This is a working overview of REV-ERB, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2026-05-25 and is reviewed periodically as new material appears.
Laboratory identification of SR9009 typically relies on chromatographic separation coupled to mass spectrometry, often with ultraviolet detection as a secondary check. Nuclear magnetic resonance spectroscopy can confirm molecular structure when a reference standard is available. Because many suppliers sell the compound as a research chemical, independent identity testing is important for experimental reproducibility. A single retention time is not sufficient proof of identity, especially when related compounds may be present. Purity assessments usually report a percentage based on area normalization.
SR9009 is generally described as poorly soluble in water and more soluble in organic solvents such as dimethyl sulfoxide and ethanol. Stock solutions are commonly prepared in an organic solvent before dilution into an aqueous buffer or vehicle. Precipitation can occur if the organic fraction is reduced too quickly or if the final concentration exceeds the compound's solubility limit. Sonication or gentle warming may aid dissolution in some protocols, but excessive heat can promote degradation. Container material and pH can also influence observed solubility.
For long-term storage, SR9009 is typically kept as a solid at low temperature, protected from moisture and light. Desiccated conditions limit hydrolysis, while opaque containers reduce photochemical breakdown. Solutions are less stable than solids and are often stored frozen in aliquots to avoid repeated freeze-thaw cycles. Stability data are not standardized across all suppliers, so users should rely on certificate-of-analysis information when available. Degradation may appear as color change, precipitate, or decreased chromatographic purity.
SR9009 is a synthetic small molecule developed as an agonist of the nuclear receptors REV-ERBα (NR1D1) and REV-ERBβ (NR1D2). These receptors help regulate circadian rhythms and metabolic gene expression. In cell and animal studies, SR9009 alters transcription of genes involved in lipid metabolism, inflammation, and mitochondrial function. It is not an approved medicine, and its pharmacological profile in humans remains largely uncharacterized. The compound is frequently discussed in the context of circadian biology and metabolic research rather than clinical use.
Preclinical reports have linked SR9009 to improved endurance and altered energy expenditure in rodents. Such findings have prompted interest in whether REV-ERB activation can influence skeletal muscle metabolism. However, the reported effects depend on dose, route, and experimental model, and replication across laboratories is limited. Human trials have not established comparable outcomes, so claims about exercise performance remain speculative. The absence of controlled human data is a central limitation in interpreting these observations.
| Property | Value | Notes |
|---|---|---|
| Appearance | White to off-white powder | Visual inspection is not sufficient for identity. |
| Solubility | Soluble in DMSO and ethanol | Low solubility in water; stock solutions use organic solvent. |
| Storage | -20°C, desiccated, protected from light | Limits hydrolysis and photodegradation. |
| Analytical method | HPLC-UV/MS | Used for identity and purity assessment. |
| Synonyms | SR9009, Stenabolic | Naming varies by supplier. |
At the molecular level, SR9009 binds the ligand-binding domain of REV-ERB and strengthens recruitment of corepressor proteins such as NCoR and HDAC3. This increases repression of target genes, including Bmal1 and other clock-controlled and metabolic genes. In rodent studies, such changes have been linked to altered lipid handling, glucose metabolism, and energy expenditure. The precise chain of events between receptor binding and whole-body effects remains an active area of research. Findings in animals do not automatically translate to humans.
Laboratory studies often administer SR9009 by injection because oral absorption appears poor in rodents. Reported pharmacokinetic properties include rapid metabolism and low systemic exposure after oral dosing. Human pharmacokinetic data are sparse, so absorption, distribution, metabolism, and excretion in people are not well defined. Some research explores related REV-ERB compounds with improved drug-like properties. Regulatory approval for any REV-ERB agonist as a human medicine has not been granted to date.
SR9009 is a synthetic small molecule studied as an agonist of the nuclear receptors REV-ERBα and REV-ERBβ. It is not an approved medicine and has no established human therapeutic use. The compound appears in scientific literature as a tool for probing circadian and metabolic regulation. Online sellers often label it as a research chemical, sometimes using the nickname Stenabolic. Its chemical identity is distinct from selective androgen receptor modulators, stimulants, and peroxisome proliferator-activated receptor delta agonists. Researchers use it mainly in cell and animal experiments.
At the molecular level, SR9009 binds REV-ERBα and REV-ERBβ and alters their repressive activity on target genes. These nuclear receptors help regulate the circadian clock, lipid synthesis, glucose metabolism, and inflammatory pathways. By changing transcription, the compound can shift the timing or magnitude of downstream metabolic processes in model systems. It does not act through androgen receptors or adenosine receptors, which distinguishes it from several substances sold for athletic performance. Whether the same transcriptional changes occur in humans at tolerable exposures remains an open question because controlled human studies are lacking.
Preclinical reports describe effects on exercise endurance, mitochondrial content, and lipid profiles in rodents, but these findings come from specific experimental conditions. Many studies use high doses or delivery methods that may not translate directly to human use. SR9009 has been reported to have low oral bioavailability and a short half-life, which complicates interpretation of oral dosing studies. It is not established as safe or effective for any indication. Literature discussions often separate its pharmacological mechanism from unverified claims made in fitness and supplement markets.
Laboratory samples of SR9009 are typically handled as research chemicals rather than pharmaceuticals. Suppliers usually state that the material is for research use only and not for human or veterinary administration. Storage recommendations generally call for a freezer at approximately −20 °C, protection from light, and a desiccated environment. The solid is often described as a white to off-white powder. Solubility is commonly reported in organic solvents such as dimethyl sulfoxide and ethanol, with low solubility in water.
Analytical identification and purity assessment often use high-performance liquid chromatography with ultraviolet detection or mass spectrometry. Liquid chromatography–tandem mass spectrometry is used to detect and quantify SR9009 in biological matrices, including urine and blood, for anti-doping or pharmacokinetic studies. Nuclear magnetic resonance spectroscopy can confirm molecular structure. Stability depends on form and storage: the solid is generally more stable than solutions, and repeated freeze–thaw cycles may degrade samples. Purity is typically reported as a percentage from a certificate of analysis.
Regulatory treatment of SR9009 varies by country and context. It is not approved as a therapeutic drug by agencies such as the United States Food and Drug Administration or the European Medicines Agency. Sports authorities list it as a prohibited substance; the World Anti-Doping Agency classifies it among hormone and metabolic modulators. Legal status for personal possession or sale differs across jurisdictions, and some countries may restrict it under analog or research chemical laws. Buyers who seek verified material often rely on independent laboratory testing because online product labels may not match contents.
Transferrin receptor 2 (TfR2) is a protein that in humans is encoded by the TFR2 gene. This protein is involved in the uptake of transferrin-bound iron into cells by endocytosis, although its role is minor compared to transferrin receptor 1.
The colony's participation in the Empire Air Training Scheme is described in J F MacDonald's War History of Southern Rhodesia as "undoubtedly Southern Rhodesia's greatest single contribution to the Allied victory", an assertion corroborated by Robert Blake in his 1977 History of Rhodesia. The Rhodesian Air Training Group (RATG) under Air Vice-Marshal Sir C W Meredith eventually operated 11 aerodromes, requiring a huge national effort to build, maintain and staff—at the scheme's peak more than a fifth of the white population was involved. This judicious management of skills and resources allowed the territory to make a much larger contribution to the Allied war effort than if it had simply sent all its manpower into the field. Southern Rhodesia was regarded as an ideal location for air training for a number of reasons. It was far from the hostilities, firmly pro-British and had excellent weather throughout the year. The British Air Ministry resolved to outsource training to the colony amid some urgency in late 1939 after EATS took a long time to get going in Canada. The RATG was the last EATS group to be formed, but the first to start training airmen; it also turned out fully qualified pilots before any of the others, doing so for the first time in November 1940. The programme originally called only for an initial training wing and six schools, but this was expanded to eight flying schools and a school for bomb aimers, navigators and air gunners. There were two air firing and bombing ranges.
=== Cell turnover === Fat cells in some mice have been shown to drop in count due to fasting and other properties were observed when exposed to cold. If the adipocytes in the body reach their maximum capacity of fat, they may replicate to allow additional fat storage.
Sources: en.wikipedia.org
=== LTG4 === There has also been postulated the existence of LTG4, a metabolite of LTE4 in which the cysteinyl moiety has been oxidized to an alpha-keto-acid (i.e.—the cysteine has been replaced by a pyruvate). Very little is known about this putative leukotriene.
=== Intersubunit bridges === Contacts across the two ribosomal subunits are known as intersubunit bridges. In the eukaryotic ribosome, additional contacts are made by 60S expansion segments and proteins. Specifically, the C-terminal extension of the 60S protein RPL19 interacts with ES6E of the 40S rRNA, and the C-terminal extension of the 60S protein RPL24 interacts with 40S rpS6 and rRNA helix h10. Moreover, the 60S expansion segments ES31 and ES41 interact with rpS3A(S1) and rpS8 of the 40S subunit, respectively, and the basic 25-amino-acid peptide RPL41 is positioned at the subunit interface in the 80S ribosome, interacting with rRNA elements of both subunits.
There are many geological issues concerning the rivers and streams of the Appalachians. In spite of the existence of the Great Appalachian Valley, many of the main rivers are transverse to the mountain system axis. The drainage divide of the Appalachians follows a tortuous course that crosses the mountainous belt just north of the New River in Virginia. South of the New River, rivers head into the Blue Ridge, cross the higher Unakas, receive important tributaries from the Great Valley, and traversing the Cumberland Plateau in spreading gorges (water gaps), escape by way of the Cumberland River and the Tennessee River rivers to the Ohio River and the Mississippi River, and thence to the Gulf of Mexico. In the central section, north of the New River, the rivers, rising in or just beyond the Valley Ridges, flow through great gorges to the Great Valley, and then across the Blue Ridge to tidal estuaries penetrating the coastal plain via the Roanoke River, James River, Potomac River, and Susquehanna River. In the northern section, the height of land lies on the inland side of the mountainous belt, and thus the main lines of drainage run from north to south, exemplified by the Hudson River. However, the valley through which the Hudson River flows was cut by the gigantic glaciers of the ice ages—the same glaciers that deposited their terminal moraines in southern New York and formed the east–west Long Island.
== Skyscrapers == The German building research firm Emporis ranks world cities by the number of their skyscrapers. Emporis defines a skyscraper as "...any multilevel building with an architectural height of at least 100 metres." Bangkok ranks number seven of the 100 cities with the most skyscrapers. Bangkok has 376. Other ASEAN cities listed are Singapore, ranked 4 with 506 skyscrapers; Kuala Lumpur, ranked 14 with 202; Jakarta, ranked 17 with 181; Hanoi, ranked 36 with 120; Ho Chi Minh City, ranked 43 with 103; and Manila, ranked 93 with 37 skyscrapers.
Sources: en.wikipedia.org
=== Homogeneous screening of yoctoreactor libraries === A homogeneous method for screening yoctoreactor libraries (yR) has recently been developed which uses water-in-oil emulsion technology to isolate individual ligand-target complexes. Called Binder Trap Enrichment (BTE), ligands to a protein target are identified by trapping binding pairs (DNA-labelled protein target and yR ligand) in emulsion droplets during dissociation dominated kinetics. Once trapped, the target and ligand DNA are joined by ligation, thus preserving the binding information. Hereafter, identification of hits is essentially a counting exercise: information on binding events is deciphered by sequencing and counting the joined DNA - selective binders are counted with a much higher frequency than random binders. This is possible because random trapping of target and ligand is "diluted" by the high number of water droplets in the emulsion. The low noise and background signal characteristic of BTE is attributed to the "dilution" of the random signal, the lack of surface artifacts and the high fidelity of the yR library and screening method. Screening is performed in a single tube method. Biologically active hits are identified in a single round of BTE characterized by a low false positive rate. BTE mimics the non-equilibrium nature of in vivo ligand-target interactions and offers the unique possibility to screen for target specific ligands based on ligand-target residence time because the emulsion, which traps the binding complex, is formed during a dynamic dissociation phase.
Bats possess a highly adapted respiratory system to cope with the demands of powered flight. They have relatively large lungs, and many species have proportionally larger alveolar surface areas and pulmonary capillary blood volumes than other mammals. During flight, the respiratory cycle has a one-to-one relationship with the wing-beat cycle. Their mammalian lungs prevent them from flying at high altitudes. Bats can also meet oxygen demands by exchanging gas through the patagium of the wing. When the bat has its wings spread, it allows for an increase in surface area to volume ratio, 85% of the surface area being the wing. The subcutaneous vessels in the membrane lie near the surface and allow for the diffusion of oxygen and carbon dioxide. The digestive system of bats varies depending on the species of bat and its diet. Digestion is relatively quick to meet the energy demands of flight. Insectivorous bats may have certain digestive enzymes to better process insects, such as chitinase to break down their chitin exoskeleton. Vampire bats, probably due to their diet of blood, are unique among vertebrates in that they do not have the enzyme maltase, which breaks down malt sugar, in their intestinal tract. Nectivorous and frugivorous bats have more maltase and sucrase enzymes than insectivores, to cope with the higher sugar contents of their diet. The adaptations of the kidneys of bats vary with their diets. Carnivorous and vampire bats consume large amounts of protein and can output concentrated urine; their kidneys have a thin cortex and long renal papillae.
Stickler syndrome, COL2A1 (75% of Stickler cases) Stickler syndrome, COL11A1 Stickler syndrome, COL11A2 (non-ocular) Stickler syndrome, COL9A1 (recessive variant) Stickler syndrome, COL9A2 (recessive variant) Stickler syndrome, COL9A3 (recessive variant) Stickler Syndrome, LOX3 (Recessive, 7 cases reported) Whether there are two or three types of Stickler syndrome is controversial. Each type is presented here according to the gene involved. The classification of these conditions is changing as researchers learn more about the genetic causes.
Sources: en.wikipedia.org
Liquid chromatography with mass spectrometry is a common approach. Ultraviolet detection and nuclear magnetic resonance can support identification when suitable standards are available.
The solid is generally kept cold, dry, and protected from light. Solutions are often frozen in single-use aliquots to reduce repeated freeze-thaw cycles.
It indicates a material sold for laboratory study, not for human use. The label does not guarantee pharmaceutical purity, sterility, or regulatory approval.
It is a synthetic compound that acts as an agonist at REV-ERBα and REV-ERBβ. It is used mainly as a research chemical to study circadian and metabolic pathways. It is not approved for human therapeutic use.