A practical reference on REV-ERB agonist: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-08-01. Anything still debated is marked as such rather than presented as settled.
Regulatory and sporting contexts treat SR9009 as a prohibited substance in many elite competitions. Its presence on banned lists reflects concerns about performance enhancement and unknown long-term safety. Analytical chemists have developed methods to detect the parent compound and its metabolites in urine and blood. Literature discussions distinguish between in vitro potency, animal pharmacology, and anecdotal human reports. The latter are difficult to verify because products sold online may lack purity or contain different compounds.
SR9009 is a synthetic small molecule studied as an agonist of the nuclear receptors REV-ERBα and REV-ERBβ. These receptors help regulate circadian rhythms, lipid metabolism, and inflammatory gene expression. In cell and animal experiments, SR9009 alters transcription of clock-controlled genes and metabolic pathways. The compound is not a hormone and does not resemble classical steroid structures. Its activity depends on binding to the ligand-binding domain of REV-ERB, where it can modify corepressor recruitment.
Research interest in SR9009 grew from studies of circadian biology and metabolic disease. Preclinical reports describe effects on exercise capacity, muscle metabolism, and blood lipid levels in rodents, but these findings come from controlled laboratory settings. The compound has low oral bioavailability in animals, which limits systemic exposure after swallowing. Investigators often use injected routes in experiments to achieve measurable plasma concentrations. Human clinical data are sparse, no approved therapeutic product exists, and whether animal effects translate to humans remains an open question.
REV-ERB proteins typically suppress gene expression by recruiting corepressor complexes to DNA response elements. SR9009 binds these receptors and strengthens that repressive action in cell-based assays. Studies in rodents have reported changes in lipid handling, mitochondrial function, and exercise capacity after treatment. Such findings are often cited as evidence for metabolic effects, but species differences and limited pharmacokinetic data make direct translation to humans uncertain. Researchers continue to examine which effects are robust and which depend on specific experimental conditions.
SR9009 is frequently discussed alongside other REV-ERB ligands, including synthetic agonists and natural heme-related molecules. Its selectivity for REV-ERB over related nuclear receptors has been measured in binding and reporter assays, though off-target activity at higher concentrations is possible. The compound is prohibited in sport by the World Anti-Doping Agency, and it is not approved for any medical use in major jurisdictions. Products sold online may be labeled as research chemicals, and their identity and purity are not guaranteed by regulatory review.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic REV-ERB agonist | Binds REV-ERBα and REV-ERBβ in preclinical models |
| Molecular formula | C20H24ClN3O4S | Reported for the parent compound |
| CAS Registry Number | 1379686-30-2 | Common identifier in chemical databases |
| Appearance | Off-white to pale yellow solid | Typical research chemical solid |
| Solubility | Soluble in DMSO and ethanol; low in water | Class: small organic molecule |
Analytical chemists detect SR9009 with liquid chromatography-tandem mass spectrometry, commonly abbreviated LC-MS/MS. Sample preparation may involve protein precipitation, liquid-liquid extraction, or solid-phase extraction before analysis. Laboratories can target the parent compound or its metabolites, depending on the matrix and the purpose of testing. Anti-doping methods require sensitive and specific assays because concentrations in biological samples can be low. Reference standards and validated methods are essential for reliable identification and quantification.
Regulatory agencies have not approved SR9009 for human therapeutic use. It is typically sold as a research chemical with labels stating that it is not for human consumption. The World Anti-Doping Agency prohibits the substance in sport, generally under the category of non-approved substances. Customs and national laws may restrict importation, sale, or possession. Product quality and legal status can vary by country and vendor, and therapeutic claims are not permitted in regulated advertising because the compound lacks approval.
SR9009 binds REV-ERB receptors and alters their repressive activity on target genes. This action can change transcription of genes involved in lipid handling, glucose metabolism, and mitochondrial function. In rodent studies, treated animals have shown changes in muscle oxidative capacity and exercise performance, though effects vary by dose, duration, and model. The precise molecular steps connecting receptor binding to whole-body outcomes are still an active area of investigation. Findings in animals do not automatically translate to humans.
Because REV-ERB receptors are core clock components, SR9009 has been examined for effects on daily rhythms as well as metabolism. Research has explored whether the compound can shift or reinforce circadian gene expression in tissues such as liver and muscle. Some studies report improved metabolic markers in obese or diabetic mice, while others show context-dependent responses. Questions remain about which effects are direct, which are secondary to timing, and how they might differ across species.
SR9009 is a synthetic small molecule studied as an agonist of REV-ERB nuclear receptors. REV-ERB alpha and REV-ERB beta help regulate circadian rhythms and metabolic gene expression. In laboratory research, SR9009 has been used to probe how these receptors affect skeletal muscle, liver, and adipose tissue. The compound was identified in academic drug-discovery work and is often described in scientific literature by its chemical name and research code. It is not an approved medicine, and human clinical data remain limited or absent.
1996: Insulin lispro, which was originally manufactured by Eli Lilly and Company, is granted approval. 2000: Insulin aspart, which was created by Novo Nordisk, is approved. 2000: Insulin glargine, which was developed by Sanofi-Aventis, is approved. 2004: Insulin glulisine, also developed by Sanofi-Aventis, is approved. 2005: Insulin detemir, which was formulated by Novo Nordisk, gets approval. 2015: Insulin degludec, created by Novo Nordisk, is approved. 2020: Insulin lispro-aabc, a faster insulin lispro formulation created by Eli Lilly and Company, is approved. 2021: Insulin glargine-yfgn, the first approved insulin biosimilar, which is produced by Viatris, is approved. 2021: Insulin glargine-aglr, a biosimilar produced by Eli Lilly and Company, is granted approval. 2024: Insulin icodec, the newest commercially available analogue by Novo Nordisk, gets approval. 2025: Insulin aspart-szjj, the first short-acting biosimilar, created by Viatris, is approved.
had reported in February 2015 that Tagliavini was able to convince pro-Russian separatists during the negotiations of the Minsk II agreement because she had the benefit of Putin's trust. Saakashvili said in an interview in August 2019: "It was a politicised commission. It was quite bad because the whole idea behind the commission was to get the responsibility off Russia, to share the blame. [...] The Americans were categorically against it. [...] it was a Steinmeier game; I think backed by Merkel to dilute Russia's blame." The Atlantic Council members stated on anniversary of the war in 2021 that Russia and South Ossetia initiated the 2008 conflict and that the EU report was erroneous.
The size of a burn is measured as a percentage of total body surface area (TBSA) affected by partial thickness or full thickness burns. First-degree burns that are only red in color and are not blistering are not included in this estimation. Most burns (70%) involve less than 10% of the TBSA. Unit of measuring burns is VSD as 10% TBSA is equal to 1VSD. There are a number of methods to determine the TBSA, including the Wallace rule of nines, Lund and Browder chart, and estimations based on a person's palm size. The rule of nines is easy to remember but only accurate in people over 16 years of age. More accurate estimates can be made using Lund and Browder charts, which take into account the different proportions of body parts in adults and children. The size of a person's handprint (including the palm and fingers) is approximately 1% of their TBSA.
Enterovirus Hepatitis A is distinguished from other viral causes by its prolonged (2–6 week) incubation period and its ability to spread beyond the stomach and intestines into the liver. It often results in jaundice, or yellowing of the skin, but rarely leads to chronic liver dysfunction. The virus has been found to cause infection due to the consumption of fresh-cut produce which has fecal contamination. Hepatitis E Norovirus Rotavirus
Sources: en.wikipedia.org
Under Appendix I of CITES (the Convention on International Trade in Endangered Species), commercial international trade of Komodo dragon skins or specimens is prohibited. Despite this, there are occasional reports of illegal attempts to trade in live Komodo dragons. The most recent attempt was in March 2019, when Indonesian police in the East Java city of Surabaya reported that a criminal network had been caught trying to smuggle 41 young Komodo dragons out of Indonesia. The plan was said to include shipping the animals to several other countries in Southeast Asia through Singapore. It was hoped that the animals could be sold for up to 500 million rupiah (around US$35,000) each. It was believed that the Komodo dragons had been smuggled out of East Nusa Tenggara province through the port at Ende in central Flores. In 2013, the total population of Komodo dragons in the wild was assessed as 3,222 individuals, declining to 3,092 in 2014 and 3,014 in 2015. Populations remained relatively stable on the bigger islands (Komodo and Rinca), but decreased on smaller islands, such as Nusa Kode and Gili Motang, likely due to diminishing prey availability. On Padar, a former population of Komodo dragons has recently become extirpated, of which the last individuals were seen in 1975. It is widely assumed that the Komodo dragon died out on Padar following a major decline of populations of large ungulate prey, for which poaching was most likely responsible.
=== RMI Training === Remote Medical International provides remote medicine training courses taught by professionally trained and clinically active practitioners. RMI has trained over 13,000 students through public and private training courses including Wilderness First Aid, Wilderness First Responder, Remote Emergency Medical Technician, Remote Medicine for the Advanced Provider, and multiple recertification courses. RMI students include: all branches of the US military, energy companies, US intelligence agencies, law enforcement, FBI, executive protection, border patrol, special operations, national research organizations, National Park and Forest Services, universities, science foundations, guiding services, and individual adventurers.
==== Adsorption and fusion ==== Sendai virus initiates infection process by host cell adsorption mediated by the recognition of specific receptor molecules. Hemagglutinin neuraminidase (HN) serves as a virus cell attachment protein that interacts with a specific cell entry receptor. NH has sialidase activity, and it is capable of cleaving sialic acid residues from the cell receptor. This cleavage triggers the fusion process of viral envelope and cell membrane, which promotes by cooperation of NH with the viral fusion protein (F). The SeV F-protein as other Paramyxovirus structural fusion proteins is a trimeric molecule that belongs to class I viral membrane fusion proteins. To perform the fusion function F protein must be proteolytically activated from it precursor inactive form F0. This activation requires F0 cleavage by host serine protease before the virus adsorption (see the section "proteolytic cleavage by cellular proteases"). F0 must be cleaved by the host protease into F1 and F2 subunits that remained connected through a disulfide covalent bond. The cleavage site in the F0-protein is located N-terminal to the fusion peptide which has N-terminal hepta-repeat 1 (HR1) and C-terminal Hepta-Repeat 2 (HR2) domains. The illustration below shows 5 stages of the fusion of the virus envelope and cellular host membrane. 1) The pre-fusion, F protein (highlighted in red) is protruding from the lipid bilayer of the viral envelope and is in a close proximity to the cellular membrane.
Sources: en.wikipedia.org
SR9009 is a synthetic small molecule studied as an agonist of the REV-ERB nuclear receptors. It is not an approved medicine, and its effects in humans are not well characterized.
No. It is a synthetic ligand that binds nuclear receptors, not a steroid or peptide hormone. Its activity depends on receptor binding rather than endocrine secretion.
Clinical evidence is limited. Most published data come from cell and animal experiments. Human safety and efficacy remain uncertain.
SR9009 is a synthetic research compound that binds and modulates the nuclear receptors REV-ERBα and REV-ERBβ. It is used in laboratory studies of circadian biology and metabolism, not as an approved medicine. It is also known by the informal name Stenabolic.