolved intrinsically disordered regions (IDRs) and extended C-terminal tails differ from the crystal structure. Dashed boxes mark the spatial proximity between CDKN1A’s RRL motif (Arg19–Arg20–Leu21) and the conserved cyclin Thr residues (Thr283 in CCND3 or Thr286 in CCND1). The inset magnifies these residues (RRL in gray; Thr283 in red; Thr286 in yellow), showing side-chain orientations. Notably, AF2 predicts variation in the C-terminal tails, suggesting CCND1 and CCND3 may exhibit distinct molecular recognition features (MoRFs).

Article Snippet: Rabbit monoclonal antibodies against CDKNA1, Thr283-phosphorylated Cyclin D3, Thr286-phosphorylated cyclin D1, HA (influenza hemagglutinin) tag, and Mcl-1 were purchased from Cell Signaling Technology (USA).

Techniques: Comparison

Journal: bioRxiv

Article Title: CDKN1A (p21 Cip/Waf1 ) stabilizes Cyclin D3 by inhibiting its phosphorylation-dependent nuclear export following butyrate treatment

doi: 10.1101/2025.06.19.660543

Figure Lengend Snippet: Molecular dynamics (MD) ensembles of the final 100 ns of the CDKN1A–CCND1–CDK4 (top) and CDKN1A–CCND3–CDK4 (bottom) complexes. Each ensemble comprises 50 snapshots taken at 2 ns intervals, illustrating how CDKN1A (wheat) interacts distinctly with CCND1 (pink) versus CCND3 (blue); CDK4 is shown in green. A dashed rectangle highlights the region containing the RRL motif of CDKN1A (black) and the conserved cyclin Thr residues (Thr286 in CCND1, orange; Thr283 in CCND3, yellow), whose side chains are displayed. The right panels show zoomed-in views of these residues, with calculated solvent-accessible surface areas (SASA) indicating Thr286 is partially solvent-exposed (0.61 ± 0.16 Å 2 ), whereas Thr283 is nearly buried (0.09 ± 0.06 Å 2 ). In the CDKN1A–CCND1 complex, the RRL motif forms multiple hydrogen bonds with CCND1, orienting Thr286 outward and facilitating phosphorylation. By contrast, Thr283 in CCND3 remains solvent-inaccessible, suggesting that CDKN1A binding induces a locally folded conformation that hinders phosphorylation and promotes CCND3 stabilization.

Article Snippet: Rabbit monoclonal antibodies against CDKNA1, Thr283-phosphorylated Cyclin D3, Thr286-phosphorylated cyclin D1, HA (influenza hemagglutinin) tag, and Mcl-1 were purchased from Cell Signaling Technology (USA).

Techniques: Solvent, Phospho-proteomics, Binding Assay