Santa Cruz Biotechnology
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Santa Cruz Biotechnology
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Image Search Results

Journal: Molecular Cancer
Article Title: RNA demethylase ALKBH5 prevents pancreatic cancer progression by posttranscriptional activation of PER1 in an m6A-YTHDF2-dependent manner
doi: 10.1186/s12943-020-01158-w
Figure Lengend Snippet: ALKBH5 induces posttranscriptional activation of PER1 to inhibit PC progression in an m6A-YTHDF2-dependent manner. ALKBH5 loss that abrogates mRNA demethylation leads to an upregulation of PER1 m6A levels in PC cells. Then, degradation of PER1 mRNA occurs on the basis of the m6A-YTHDF2 interaction. PER1 downregulation results in the inhibition of ATM phosphorylation and inactivation of the ATM-CHK2-P53/CDC25C pathways. G2/M arrest in PC cells was suppressed as a result. The PER1-related P53 downregulation and P53-dependent transcriptional inactivation of ALKBH5 indicates a feedback loop underlying the progression of PC
Article Snippet: The primary antibodies were rabbit monoclonal anti-ALKBH5 (ab195377, Abcam), mouse monoclonal anti-PER1 (sc-398,890, Santa Cruz), mouse monoclonal anti-p-ATM (Ser-1981; sc-47,739, Santa Cruz), rabbit monoclonal anti-p-CHK2 (Thr-68; ab32148, Abcam),
Techniques: Activation Assay, Inhibition

Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: Diagram of the human cdc25C constructs used. All cdc25C constructs contained an N-terminal Myc epitope tag (black box). A 14-3-3 binding motif of cdc25C (RSPSMP) is phosphorylated at the second serine residue (S216) in the consensus (44, 47, 49), and mutation of the serine residue to alanine abolishes binding to 14-3-3 proteins (49). The phosphatase domain (hatched box) is located in the C terminus with the active site (HCEFSSER) shown. Substitution of the cysteine residue at position 377 with serine disrupts phosphatase activity (4, 11, 40). The N-terminal box (vertical lines) represents the HA epitope and the HIV-1 Rev NES, and the C-terminal stippled box represents the SV40 large-T-antigen NLS.
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Construct, Binding Assay, Mutagenesis, Activity Assay
![Specificity of MAbs to cdc25C. (A) MAbs were raised to a GST fusion protein that contained the first 258 amino acids of human cdc25C (GST 1–258). Bacterial lysates expressing either GST-cdc25A (10 μl; lane 1), GST-cdc25B (20 and 30 μl; lanes 2 and 3, respectively), or GST 1–258 (10 μl; lane 4) were separated in an SDS–7.5% polyacrylamide gel and Western (W.) blotted with DG122, a mouse MAb specific for GST, and the four cdc25C antibodies, TC14, TC15, TC19, and TC113. (B) Indicated Myc-tagged cdc25C constructs were translated in vitro with [35S]methionine; 15 μl of in vitro translate was immunoprecipitated with the indicated antibodies, and the immunoprecipitated proteins were visualized by autoradiography. The Δ 201–258 construct contains an in-frame deletion of amino acids 201 to 258 (lane 2). Δ 201–258 (211–221) and Δ 201–258 (222–246) (lanes 3 and 4) are mutant proteins that contain insertions of the indicated amino acids into the Δ 201–258 mutant. 1–258, 1–150, and 259–473 (lanes 5 to 7) are shown in Fig. Fig.1.1. (C) cdc25c diagram showing where the MAbs bind. The N-terminal myc tag is recognized by MAb 9E-10.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_4405/pmc00104405/pmc00104405__mb0691199002.jpg)
Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: Specificity of MAbs to cdc25C. (A) MAbs were raised to a GST fusion protein that contained the first 258 amino acids of human cdc25C (GST 1–258). Bacterial lysates expressing either GST-cdc25A (10 μl; lane 1), GST-cdc25B (20 and 30 μl; lanes 2 and 3, respectively), or GST 1–258 (10 μl; lane 4) were separated in an SDS–7.5% polyacrylamide gel and Western (W.) blotted with DG122, a mouse MAb specific for GST, and the four cdc25C antibodies, TC14, TC15, TC19, and TC113. (B) Indicated Myc-tagged cdc25C constructs were translated in vitro with [35S]methionine; 15 μl of in vitro translate was immunoprecipitated with the indicated antibodies, and the immunoprecipitated proteins were visualized by autoradiography. The Δ 201–258 construct contains an in-frame deletion of amino acids 201 to 258 (lane 2). Δ 201–258 (211–221) and Δ 201–258 (222–246) (lanes 3 and 4) are mutant proteins that contain insertions of the indicated amino acids into the Δ 201–258 mutant. 1–258, 1–150, and 259–473 (lanes 5 to 7) are shown in Fig. Fig.1.1. (C) cdc25c diagram showing where the MAbs bind. The N-terminal myc tag is recognized by MAb 9E-10.
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Expressing, Western Blot, Construct, In Vitro, Immunoprecipitation, Autoradiography, Mutagenesis

Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: cdc25C is present in the cytoplasm of asynchronously growing human cells. (A) Two-milligram aliquots of EBC extracts prepared from U-2OS cells were immunoprecipitated with cdc25C-specific antibodies TC14 (lanes 2 and 7), TC15 (lanes 3 and 8), TC113 (lanes 4 and 9), and TC19 (lanes 5 and 10) or the Myc antibody 9E-10 (lanes 1 and 6). The immune complexes resolved in SDS–7.5% polyacrylamide gels followed by Western blotting with either a mixture of TC14, TC15, and TC19 (lanes 1 to 5) or an anti-cdc25C rabbit polyclonal antibody (Santa Cruz) (lanes 6 to 10). The position of cdc25C, which migrated as a doublet, is indicated by the bracket. The arrow indicates the immunoglobulin heavy chain. The positions of the molecular weight markers are indicated in kilodaltons to the left of each gel. B. U-2OS (lanes 1, 4, and 7), MRC-5 (lanes 2, 5, and 8), and WI-38 (lanes 3, 6, and 9) cells were harvested by trypsinization, and the cell pellets were boiled in 2% SDS; 50 (lanes 1 to 6) or 25 (lanes 7 to 9) μg of protein extract was separated in an SDS–10% polyacrylamide gel, and then Western blotting was performed with the indicated antibodies. The immune complexes were detected by using the Pierce Supersignal system. TC14, TC15, and TC113 all recognized a specific doublet at ∼55 kDa in each of the different cell types. In addition to this band, they specifically recognized a band at ∼47 kDa (open arrow) in U-2OS cells. On longer exposures, this band was also detected in MRC-5 and WI-38 cells. No other specific signal was detected with these antibodies. (C) Two-milligram aliquots of whole-cell (lanes 1 and 4), cytoplasmic (lanes 2 and 5), or nuclear (lanes 3 and 6) extracts prepared from U-2OS cells were immunoprecipitated with either an anti-Rb antibody (MAb 245; Pharmingen) (lanes 1 to 3) or an anti-cdc25C antibody (TC113) (lanes 4 to 6). The immune complexes were resolved in an SDS–7.5% polyacrylamide gel and Western blotted with MAb 245 (lanes 1 to 3) or a mixture of TC14, TC15, and TC19 (lanes 4 to 6). The cdc25C doublet is indicated by the bracket. The thick arrow indicates the immunoglobulin heavy chains; the position of Rb on the gel is indicated by the thin arrow. (D) Two-milligram aliquots of whole-cell (lane 1), cytoplasmic (lanes 2 and 3), or nuclear (lane 4) extracts prepared from U-2OS cells were immunoprecipitated with the cdc25C MAb (TC113). The cytoplasmic extracts in lane 3 were prepared in the presence of a cocktail of phosphatase inhibitors (10 μM cypermethrin, 200 μM dephostatin, 200 nM okadaic acid, and 25 nM tautomycin). cdc25C is indicated by a bracket; the arrow indicates the position of the immunoglobulin heavy chain.
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Immunoprecipitation, Western Blot, Molecular Weight

Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: Cellular localization of cdc25C in human cells. (A) Indirect immunofluorescence with the cdc25C antibodies was performed in multiple cell types. U-2OS cells immunostained with either TC14 (left) or TC113 (right) are shown in the top panels. The primary human fibroblasts, MRC-5 (bottom left) and WI-38 (bottom right), were immunostained with antibody TC113. In each pair, the left panel shows antibody staining while the right panel shows the DAPI stain of the same field (original magnification, ×100). (B) MRC-5 cells were immunostained with polyclonal sera specific for phospho-histone H3 (α pH3) (17), a MAb to cdc25C (TC113), and DAPI, as indicated, and visualized by confocal microscopy. The merge of the cdc25C and the pH3 staining is shown in the bottom left panel. A cell that stains positively for histone H3 and shows partial chromatin condensation (DAPI) is indicated by the thick arrow. A cell that does not stain with the phospho-histone H3 antibody in which the chromatin is not condensed is indicated by the thin arrow (original magnification, ×63). (C) U-2OS cells were treated with mimosine to induce a G1 arrest. Six hours after mimosine release, cells were γ irradiated (γ-IR) with a dose of 6 Gy and then incubated in either the presence or absence of the crm1 inhibitor leptomycin B (LMB) for an additional 18 h. Cells were immunostained with either an anti-cdc25C antibody (TC113) or an anti-cyclin B1 antibody (CB169). In each pair, the left panel shows immunofluorescence while the right panel shows the DAPI stain of the same field (original magnification, ×100). The cell cycle profiles of the cells in mimosine (mimosine), cells 6 h after release from mimosine (6 hours), and the γ-irradiated cells (γ-IR) and irradiated cells treated with leptomycin B (γ-IR + LMB) are shown.
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Immunofluorescence, Staining, Confocal Microscopy, Irradiation, Incubation

Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: Cytoplasmic localization of cdc25C is dependent on a 14-3-3 binding motif. (A) U-2OS cells were transiently transfected with the indicated cdc25C constructs and visualized by confocal microscopy with the anti-Myc antibody 9E-10 (α myc) and DAPI staining. The arrow highlights cells showing condensed fractured chromatin indicative of PCC (original magnification, ×63). (B) Extracts of U-2OS cells cotransfected with plasmids expressing an HA-tagged 14-3-3ɛ cDNA and the indicated Myc-tagged cdc25C constructs were immunoprecipitated with an anti-Myc antibody (9E-10) or an anti-HA antibody (12CA5). The immune complexes were washed and then resolved in either an SDS–7.5% polyacrylamide gel (lanes 1 to 4, top panel) or an SDS–10% polyacrylamide gel (lanes 5 and 6, top panel; lanes 7 to 18, middle and bottom panels). The cdc25C constructs were detected by Western blotting (WB) with a polyclonal Myc antibody (Santa Cruz), and the HA 14-3-3ɛ was detected by Western blotting with the anti-HA MAb (12CA5).
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Binding Assay, Transfection, Construct, Confocal Microscopy, Staining, Expressing, Immunoprecipitation, Western Blot

Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: Effect of localization on cdc25C function. (A) U-2OS cells transfected with Myc-tagged cdc25C and cyclin B1 were immunostained with antibodies to the Myc epitope (α-myc) the mitosis-specific antibody MPM2 (α-MPM2) and DAPI. A cell immunostained with both the Myc and MPM2 antibodies showed condensed fractured chromatin when stained with DAPI (thin arrow). An untransfected cell undergoing mitosis is stained by the MPM2 antibody (thick arrow). (B) U-2OS cells transfected with the indicated Myc-tagged cdc25C constructs were immunostained with the anti-Myc antibody (9E-10) and DAPI. More than a 100 Myc-positive, cdc25C-expressing cells were counted, and the percentage of cells containing condensed fragmented chromatin was determined in three independent experiments. (C) U-2OS cells were treated with mimosine to induce a G1 arrest. Cells were transfected with cdc25C and a CD19 cDNA in the presence of mimosine. Six hours after transfection, the DNA was removed and the cells were refed twice with mimosine-containing medium; 20 h after mimosine was first added to the cells, cells were refed with fresh medium; cells were then harvested at the indicated time points for FACS analysis or were immunostained for Myc-tagged cdc25C and the endogenous cyclin B1 as described in the text and with DAPI to determine PCC. Six hours after mimosine was removed, 100 μM HU was added to one set of plates for 6 h. Open bars indicate the percentage of cells undergoing PCC; filled bars indicate the percentage of transfected cells staining positively for cyclin B1. A, asynchronous. The percentages of CD19-positive cells in G1, S, and G2 phases at the indicated timepoints are tabulated at the bottom. (D) Cells from the experiment described above were stained with a polyclonal antibody to the Myc epitope (α-myc) a MAb to cyclin B1 (α-B1), or DAPI. Cells arrested in mimosine (0) show little staining for cyclin B1. After mimosine release, the percentage of cells staining for cyclin B1 increases until all cells stain for cyclin B1 (12 and 12+HU). All cells undergoing PCC (thin arrow) show staining for cyclin B1 (original magnification, ×60).
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Transfection, Staining, Construct, Expressing

Journal:
Article Title: Cytoplasmic Localization of Human cdc25C during Interphase Requires an Intact 14-3-3 Binding Site
doi:
Figure Lengend Snippet: Effect of a heterologous NES or NLS on cdc25C localization and function. (A) U-2OS cells were transfected with constructs expressing either the Myc-tagged NLS or HA-tagged NES fusion of cdc25C. The cells were fixed and visualized with indirect immunofluorescence with antibody to the HA or Myc epitope (left panel of each pair) and DAPI (right panel of each pair). The original magnification on all the panels is ×60 except for the S216ANLS panel (×40). (B) WT cdc25C and the NES fusions were transfected into U-2OS cells either alone (left) or in the presence of ectopically expressed cyclin B1 (right). (C) WT and the NLS fusions were transfected into U-2OS cells alone (left), cotransfected with cyclin B1 (middle), or cotransfected with an NLS-tagged version of cyclin B1 (right).
Article Snippet: All four cdc25C antibodies specifically immunoprecipitated a doublet that migrated at approximately 55 kDa in U-2OS cells upon Western blotting with either a mixture of the cdc25C MAbs or an
Techniques: Transfection, Construct, Expressing, Immunofluorescence