Mouse Anti-CDC25A Recombinant Antibody (DCS-120) (CBMAB-C4844-CQ)

Name: Mouse Anti-CDC25A Recombinant Antibody (DCS-120)
SKU: CBMAB-C4844-CQ
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-CDC25A Recombinant Antibody (DCS-120) (CBMAB-C4844-CQ) in WB

Cell lysates from RMS-PR and RMS-RR cells untreated (−) or treated (+) with 6 Gy of irradiation collected 12h after RT, were analyzed by immunoblotting with specific antibodies for indicated proteins; α-Tubulin expression shows the loading of samples. Western blot showed are representative of three different experiments. ...View More

Petragnano, F., Pietrantoni, I., Camero, S., Codenotti, S., Milazzo, L., Vulcano, F., ... & Marampon, F. (2020). Clinically relevant radioresistant rhabdomyosarcoma cell lines: Functional, molecular and immune-related characterization. Journal of biomedical science, 27, 1-18.

Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CDC25A Recombinant Antibody (DCS-120) (CBMAB-C4844-CQ) in IHC

Expression of Cdc25A is decreased in HEK293, HepG2, and HT-29 cell lines after fibrate treatment. Graphs display results as fold changes. ...View More

Cizkova, K., Steigerova, J., Gursky, J., & Ehrmann, J. (2016). Stimulating effect of normal-dosing of fibrates on cell proliferation: word of warning. Lipids in health and disease, 15, 1-11.

Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CDC25A Recombinant Antibody (DCS-120) (CBMAB-C4844-CQ) in WB

Series of Western blot experiments assessing key signaling molecule proteins from cell lysates of RLT-PSC cells.
PSCs were exposed to CHG and/or to subsequent TGF-β1 treatment. Best representative images of key signaling molecules of the stellate cells are indicated in Western blot membranes. Ponceau staining was used to assess the equal loading of gels. Significant (p<0.05)* and highly significant differences (p<0.001)** are marked. ...View More

Kiss, K., Baghy, K., Spisák, S., Szanyi, S., Tulassay, Z., Zalatnai, A., ... & Firneisz, G. (2015). Chronic hyperglycemia induces trans-differentiation of human pancreatic stellate cells and enhances the malignant molecular communication with human pancreatic cancer cells. PLoS One, 10(5), e0128059.

Distributed under Open Access license CC BY 4.0, without modification.

Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

DCS-120

Application

WB, IF, IP, IHC-P

Immunogen

Purified recombinant Cdc25A.

Host Species

Mouse

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG2a, κ

Clonality

Monoclonal Antibody

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)	1:50-1:500
IHC-P	1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS, 0.1% gelatin

Preservative

< 0.1% sodium azide

Concentration

0.2 mg/ml

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

Cell Division Cycle 25A

Introduction

CDC25A (Cell Division Cycle 25A) is a Protein Coding gene. Diseases associated with CDC25A include Breast Cancer. Among its related pathways are Metabolism of proteins and CDK-mediated phosphorylation and removal of Cdc6. Gene Ontology (GO) annotations related to this gene include protein kinase binding and protein tyrosine phosphatase activity. An important paralog of this gene is CDC25B.

Entrez Gene ID

993

UniProt ID

P30304

Alternative Names

Cell Division Cycle 25A; EC 3.1.3.48; Dual Specificity Phosphatase CDC25A; Dual Specificity Phosphatase Cdc25A; M-Phase Inducer Phosphatase 1; CDC25 Isoform A1-CAG; CDC25A2-CAG Isoform; CDC25A2;

Function

Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.

Biological Process

Cell division Source: UniProtKB-KW
Cell population proliferation Source: UniProtKB
Cellular response to UV Source: UniProtKB
G1/S transition of mitotic cell cycle Source: Reactome
G2/M transition of mitotic cell cycle Source: GO_Central
Positive regulation of G2/MI transition of meiotic cell cycle Source: GO_Central
Positive regulation of G2/M transition of mitotic cell cycle Source: GO_Central
Protein deubiquitination Source: Reactome
Regulation of cell cycle Source: Reactome
Regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
Response to radiation Source: UniProtKB

Cellular Location

Cytosol; Nucleoplasm; Nucleus; Cytoplasm

PTM

Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation.
Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization.

Liu, W. H., Qiao, H. Y., Xu, J., Wang, W. Q., Wu, Y. L., & Wu, X. (2020). LINC00473 contributes to the radioresistance of esophageal squamous cell carcinoma by regulating microRNA‑497‑5p and cell division cycle 25A. International journal of molecular medicine, 46(2), 571-582.

Yang, Y., Sun, X., Cui, W., Liu, N., Wang, K., Qu, L., & Pan, C. (2021). The detection of mutation within goat cell division cycle 25 A and its effect on kidding number. Animal Biotechnology, 1-6.

Lara-Chica, M., Correa-Sáez, A., Jiménez-Izquierdo, R., Garrido-Rodríguez, M., Ponce, F. J., Moreno, R., ... & Calzado, M. A. (2021). A novel CDC25A/DYRK2 regulatory switch modulates cell cycle and survival. Cell Death & Differentiation, 1-13.

Tang, Y., Cao, J., Cai, Z., An, H., Li, Y., Peng, Y., ... & Li, K. (2020). Epigallocatechin gallate induces chemopreventive effects on rats with diethylnitrosamine‑induced liver cancer via inhibition of cell division cycle 25A. Molecular Medicine Reports, 22(5), 3873-3885.

Chen, S., Tang, Y., Yang, C., Li, K., Huang, X., & Cao, J. (2020). Silencing CDC25A inhibits the proliferation of liver cancer cells by downregulating IL‑6 in vitro and in vivo. International journal of molecular medicine, 45(3), 743-752.

Yin, W., Xu, J., Li, C., Dai, X., Wu, T., & Wen, J. (2020). Circular RNA circ_0007142 facilitates colorectal cancer progression by modulating CDC25A expression via miR-122-5p. OncoTargets and therapy, 13, 3689.

Ding, F. N., Gao, B. H., Wu, X., Gong, C. W., Wang, W. Q., & Zhang, S. M. (2019). miR‐122‐5p modulates the radiosensitivity of cervical cancer cells by regulating cell division cycle 25A (CDC25A). FEBS open bio, 9(11), 1869-1879.

Liu, W., Wu, M., Du, H., Shi, X., Zhang, T., & Li, J. (2018). SIRT6 inhibits colorectal cancer stem cell proliferation by targeting CDC25A. Oncology letters, 15(4), 5368-5374.

Zhang, W., Zeng, Q., Ban, Z., Cao, J., Chu, T., Lei, D., ... & Zeng, X. (2018). Effects of let‑7c on the proliferation of ovarian carcinoma cells by targeted regulation of CDC25a gene expression. Oncology letters, 16(5), 5543-5550.

Zwergel, C., Czepukojc, B., Evain-Bana, E., Xu, Z., Stazi, G., Mori, M., ... & Valente, S. (2017). Novel coumarin-and quinolinone-based polycycles as cell division cycle 25-A and-C phosphatases inhibitors induce proliferation arrest and apoptosis in cancer cells. European journal of medicinal chemistry, 134, 316-333.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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For research use only. Not intended for any clinical use.

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