mouse anti-proliferating cell nuclear antigen (pcna) antibody  (Boster Bio)

Journal: Biomedical Reports

Article Title: TiO 2 NPs improve ultrasound response: CS/β-GP/TiO 2 NP hydrogel enabling on-demand administration

doi: 10.3892/br.2025.2020

Figure Lengend Snippet: Western blotting results of different composite hydrogels. The results of western blotting assay revealed no significant differences in cell protein expression among the different groups (P>0.05). PCNA, proliferating cell nuclear antigen; CS/β-GP, chitosan/β-glycerophosphate; TiO 2 NPs, titanium dioxide nanoparticles.

Article Snippet: The following materials were used: i) CS powder (95% deacetylation degree; cat. no. C105799; Aladdin Scientific Corp.), ii) β-GP pentahydrate (cat. no. D106347; Aladdin Scientific Corp.), iii) sodium fluorescein (NaF; cat. no. F105615; Aladdin), iv) TiO 2 NPs (20-40 nm; cat. no. NM000800; Beijing Solarbio Science & Technology Co., Ltd.), v) L929 murine fibroblast cells (cat. no. KGG1306-1), vi) RPMI-1640 medium (containing newborn calf serum, double antibiotics; cat. no. KGL1509-500), vii) Cell Counting Kit-8 (CCK-8) cell proliferation assay kit (cat. no. KGA9305-500), viii) LIVE/DEAD cell viability assay kit (cat. no. KGA9501-1000), ix) bovine serum albumin (BSA) (standard grade, heat-treated) (cat. no. KGL2314-10), x) bicinchoninic acid (BCA) protein quantification assay kit (cat. no. KGB2101-250), all from Jiangsu KeyGen Biotech Co., Ltd., xi) mouse anti-proliferating cell nuclear antigen (PCNA) antibody (1:1,000; cat. no. BM0104) and xii) goat anti-mouse IgG/HRP antibody (1:10,000; cat. no. BA1056) both from Boster Biological Technology Co. Ltd.

Techniques: Western Blot, Expressing, Titanium Dioxide

Journal: PLOS One

Article Title: Cysteine dioxygenase knockout and taurine deficiency impair mouse uterine adenogenesis by inhibiting epithelial cell proliferation and enhancing apoptosis

doi: 10.1371/journal.pone.0329503

Figure Lengend Snippet: (a-d) 10 days taurine supplementation to the Cdo KO mice (KO+Tau) increases the taurine level (a), the number of uterine glands marked by Foxa2 (b, c) and Foxa2 mRNA levels (d) in the uterine tissue. (e) Western Blot detection and analysis of PCNA protein levels in the uteri of the WT, Cdo KO and KO + Tau mice (n ≥ 3). (f) Western blot detection of BAX/BCL2 protein levels (up) and the analysis of BAX/BCL2 ration (down) in the uteri of the WT, Cdo KO and KO + Tau mice. WT: wild type. KO: Cdo KO. PND: Postnatal day. Scale bar represents 20 μm. *P < 0.05, **P < 0.01, ***P < 0.001.

Article Snippet: The membrane was blocked with 5% (w/v) nonfat dry milk in 0.05 mol/L pH 7.4 Tris buffered saline (TBS) for 1 h and incubated with rabbit anti-CDO antibody (ab53436, abcam, Cambridge, UK; 1:2000), mouse anti- proliferating cell nuclear antigen (PCNA) antibody (60097–1-Ig, Proteintech Group, Inc., IL, USA; 1:2000), rabbit anti-BCL2-Associated X Protein (BAX) antibody ( T40051 , Abmart Shanghai Co.,Ltd., China, 1:2000), rabbit anti-BCL2-Associated X Protein (BAX) antibody (ab182858, abcam, Cambridge, UK; 1:2000), and internal control rabbit anti-Tubulin antibody (K006154P, Beijing Solarbio Science & Technology Co.,Ltd., China, 1:2000) overnight at 4°C.

Techniques: Western Blot

Journal: The Journal of Biological Chemistry

Article Title: An anomalous abundance of tryptophan residues in ceramide synthases based on analysis of all membrane proteins in the Swiss-Prot database

doi: 10.1016/j.jbc.2024.108053

Figure Lengend Snippet: Effect of mutating N-terminal Trp residues on CerS activity. A , sequence alignment of the N-terminus of human CerS1-6. The red arrow indicates the Trp residue of interest. Sequences were aligned using ClustalW. B , sequences of the N-terminus presented as a logo, which is a representation of the conservation of amino acids at each position. The height of the letter represents the dominance of that particular residue at that position; if there are no dominant residues, the position is blank or a combination of many small residues. The sequence logo was generated from 209 CerS1-6 homologous sequences from 84 species, ranging from amoeba to human, based on data from Ref. . When comparing alignments, the distances between residues in the logos vary due to the effect of the alignments from distant species. Arrows indicate the Trp of interest. The logo was built using WebLogo. C , homogenates were prepared from WT HEK cells overexpressing the indicated CerS, except for CerS2, which was overexpressed in HEK/CerS2 −/− cells. CerS activity was assayed using the indicated acyl-CoAs. CerS2 activity was assayed using 40 μg of protein from a cell homogenate for 25 min; CerS3 was assayed using 40 μg for 30 min; CerS4 was assayed using 35 μg for 25 min; CerS5 using 2 μg for 10 min; and CerS6 using 5 μg for 10 min. Results are means ± S.D. for a typical experiment repeated a minimum of three times in duplicate with similar results. ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001. Levels of protein expression were ascertained by Western blotting using an anti-HA antibody. The glycosylated form is the upper band, and the nonglycosylated form is the lower band . Anti-tubulin (CerS3, 4, 5, and 6) or anti-PCNA (CerS2) were used as loading controls. Molecular weight markers (kDa) are indicated. Western blots were repeated at least three times with similar results.

Article Snippet: Equal loading was confirmed using a mouse anti-tubulin antibody (Sigma,1:10,000) or mouse anti-proliferating cell nuclear antigen (anti-PCNA) antibody (Santa Cruz, 1:500) and goat anti-mouse horseradish peroxidase (Jackson ImmunoResearch, 1:5000) as the secondary antibody.

Techniques: Activity Assay, Sequencing, Residue, Generated, Expressing, Western Blot, Molecular Weight