ArticleProtein expression and purification2011
Expression and purification of full-length mouse CARM1 from transiently transfected HEK293T cells using HaloTag technology.
Article in Protein expression and purification, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- CARM1 regulates replication fork speed and stress response by stimulating PARP1.Molecular cell · 2021Article
- Visualizing and Manipulating Biological Processes by Using HaloTag and SNAP-Tag Technologies.Chembiochem : a European journal of chemical biology · 2020Review
- Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition.Nature communications · 2017Article
- Angiomotin regulates prostate cancer cell proliferation by signaling through the Hippo-YAP pathway.Oncotarget · 2017Article
- A Homogenous Bioluminescent System for Measuring GTPase, GTPase Activating Protein, and Guanine Nucleotide Exchange Factor Activities.Assay and drug development technologies · 2015Article
- HaloTag technology: a versatile platform for biomedical applications.Bioconjugate chemistry · 2015Review
- Angiomotin is a novel component of cadherin-11/β-catenin/p120 complex and is critical for cadherin-11-mediated cell migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Polyethyleneimine-based transient gene expression processes for suspension-adapted HEK-293E and CHO-DG44 cells.Protein expression and purification · 2013Article
- CARM1 automethylation is controlled at the level of alternative splicing.Nucleic acids research · 2013Article
- Application of HaloTag technology to expression and purification of cannabinoid receptor CB2.Protein expression and purification · 2013Article
- HaloTag, a Platform Technology for Protein Analysis.Current chemical genomics · 2012Article
- Development of a dehalogenase-based protein fusion tag capable of rapid, selective and covalent attachment to customizable ligands.Current chemical genomics · 2012Article
- HaloTag: a novel reporter gene for positron emission tomography.American journal of translational research · 2011Article
- Transforming growth factor beta-induced reactivation of Epstein-Barr virus involves multiple Smad-binding elements cooperatively activating expression of the latent-lytic switch BZLF1 gene.Journal of virology · 2011Article
- Automethylation of CARM1 allows coupling of transcription and mRNA splicing.Nucleic acids research · 2011Article
- Challenges and opportunities in the purification of recombinant tagged proteins.Biotechnology advancesReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Coactivator-associated arginine methyl transferase 1 (CARM1) is a protein arginine methyltransferase (PRMT) family member that functions as a coactivator in androgen and estrogen signaling pathways and plays a role in the progression of prostate and breast cancer. CARM1 catalyzes methylation of diverse protein substrates. Prior attempts to purify the full-length mouse CARM1 protein have proven unsatisfactory. The full-length protein expressed in Escherichia coli forms insoluble inclusion bodies that are difficult to denature and refold. The presented results demonstrate the use of a novel HaloTag™ technology to purify full-length CARM1 from both E. coli and mammalian HEK293T cells. A small amount of CARM1 was purified from E. coli; however, the protein was truncated on the N-terminus by 10-50 amino acids, most likely due to endogenous proteolytic activity. In contrast, substantial quantities of soluble full-length CARM1 were purified from transiently transfected HEK293T cells. The CARM1 from HEK293T cells was isolated alongside a number of co-purifying interacting proteins. The covalent bond formed between the HaloTag and the HaloLink resin allowed the use of stringent wash conditions without risk of eluting the CARM1 protein. The results also illustrate a highly effective approach for purifying and enriching both CARM1-associated proteins as well as substrates for CARM1's methyltransferase activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.