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Biological Activity for Thalidomide
Thalidomide is a selective inhibitor of tumor necrosis factor α (TNF-α) synthesis. Anti-inflammatory; promotes T-cell activation. Predicted to reduce cytokine release in SARS-CoV-2 infection. Also binds cereblon, inhibiting ubiquitin ligase activity. Teratogenic and sedative-hypnotic. Promotes degradation of transcription factor SALL4.
Technical Data for Thalidomide
|Storage||Store at RT|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
Solubility Data for Thalidomide
|Solvent||Max Conc. mg/mL||Max Conc. mM|
Preparing Stock Solutions for Thalidomide
The following data is based on the product molecular weight 258.23. Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.
|Concentration / Solvent Volume / Mass||1 mg||5 mg||10 mg|
|0.25 mM||15.49 mL||77.45 mL||154.9 mL|
|1.25 mM||3.1 mL||15.49 mL||30.98 mL|
|2.5 mM||1.55 mL||7.75 mL||15.49 mL|
|12.5 mM||0.31 mL||1.55 mL||3.1 mL|
References for Thalidomide
References are publications that support the biological activity of the product.
Boireau et al (1997) Thal. reduces MPTP-induced decrease in striatal DA levels in mice. Neurosci.Lett. 234 123 PMID: 9364513
Kanbayashi et al (1996) Thal., a hypnotic with immune modulating properties, increases cataplexy in canine narcolepsy. Neuroreport 7 1881 PMID: 8905685
Makonkawkeyoon et al (1993) Thal. inhibits the replication of human-immunodeficiency-virus type 1. Proc.Natl.Acad.Sci.U.S.A. 90 5974 PMID: 8327469
Zhang et al (2008) Thal. influences growth and vasculogenic mimicry channel formation in melanoma. J.Exp.Clin.Cancer Res. 27 60 PMID: 18983651
Sampaio et al (1991) Thal. selectively inhibits tumor necrosis factor α production by stimulated human monocytes. J.Exp.Med. 173 699 PMID: 1997652
Merck Index 12 9390
Ito et al (2010) Identification of a primary target of Thal. teratogenicity. Science 327 1345 PMID: 20223979
Donovan et al (2018) Thal. promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray Syndrome. Elife 7 e38430 PMID: 30067223
Li et al (2021) Network bioinformatics analysis provides insight into drug repurposing for COVID-2019. Med.Drug Discov. 10 PMID: 33817623
If you know of a relevant reference for Thalidomide, please let us know.
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Keywords: Thalidomide, Thalidomide supplier, TNF-α, TNF-alpha, alfa, synthesis, inhibitors, inhibits, Tumor, Necrosis, Factor-α, Cytokines, Signaling, Signalling, angiogenesis, teratogen, anti-inflammatory, cereblon, ubiquitin, E3, ligase, modulator, CELMoD, SALL4, SARS-Cov-2, COVID-19, coronaviruses, Antiangiogenics, Ubiquitin, Ligases, Other, Transcription, Factors, Molecular, Glues, 0652, Tocris Bioscience
12 Citations for Thalidomide
Citations are publications that use Tocris products. Selected citations for Thalidomide include:
Helmy et al (2015) Additive Renoprotection by pioglit. and fenofi. against Inflammatory, Oxidative and Apoptotic Manifestations of cisp. Nephrotoxicity: Modulation by PPARs. PLoS One 10 e0142303 PMID: 26536032
Eter and Spitznas (2002) DMSO mimics inhibitory effect of Thal. on choriocapillary endothelial cell proliferation in culture. Oncol Lett 86 1303 PMID: 12386094
Sung et al (2009) Curcumin circumvents chemoresistance in vitro and potentiates the effect of Thal. and borte. against human multiple myeloma in nude mice model. Mol Cancer Ther 8 959 PMID: 19372569
Prete et al (2016) Amyloid Precursor Protein (APP) May Act as a Substrate and a Recognition Unit for CRL4CRBN and Stub1 E3 Ligases Facilitating Ubiquitination of Proteins Involved in Presynaptic Functions and Neurodegeneration. J Biol Chem 291 17209 PMID: 27325702
Girgis et al (2010) Effect of Thal. and arsenic trioxide on the release of tumor necrosis factor-α and vascular endothelial growth factor from the KG-1a human acute myelogenous leukemia cell line. MBio 1 663 PMID: 22966360
Kannappan et al (2010) γ-Tocotrienol but not γ-tocopherol blocks STAT3 cell signaling pathway through induction of protein-tyrosine phosphatase SHP-1 and sensitizes tumor cells to chemotherapeutic agents. J Biol Chem 285 33520 PMID: 20720018
Gu et al (2010) Intraperitoneal injection of Thal. attenuates bone cancer pain and decreases spinal tumor necrosis factor-α expression in a mouse model. Mol Pain 6 64 PMID: 20923560
Pandey et al (2010) Betulinic acid suppresses STAT3 activation pathway through induction of protein tyrosine phosphatase SHP-1 in human multiple myeloma cells. Int J Cancer 127 282 PMID: 19937797
Sandur et al (2010) 5-hydroxy-2-methyl-1,4-naphthoquinone, a vitamin K3 analogue, suppresses STAT3 activation pathway through induction of protein tyrosine phosphatase, SHP-1: potential role in chemosensitization. Mol Cancer Res 8 107 PMID: 20068065
Ahn et al (2007) Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NF-kappaB regulated gene products. Blood 110 2286 PMID: 17609425
Pathak et al (2007) Ursolic acid inhibits STAT3 activation pathway leading to suppression of proliferation and chemosensitization of human multiple myeloma cells. Mol Cancer Res 5 943 PMID: 17855663
Rocha et al (2006) Relevance of tumour necrosis factor-alpha for the inflammatory and nociceptive responses evoked by carrageenan in the mouse paw. Br J Pharmacol 148 688 PMID: 16702985
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Literature in this Area
Tocris offers the following scientific literature in this area to showcase our products. We invite you to request* your copy today!
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Targeted Protein Degradation Research Product Guide
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Programmed Cell Death Poster
There are two currently recognized forms of programmed cell death: apoptosis and necroptosis. This poster summarizes the signaling pathways involved in apoptosis, necroptosis and cell survival following death receptor activation, and highlights the influence of the molecular switch, cFLIP, on cell fate.
Targeted Protein Degradation Poster
Degraders (e.g. PROTACs) are bifunctional small molecules, that harness the Ubiquitin Proteasome System (UPS) to selectively degrade target proteins within cells. They consist of three covalently linked components: an E3 ubiquitin ligase ligand, a linker and a ligand for the target protein of interest. Authored in-house, this poster outlines the generation of a toolbox of building blocks for the development of Degraders. The characteristics and selection of each of these components are discussed. Presented at EFMC 2018, Ljubljana, Slovenia