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Mouse Anti-ATF2 Recombinant Antibody (CBYC-A840) (CBMAB-A3864-YC)


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Published Data
Mouse Anti-ATF2 Recombinant Antibody (CBYC-A840) (CBMAB-A3864-YC) in WB
Western blot assay showed that the change of miRNA-363-3p did not alter the levels of TP53, phosphorylated TP53 and BCL2 proteins in miRNA-363-3p-ectopic OCI-Ly8 and miRNA-363-3p-knockout OCILy3 cells. However, the levels of phosphorylated ATF2 was affected. ...View More
Zhou, W., Xu, Y., Zhang, J., Zhang, P., Yao, Z., Yan, Z., ... & Liu, Y. (2022). MiRNA-363-3p/DUSP10/JNK axis mediates chemoresistance by enhancing DNA damage repair in diffuse large B-cell lymphoma. Leukemia, 36(7), 1861-1869.
Mouse Anti-ATF2 Recombinant Antibody (CBYC-A840) (CBMAB-A3864-YC) in WB
The overexpression and knockdown efficiency of ATF2 were confirmed by Western blot analysis. ...View More
Lee, J. W., Kim, D. M., Jang, J. W., Park, T. G., Song, S. H., Lee, Y. S., ... & Bae, S. C. (2019). RUNX3 regulates cell cycle-dependent chromatin dynamics by functioning as a pioneer factor of the restriction-point. Nature communications, 10(1), 1897.
Mouse Anti-ATF2 Recombinant Antibody (CBYC-A840) (CBMAB-A3864-YC) in WB
Western blot bands for p-RAF-1, ATF2, p-ATF2, Elk1, p-Elk1, c-Jun and p-cJun. ...View More
Karatug Kacar, A., & Bolkent, S. (2018). Necrotic cell death occur via JNK pathway with the activity of transcription factor c-Jun by 4-MC in INS-1 cell line. Journal of cellular biochemistry, 119(2), 2048-2060.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBYC-A840
Antibody Isotype
IgG1, κ
Application
ELISA, IHC, WB, IF, IHC-P

Basic Information

Immunogen
ATF-2 phosphorylated at Thr 71.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

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.

Target

Full Name
Activating Transcription Factor 2
Introduction
ATF2 is a transcription factor that is a member of the leucine zipper family of DNA binding proteins. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions This protein binds t
Entrez Gene ID
1386
UniProt ID
P15336
Alternative Names
Activating Transcription Factor 2; Cyclic AMP-Responsive Element-Binding Protein 2; CAMP Response Element-Binding Protein CRE-BP1; CAMP-Dependent Transcription Factor ATF-2; Histone Acetyltransferase ATF2; CREB-2; CREB2; HB16; Activating Transcription Fac
Function
Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro (PubMed:10821277).
In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type.
Biological Process
Adipose tissue development Source: Ensembl
Amelogenesis Source: Ensembl
Cellular response to amino acid starvation Source: Reactome
Cellular response to DNA damage stimulus Source: UniProtKB
Fat cell differentiation Source: Ensembl
Histone H2B acetylation Source: ARUK-UCL
Histone H4 acetylation Source: ARUK-UCL
Intra-S DNA damage checkpoint Source: UniProtKB
Negative regulation of angiogenesis Source: BHF-UCL
Negative regulation of epithelial cell proliferation Source: Ensembl
Negative regulation of transcription by RNA polymerase II Source: Ensembl
Outflow tract morphogenesis Source: Ensembl
Positive regulation of cardiac muscle myoblast proliferation Source: BHF-UCL
Positive regulation of DNA-binding transcription factor activity Source: UniProtKB
Positive regulation of gene expression Source: BHF-UCL
Positive regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB
Positive regulation of neuron apoptotic process Source: Ensembl
Positive regulation of transcription by RNA polymerase II Source: NTNU_SB
Positive regulation of transforming growth factor beta2 production Source: Ensembl
Regulation of DNA-binding transcription factor activity Source: Reactome
Regulation of transcription, DNA-templated Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: BHF-UCL
Response to osmotic stress Source: UniProtKB
Response to water deprivation Source: Ensembl
Cellular Location
Cytoplasm; Nucleus; Mitochondrion outer membrane. Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-52 is required for its nuclear localization and negatively regulates its mitochondrial localization. Co-localizes with the MRN complex in the IR-induced foci (IRIF).
PTM
Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity (PubMed:9430721, PubMed:12110590). Phosphorylated by PLK3 following hyperosmotic stress (PubMed:21098032). Also phosphorylated and activated by JNK and CaMK4 (PubMed:8855261). ATM-mediated phosphorylation at Ser-490 and Ser-498 stimulates its function in DNA damage response (PubMed:15916964). Phosphorylation at Ser-62, Thr-73 and Ser-121 activates its transcriptional activity (PubMed:15105425). Phosphorylation at Thr-69 or Thr-71 enhances acetylation of histones H2B and H4 (PubMed:10821277).
More Infomation

Fritz, V., Malek, L., Gaza, A., Wormser, L., Appel, M., Kremer, A. E., ... & Dietrich, P. (2021). Combined De-Repression of Chemoresistance Associated Mitogen-Activated Protein Kinase 14 and Activating Transcription Factor 2 by Loss of microRNA-622 in Hepatocellular Carcinoma. Cancers, 13(5), 1183.

Xu, X., Xia, J., Zhao, S., Wang, Q., Ge, G., Xu, F., ... & Yang, Y. (2021). Qing‐Fei‐Pai‐Du decoction and wogonoside exert anti‐inflammatory action through down‐regulating USP14 to promote the degradation of activating transcription factor 2. The FASEB Journal, 35(9), e21870.

Giannoudis, A., Malki, M. I., Rudraraju, B., Mohhamed, H., Menon, S., Liloglou, T., ... & Palmieri, C. (2020). Activating transcription factor-2 (ATF2) is a key determinant of resistance to endocrine treatment in an in vitro model of breast cancer. Breast Cancer Research, 22(1), 1-17.

Zhang, C., Zhang, R., Dai, X., Cao, X., Wang, K., Huang, X., & Ren, Q. (2020). Activating transcription factor 2 (ATF2) negatively regulates the expression of antimicrobial peptide genes through tumor necrosis factor (TNF) in Macrobrachium nipponense. Fish & Shellfish Immunology, 107, 26-35.

Li, M., Song, S. W., Ge, Y., Jin, J. Y., Li, X. Y., & Tan, X. D. (2020). The Ras-ERK signaling pathway regulates acetylated activating transcription factor 2 via p300 in pancreatic cancer cells. Annals of Translational Medicine, 8(19).

Huebner, K., Procházka, J., Monteiro, A. C., Mahadevan, V., & Schneider-Stock, R. (2019). The activating transcription factor 2: an influencer of cancer progression. Mutagenesis, 34(5-6), 375-389.

Aoki, Y., Nishizawa, D., Yoshida, K., Hasegawa, J., Kasai, S., Takahashi, K., ... & Ikeda, K. (2018). Association between the rs7583431 single nucleotide polymorphism close to the activating transcription factor 2 gene and the analgesic effect of fentanyl in the cold pain test. Neuropsychopharmacology reports, 38(2), 86-91.

Luo, L., Cai, L., Luo, L., Tang, Z., & Meng, X. (2018). Silencing activating transcription factor 2 promotes the anticancer activity of sorafenib in hepatocellular carcinoma cells. Molecular medicine reports, 17(6), 8053-8060.

Raghavan, S., Singh, N. K., Gali, S., Mani, A. M., & Rao, G. N. (2018). Protein kinase Cθ via activating transcription factor 2-mediated CD36 expression and foam cell formation of Ly6Chi cells contributes to atherosclerosis. Circulation, 138(21), 2395-2412.

Song, W. J., Dong, Y., Luo, C., & Chen, Y. Y. (2017). p38MAPK family isoform p38α and activating transcription factor 2 are associated with the malignant phenotypes and poor prognosis of patients with ovarian adenocarcinoma. Pathology-Research and Practice, 213(10), 1282-1288.

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

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