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
- IHC-P
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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.
- ICC/IF
Unknown
Immunocytochemistry/ Immunofluorescence - Anti-MTA2/PID antibody (AB8106)
Immunofluorescence of PID in HeLa cells using ab8106 at 10 ug/ml.
- ICC/IF
Unknown
Immunocytochemistry/ Immunofluorescence - Anti-MTA2/PID antibody (AB8106)
ab8106 at 10μg/ml staining MTA2/PID in Hela cells by ICC/IF
- 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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- 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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Reactivity data
出荷温度及び保存条件
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出荷温度
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補足情報
This supplementary information is collated from multiple sources and compiled automatically.
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.
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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
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Life science alliance 7: PubMed38649186
2024
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International journal of molecular sciences 25: PubMed38474064
2024
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Cancer research 84:241-257 PubMed37963210
2023
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Cancer communications (London, England) 43:1117-1142 PubMed37658635
2023
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PLoS pathogens 19:e1011477 PubMed37410772
2023
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Journal of cell science 136: PubMed36861403
2023
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Molecular cell 83:715-730.e6 PubMed36868189
2023
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Journal of Cancer 14:262-274 PubMed36741260
2023
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BMC biology 20:294 PubMed36575438
2022
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