Evidence map›Paper›PMID 23115610›Full record

ArticleCurrent chemical genomics2012

The HaloTag: Improving Soluble Expression and Applications in Protein Functional Analysis.

Scott N Peterson, Keehwan Kwon

Abstract read
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Article in Current chemical genomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
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  9. Cooperative assembly of a four-molecule signaling complex formed upon T cell antigen receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. Nuclear Import ofFrontiers in plant science · 2018
    Article
  12. Article
  13. Article
  14. Review
  15. Expression, purification and crystallization of the SKICH domain of human TAX1BP1.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  16. Article
  17. A genetically encoded fluorescent probe in mammalian cells.Journal of the American Chemical Society · 2013
    Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Scott N PetersonJ. Craig Venter Institute, 9704 Medical Center Drive, Rockville, Maryland 20850, USA.
Keehwan Kwon

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Technological and methodological advances have been critical for the rapidly evolving field of proteomics. The development of fusion tag systems is essential for purification and analysis of recombinant proteins. The HaloTag is a 34 KDa monomeric protein derived from a bacterial haloalkane dehalogenase. The majority of fusion tags in use today utilize a reversible binding interaction with a specific ligand. The HaloTag system is unique in that it forms a covalent linkage to its chloroalkane ligand. This linkage permits attachment of the HaloTag to a variety of functional reporters, which can be used to label and immobilize recombinant proteins. The success rate for HaloTag expression of soluble proteins is very high and comparable to maltose binding protein (MBP) tag. Furthermore, cleavage of the HaloTag does not result in protein insolubility that often is observed with the MBP tag. In the present report, we describe applications of the HaloTag system in our ongoing investigation of protein-protein interactions of the Y. pestis Type 3 secretion system on a custom protein microarray. We also describe the utilization of affinity purification/mass spectroscopy (AP/MS) to evaluate the utility of the Halo Tag system to characterize DNA binding activity and protein specificity.

Indexed as

E. coli RpoA.expressionHaloTagimmobilizationprotein-DNA interactionsprotein-protein interactionsType 3 secretion factors

Identifiers

PMID23115610
PMCPMC3480702

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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.