Anti-MED12 antibody
5
(3 Reviews)
|
(14 Publications)
Rabbit Polyclonal MED12 antibody. Suitable for IHC-P, IP, WB, ICC/IF and reacts with Human, Mouse samples. Cited in 14 publications. Immunogen corresponding to Synthetic Peptide within Human MED12 aa 2150-2200.
View Alternative Names
ARC240, CAGH45, HOPA, KIAA0192, TNRC11, TRAP230, MED12, Mediator of RNA polymerase II transcription subunit 12, Activator-recruited cofactor 240 kDa component, CAG repeat protein 45, Mediator complex subunit 12, OPA-containing protein, Thyroid hormone receptor-associated protein complex 230 kDa component, Trinucleotide repeat-containing gene 11 protein, Trap230
- IHC-P
Unknown
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-MED12 antibody (AB70842)
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human breast carcinoma tissue labelling MED12 with ab70842 at 1/1000 (1µg/ml). Detection : DAB.
- IP
Unknown
Immunoprecipitation - Anti-MED12 antibody (AB70842)
Detection of Human MED12 by Immunoprecipitation using Whole cell lysate from HeLa cells (1 mg for IP, 20% of IP loaded), using ab70842 for IP at 3 µg/mg lysate. Subsequent WB detection was performed using ab70842 at 1 µg/ml.
All lanes:
Immunoprecipitation - Anti-MED12 antibody (ab70842)
Predicted band size: 243 kDa
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- WB
Unknown
Western blot - Anti-MED12 antibody (AB70842)
All lanes:
Western blot - Anti-MED12 antibody (ab70842) at 0.1 µg/mL
Lane 1:
Whole cell lysate from HeLa cells at 50 µg
Lane 2:
Whole cell lysate from HeLa cells at 15 µg
Lane 3:
Whole cell lysate from HeLa cells at 5 µg
Lane 4:
Whole cell lysate from 293T cells at 50 µg
Lane 5:
Whole cell lysate from NIH 3T3 cells at 50 µg
Predicted band size: 243 kDa
Observed band size: 238 kDa,65 kDa
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Exposure time: 3min
- WB
CiteAb
Western blot - Anti-MED12 antibody (AB70842)
MED12 western blot using anti-MED12 antibody ab70842. Publication image and figure legend from Shishkova, E., Zeng, H., et al., 2017, Nat Commun, PubMed 28537268.
ab70842 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab70842 please see the product overview.
Requirement of the N-terminal domain for substrate recognition by CARM1.(a) Schematic diagram of FL and N-terminal truncated CARM1 derivatives. CARM1 FL protein contained 608 residues. CARM1 28–608 lacks the first, unstructured 28 residues denoted in grey. CARM1 140–608 lacks the first 140 residues encompassing the EVH1 domain denoted in green. (b) Western blot analyses of co-immunoprecipitated BAF155, MED12, PABP1, NCOA3 and TET2 with FLAG-tagged CARM1, transiently transfected into HEK293T CARM1 KO cells. CARM1 was immunoprecipiated with the anti-FLAG antibody, and the presence of BAF155, MED12, PABP1, NCOA3 and TET2 in the immunoprecipitates was detected with western blots using the respective antibodies. The loading controls are depicted below the corresponding western blot results, separately for BAF155, MED12 and PABP1, and the other two proteins. In all cases the amount of co-precipitated protein was strongly reduced in cell lines expressing N-terminus truncated CARM1 140–608. (c) Western blot analyses of total ADMA-containing proteins co-precipitated with CARM1. The FLAG-tagged CARM1 immunoprecipitates in b were probed with ADMA antibodies. The strong reduction in the levels of ADMA—containing proteins in cells expressing CARM1 140–680 was evident on both short (left) and long exposure (right). The corresponding loading control was shared between the experiments in b (BAF155, MED12 and PABP1) and c and is depicted in b labelled with IB : FLAG. (d) FP assay using purified recombinant 6xHis-CARM1 28–140 and fluorescein-labelled BAF155 peptide. Pronounced increase in FP was observed at high concentrations of recombinant CARM1, but not with the BSA control, demonstrating that the EVH1 domain of CARM1 directly interacts with the enzyme's substrate at low affinity. (e) Coomassie Blue staining of highly purified recombinant 6xHis-CARM1 28–140 used in the FP assay (d).
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Reactivity data
Properties and storage information
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Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MED12 functions as a core component of the larger Mediator complex which plays an important role in controlling RNA polymerase II-dependent genes. Through interactions with activators and repressors MED12 participates in chromatin modification and looping affecting gene transcription rates. It is enriched in tissues where fine control of gene expression is essential impacting growth differentiation and development processes.
Pathways
MED12 integrates into critical signaling pathways including the Wnt/β-catenin and Hedgehog pathways. In these pathways MED12 interacts with other proteins like β-catenin serving as a connecting node that influences the transcription of target genes essential for cell proliferation and differentiation. Such interactions help coordinate cellular responses to external signals and ensure proper pathway regulation.
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Target data
Publications (14)
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Communications biology 8:1180 PubMed40775066
2025
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American journal of cancer research 13:1999-2012 PubMed37293147
2023
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Cell reports 41:111852 PubMed36543134
2022
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Molecular metabolism 48:101227 PubMed33812059
2021
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Cell death & disease 10:387 PubMed31097718
2019
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Molecular cancer 18:93 PubMed31072327
2019
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The Journal of biological chemistry 294:9076-9083 PubMed31028171
2019
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Molecular cell 73:250-263.e5 PubMed30527662
2018
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eNeuro 4: PubMed28955722
2017
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Nature communications 8:15571 PubMed28537268
2017
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WB
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Product promise
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