ArticleJournal of industrial microbiology & biotechnology2012
Soluble expression of recombinant human CD137 ligand in Escherichia coli by co-expression of chaperones.
Article in Journal of industrial microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
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.
Who cites it
0 citing papers in PubMed, 10 citations in OpenAlex.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CD137 ligand (CD137L) is a member of the tumor-necrosis factor superfamily that binds CD137 to provide positive co-stimulatory signals for T cells activation. Co-stimulation through CD137/CD137L has become one of the promising approaches for cancer therapy. Previous reports have shown that CD137L expressed in Escherichia coli resulted in inclusion bodies or low yield. In this study, the effects of five different chaperone teams on the soluble expression of recombinant human CD137L protein were explored and analyzed. The poor expression of CD137L in the cytoplasm of E. coli was improved significantly by co-expression of chaperone GroES-GroEL-Tf. After dual induction and affinity chromatography, purified recombinant CD137L was obtained at a yield of 3 mg protein per liter with purity greater than 98% from original undetectable level. Additionally, the purified recombinant CD137L could bind CD137-positive cells in a dose-dependent manner, markedly promote the growth of activated mice T cells, and elevate the release of IL-2. The present work provides an effective system for soluble expression of functional human co-stimulatory molecule CD137L, which will facilitate the clinical developments of recombinant protein drugs.
Indexed as
Identifiers
What OpenQuestion holds
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.