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AB8106

Anti-MTA2/PID 抗体

Anti-MTA2/PID antibody

5

(2 Reviews)

|

(43 Publications)

Rabbit Polyclonal MTA2/PID antibody. Suitable for IP, ELISA, WB, IHC-P, ICC/IF, IHC-Fr and reacts with Mouse, Rat, Human samples. Cited in 43 publications.

別名を表示する

MTA1L1, PID, MTA2, Metastasis-associated protein MTA2, Metastasis-associated 1-like 1, p53 target protein in deacetylase complex, MTA1-L1 protein

5 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-MTA2/PID antibody (AB8106)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-MTA2/PID antibody (AB8106)

ab8106 (2μg/ml) staining MTA2/PID in human ileum using an automated system (DAKO Autostainer Plus). Using this protocol there is strong nuclear staining.
Sections were rehydrated and antigen retrieved with the Dako 3 in 1 AR buffer EDTA pH 9.0 in a DAKO PT Link. Slides were peroxidase blocked in 3% H2O2 in methanol for 10 mins. They were then blocked with Dako Protein block for 10 minutes (containing casein 0.25% in PBS) then incubated with primary antibody for 20 min and detected with Dako Envision Flex amplification kit for 30 minutes. Colorimetric detection was completed with Diaminobenzidine for 5 minutes. Slides were counterstained with Haematoxylin and coverslipped under DePeX. Please note that, for manual staining, optimization of primary antibody concentration and incubation time is recommended. Signal amplification may be required.

Immunocytochemistry/ Immunofluorescence - Anti-MTA2/PID antibody (AB8106)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-MTA2/PID antibody (AB8106)

Immunofluorescence of PID in HeLa cells using ab8106 at 10 ug/ml.

Immunocytochemistry/ Immunofluorescence - Anti-MTA2/PID antibody (AB8106)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-MTA2/PID antibody (AB8106)

ab8106 at 10μg/ml staining MTA2/PID in Hela cells by ICC/IF

Western blot - Anti-MTA2/PID antibody (AB8106)
  • WB

Unknown

Western blot - Anti-MTA2/PID antibody (AB8106)

All lanes:

Western blot - Anti-MTA2/PID antibody (ab8106) at 1 µg/mL

Lane 1:

HeLa whole cell lysate with absence of blocking peptide

Lane 2:

HeLa whole cell lysate with presence of blocking peptide

Predicted band size: 75 kDa

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Western blot - Anti-MTA2/PID antibody (AB8106)
  • WB

CiteAb

Western blot - Anti-MTA2/PID antibody (AB8106)

Western Blotting using Anti-MTA2/PID antibody, ab8106. Publication image from Ma, C. et al., 2018, Mol Cancer, 29625565. Legend direct from paper.

Involvement of NuRD complex in the regulation of breast cancer cell senescence and suppression mediated by SALL1. a and b Transfection of mutated SALL1 (mSALL1, deleted the NuRD binding peptide motif of conserved 12-amino) in MCF-7 and E0771 cancer cells did not induce SA-β-Gal+ cell populations (in a) and promote cancer cell cycle arrest in S phase (in b). In contrast, transfection of full-length SALL1 into MCF-7 and E0771 breast cancer cells significantly induced tumor cell senescence (around 40%) and promoted cell cycle arrest in S phase. Breast cancer cells were transfected with the indicated constructs and cultured for additional 72 h. Senescent cells were analyzed using the SA-β-Gal activity assay and the cell cycle distribution in tumor cells was analyzed after incubation with propidium iodide. Data shown in (a) are mean ± SD from three independent experiments with similar results. **p < 0.01 compared with the mSALL1 and vector control groups. c and d Transfection of SALL1-S2E into MCF-7 and E0771 breast cancer cells lost the ability to induce tumor cell senescence. However, transfection of SALL1-S2A into breast cancer cells significantly augmented senescence induction in both cell lines compared with that of in wild type SALL1-transfected tumor cells. Cell transfection procedure and SA-β-Gal+ cell determination were identical to (a). SALL1-S2E : substitution of the serine with a glutamic acid in SALL1. SALL1-S2A : mutating the serine to an alanine in SALL1. SA-β-Gal+ tumor cells were identified with dark blue granules as indicated by the arrows (in c). Data shown in (d) are mean ± SD from three independent experiments with similar results. **p < 0.01, compared with the vector control group. #p < 0.01, compared with the wild type SALL1 group. e Transfection of wild type SALL1 and SALL1-S2A into MCF-7 tumor cells recruited NuRD complex components determined with GST pulldown analyses. In contrast, transfection of SALL1-S2E markedly disrupted recruitment of NuRD components. MCF-7 cells were transfected with or without plasmids pEBG-SALL1, pEBG-SALL1-S2A, and pEBG-SALL1-S2E, and cultured for 3 days. Total protein lysates precipitated with Protein G-Sepharose beads. Pulldowns were analyzed by western blotting with antibodies against SALL1, HDAC1, MTA2, MBD3 and RbAp46/48

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Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Human, Mouse, Rat

アプリケーション

IP, IHC-Fr, IHC-P, ELISA, ICC/IF, WB

applications

免疫原

The exact immunogen used to generate this antibody is proprietary information.

特異性

No cross-reactivity to MTA1.

Reactivity data

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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification
バッファー組成
pH: 7.2 Preservative: 0.02% Sodium azide
出荷温度
Blue Ice
短期保存温度
+4°C
長期保存温度
+4°C

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

MTA2 also known as metastasis-associated protein 2 is a component of the nucleosome remodeling and deacetylase (NuRD) complex weighing approximately 77 kDa. MTA2 is widely expressed throughout the human body including in vital organs and tissues such as the liver brain and lung. It plays a significant role in regulating gene expression by modifying chromatin structure. This protein often localizes in the nucleus where it can regulate various cellular processes.
Biological function summary

MTA2 influences the suppression and activation of gene transcription. It acts as an integral part of the NuRD complex which combines chromatin remodeling and histone deacetylase activities. Through this role MTA2 helps control cellular differentiation proliferation and development. By modulating epigenetic states MTA2 can impact cellular responses to external stimuli helping cells adapt to changes in their environment.

Pathways

MTA2 engages in cellular signaling pathways including the Notch signaling and Wnt signaling pathways. These pathways are important for regulating cell fate decisions. MTA2 interacts with other proteins such as HDAC1 and HDAC2 to exert its influence on transcriptional repression and gene silencing. The NuRD complex of which MTA2 is part serves as a critical mediator in these pathways highlighting its importance in cellular homeostasis.

MTA2 participation links it to cancer progression and metastasis. It shows overexpression in several cancers including breast and liver cancer where it correlates with more aggressive tumor behavior and poor prognosis. Interestingly MTA2 also associates with prostate cancer through its interaction with the androgen receptor influencing cancer cell survival and proliferation. Identifying MTA2’s connections with these conditions has pointed to potential therapeutic targets within these molecular pathways.

製品プロトコール

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ターゲットの情報

May function as a transcriptional coregulator (PubMed : 16428440, PubMed : 28977666). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed : 16428440, PubMed : 28977666).
See full target information MTA2

文献 (43)

Recent publications for all applications. Explore the full list and refine your search

Acta biochimica et biophysica Sinica 57:1457-1468 PubMed39757769

2025

MYB represses ζ-globin expression through upregulating ETO2.

Applications

Unspecified application

Species

Unspecified reactive species

Zejun Dong,Yuhua Ye,Wei Zhang,Hualei Luo,Jialong Li,Qianqian Zhang,Xinhua Zhang,Xiang Guo,Xiangmin Xu

Life science alliance 7: PubMed38649186

2024

lncRNA LINC00941 modulates MTA2/NuRD occupancy to suppress premature human epidermal differentiation.

Applications

Unspecified application

Species

Unspecified reactive species

Eva Morgenstern,Carolin Molthof,Uwe Schwartz,Johannes Graf,Astrid Bruckmann,Sonja Hombach,Markus Kretz

International journal of molecular sciences 25: PubMed38474064

2024

Circ Drives Gastric Cancer Progression through Suppressing Degradation via Interacting with UCHL3.

Applications

Unspecified application

Species

Unspecified reactive species

Gengchen Xie,Bo Lei,Zhijie Yin,Fei Xu,Xinghua Liu

Cancer research 84:241-257 PubMed37963210

2023

The Chromatin Remodeler CHD4 Sustains Ewing Sarcoma Cell Survival by Controlling Global Chromatin Architecture.

Applications

Unspecified application

Species

Unspecified reactive species

Joana Graca Marques,Blaz Pavlovic,Quy A Ngo,Gloria Pedot,Michaela Roemmele,Larissa Volken,Samanta Kisele,Romain Perbet,Marco Wachtel,Beat W Schäfer

Cancer communications (London, England) 43:1117-1142 PubMed37658635

2023

JARID2 coordinates with the NuRD complex to facilitate breast tumorigenesis through response to adipocyte-derived leptin.

Applications

Unspecified application

Species

Unspecified reactive species

Wei Liu,Yi Zeng,Xinhui Hao,Xin Wang,Jiaxiang Liu,Tianyang Gao,Mengdi Wang,Jingyao Zhang,Miaomiao Huo,Ting Hu,Tianyu Ma,Die Zhang,Xu Teng,Hefen Yu,Min Zhang,Baowen Yuan,Wei Huang,Yunkai Yang,Yan Wang

PLoS pathogens 19:e1011477 PubMed37410772

2023

Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1.

Applications

Unspecified application

Species

Unspecified reactive species

Carlos F De La Cruz-Herrera,Michael H Tatham,Umama Z Siddiqi,Kathy Shire,Edyta Marcon,Jack F Greenblatt,Ronald T Hay,Lori Frappier

Journal of cell science 136: PubMed36861403

2023

Characterization of the nuclear import of the human CHD4-NuRD complex.

Applications

Unspecified application

Species

Unspecified reactive species

Helen Hoffmeister,Simon Holzinger,Marie-Sofie Dürr,Astrid Bruckmann,Susanne Schindler,Regina Gröbner-Ferreira,Reinhard Depping,Gernot Längst

Molecular cell 83:715-730.e6 PubMed36868189

2023

Gene silencing dynamics are modulated by transiently active regulatory elements.

Applications

Unspecified application

Species

Unspecified reactive species

Marit W Vermunt,Jing Luan,Zhe Zhang,A Josephine Thrasher,Anran Huang,Megan S Saari,Eugene Khandros,Robert A Beagrie,Shiping Zhang,Pranay Vemulamada,Matilda Brilleman,Kiwon Lee,Jennifer A Yano,Belinda M Giardine,Cheryl A Keller,Ross C Hardison,Gerd A Blobel

Journal of Cancer 14:262-274 PubMed36741260

2023

MTA2 is one of 14 Transcription factors predicting recurrence free survival in gastric cancer and promotes cancer progression by targeting MCM5.

Applications

Unspecified application

Species

Unspecified reactive species

Anshu Li,Yan Guo,Zhijie Yin,Xinghua Liu,Gengchen Xie

BMC biology 20:294 PubMed36575438

2022

SMYD3 associates with the NuRD (MTA1/2) complex to regulate transcription and promote proliferation and invasiveness in hepatocellular carcinoma cells.

Applications

Unspecified application

Species

Unspecified reactive species

Yang Yang,Rongfang Qiu,Siyu Zhao,Lin Shen,Bufu Tang,Qiaoyou Weng,Ziwei Xu,Liyun Zheng,Weiqian Chen,Gaofeng Shu,Yajie Wang,Zhongwei Zhao,Minjiang Chen,Jiansong Ji
View all publications

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