This is a working overview of REV-ERB agonist, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2025-10-26 and is reviewed periodically as new material appears.
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.
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.
| 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 |
Laboratory samples of SR9009 are typically supplied as a white to off-white powder. The compound dissolves readily in organic solvents such as dimethyl sulfoxide and ethanol, while its solubility in water is low. Because of this solubility profile, researchers often prepare concentrated stock solutions in an organic solvent before diluting them into aqueous assay buffers. Light exposure, moisture, and repeated freeze-thaw cycles can degrade many small molecules, so handling procedures usually aim to minimize these factors. Purity is commonly checked before use.
Storage conditions for research-grade SR9009 generally involve a freezer at approximately minus twenty degrees Celsius, sometimes lower for long-term preservation. Containers should remain tightly closed and protected from light. Desiccants may be used to limit moisture uptake. Solutions are often stored in aliquots to avoid repeated warming and cooling. Stability data for the compound under various conditions are limited, so laboratories typically follow supplier recommendations and verify performance through periodic analytical checks rather than assuming indefinite stability.
Identity and purity testing for SR9009 commonly uses liquid chromatography coupled with tandem mass spectrometry. This method separates the compound from matrix components and detects it by mass-to-charge transitions, providing sensitive and specific confirmation. Nuclear magnetic resonance spectroscopy can support structural identification, while high-performance liquid chromatography with ultraviolet detection may estimate purity. Because online products labeled as SR9009 may contain other substances or no active compound at all, independent verification is important in research settings. Certificates of analysis are useful but not a substitute for in-house testing.
Mechanistically, SR9009 binds the ligand-binding domain of REV-ERBα/β and enhances recruitment of corepressor complexes. This represses target genes rather than activating them. Because REV-ERB proteins normally compete with ROR proteins at shared response elements, the net effect depends on tissue and timing. Researchers use SR9009 to probe how nuclear receptor signaling links the clock to metabolism, inflammation, and muscle biology. Findings are largely preclinical, and the precise contribution of each receptor subtype remains under study.
SR9009 is frequently discussed in fitness and research-chemical contexts, yet it has no approved medical indication. Regulatory agencies have not authorized it for human use, and it is not a standard prescription drug. Some sports organizations list it as a prohibited substance because of its potential performance-enhancing properties. Published human data are sparse, so claims about its effects in people often rely on animal models or anecdotal reports. Quality and identity of online materials can vary widely.
SR9009 is a synthetic small molecule studied as a REV-ERB agonist. REV-ERBα and REV-ERBβ are nuclear receptors that help regulate circadian rhythms and metabolic gene expression. The compound was identified in academic screening efforts to find synthetic ligands for these receptors. In cell and animal studies, SR9009 alters transcription of genes involved in lipid and glucose metabolism, and it can shift circadian behavior. It is not an approved therapeutic agent.
== Description == There is no mention of the Korean People's Revolutionary Army in documents written by Kim Il Sung himself during his time in the Soviet Army. Coined in the wake of the May 25th Instructions, the purported army is connected to Kim Il Sung's cult of personality initiated by the guerrilla faction from the Soviet Army's 88th Separate Rifle Brigade, which seized power in North Korea. The KPRA was first mentioned in the late 1940s. Korean People's Revolutionary Army was allegedly founded on 25 April 1932. North Korean historiography credits the defeat of Japan in 1945 mostly to the KPRA, downplaying Soviet involvement. From 1978, North Korea marked 25 April as the "true" founding date of the Korean People's Army (KPA), with the KPA being claimed to just be the reconstitution of the KPRA. North Korean leader Kim Jong Un moved back the KPA's official founding date back to its original date of 8 February 1948, with 25 April instead becoming the official foundation date of the KPRA
%) is also used as aquarium plants fertilizer. The more soluble form of iron, Fe(II), is a micronutrient needed by aquatic plants. By binding to Fe2+ ions DTPA prevents their precipitation as Fe(OH)3, or Fe2O3·nH2O poorly soluble oxy-hydroxides after their oxidation by dissolved oxygen. It increases the solubility of Fe2+ and Fe3+ ions in water, and therefore the bioavailability of iron for aquatic plants. It contributes so to maintain iron under a dissolved form (probably a mix of Fe(II) and Fe(III) DTPA complexes) in the water column. It is unclear to what extent does DTPA really contribute to protect dissolved Fe2+ against air oxidation and if the Fe(III)-DTPA complex cannot also be directly assimilated by aquatic plants simply because of its enhanced solubility. Under natural conditions, that is, in the absence of complexing DTPA, Fe2+ is more easily assimilated by most organisms, because of its 100-fold higher solubility than that of Fe3+. In pulp and paper mills DTPA is also used to remove dissolved ferrous and ferric ions (and other redox-active metal ions, such as Mn or Cu) that otherwise would accelerate the catalytic decomposition of hydrogen peroxide (H2O2 reduction by Fe2+ ions according to the Fenton reaction mechanism). This helps preserving the oxidation capacity of the hydrogen peroxide stock which is used as oxidizing agent to bleach pulp in the chlorine-free process of paper making. Several thousand tons of DTPA are produced annually for this purpose in order to limit the non-negligible losses of H2O2 by this mechanism.
Southern Rhodesia had long been distinctive among British dependencies in that it had financed and developed its own security forces and command structure. After UDI, this posed a particular dilemma for the British government, which considered and rejected various proposals aimed at ending Rhodesia's state of rebellion by force. Harold Wilson once remarked that bringing an end to Rhodesian independence "would not be a case of arresting a subversive individual. It would mean a bloody war, and probably a bloody war turning into a bloody civil war." The formidable nature of the Rhodesian security forces, as well as British fears of a direct South African intervention on behalf of the rogue colony, preempted the further consideration of military options. For much of its existence, Rhodesia maintained a small professional standing army of 3,400 troops, about a third of whom were black volunteers. In the tradition of many colonial armies, it was primarily organised into light infantry battalions trained and equipped for counter-insurgency warfare or internal security actions, and possessed little artillery or armour. The Royal Rhodesian Air Force (RRAF) had 1,000 personnel and six squadrons of aircraft, including forty to fifty Hawker Hunter and de Havilland Vampire strike aircraft and English Electric Canberra light bombers. It also possessed a helicopter squadron, a transport squadron, and a light reconnaissance squadron.
Below its Curie point of 770 °C (1,420 °F; 1,040 K), α-iron changes from paramagnetic to ferromagnetic: the spins of the two unpaired electrons in each atom generally align with the spins of its neighbors, creating an overall magnetic field. This happens because the orbitals of those two electrons (dz2 and dx2 − y2) do not point toward neighboring atoms in the lattice, and therefore are not involved in metallic bonding. In the absence of an external source of magnetic field, the atoms get spontaneously partitioned into magnetic domains, about 10 micrometers across, such that the atoms in each domain have parallel spins, but some domains have other orientations. Thus a macroscopic piece of iron will have a nearly zero overall magnetic field. Application of an external magnetic field causes the domains that are magnetized in the same general direction to grow at the expense of adjacent ones that point in other directions, reinforcing the external field. This effect is exploited in devices that need to channel magnetic fields to fulfill design function, such as electrical transformers, magnetic recording heads, and electric motors. Impurities, lattice defects, or grain and particle boundaries can "pin" the domains in the new positions, so that the effect persists even after the external field is removed – thus turning the iron object into a (permanent) magnet.
Sources: en.wikipedia.org
Sequence variation of Bemisia tabaci Chemosensory protein 2 in cryptic species B and Q: new DNA markers for whitefly recognition. Gene 2016a; 576: 284-291. 26. Zhu J, Wang G, Pelosi P. Plant transcriptomes reveal hidden guests. Biochem Biophys Res Commun. 2016; 474: 497-502. 27. Perkin LC, Friesen KS, Flinn PW, Oppert B. Venom gland components of the ectoparasitoid wasp, Anisopteromalus calandrae. J. Venom Res. 2015; 6: 19-37. 28. Celorio-Mancera MdP, Sundmalm SM, Vogel H, Rutishauser D, Ytterberg AJ, Zubarv RA et al. Chemosensory proteins, major salivary factors in caterpillar mandibular glands. Insect Biochem Mol Biol. 2012; 42: 796-805. 29. González-Caballero N, Valenzuela JG, Ribeiro JMC, Cuervo P, Brazil RP. Transcriptome exploration of the sex pheromone gland of Lutzomyia longipalpis (Diptera: Psychodidae: Phlebotominae). Parasit Vect. 2013; 6: 56. 30. Liu YL, Guo H, Huang LQ, Pelosi P, Wang CZ. Unique function of a chemosensory protein in the proboscis of two Helicoverpa species. J Exp Biol. 2014; 217: 1821-1826. 31. Zhu J, Iovinella I, Dani FR, Liu YL, Huang LQ, Liu Y, et al. Conserved chemosensory proteins in the proboscis and eyes of Lepidoptera. Int J Biol Sci. 2016; 12: 1394-1404. 32. Xuan N, Guo X, Xie HY, Lou QN, Bo LX, Liu GX, et al. Increased expression of CSP and CYP genes in adult silkworm females exposed to avermectins. Insect Sci. 2015; 22: 203-219. 33. Sabatier L, Jouanguy E, Dostert C, Zachary D, Dimarcq JL, Bulet P, et al.
standard conditions of temperature and pressure (STP) A standardisation of ambient temperature and pressure used in order to easily compare experimental results. Standard temperature is 25 degrees Celsius (°C) and standard pressure is 100.000 kilopascals (kPa). Standard conditions are often denoted with the abbreviation STP or SATP.
== Function == EosFP emits a strong green fluorescence (516 nm) that changes irreversibly to red (581 nm) when irradiated with UV-light of 390 nm. This modification occurs due to a break in the peptide backbone next to the chromophore. This mechanism allows for localized tagging of the protein and makes EosFP an appropriate tool for tracking protein movement within living cells. Formation of the red chromophore involves cleaving the peptide backbone but includes almost no other changes in the protein structure. According to single-molecule fluorescence spectroscopy, EosFP is tetrameric, and exhibits strong Forster resonance coupling within individual fluorophores. Like other fluorescent proteins, Eos can be used to report diverse signals in cells, tissues and organs without disturbing complex biological machinery. While the use of fluorescent proteins was once limited to the green fluorescent protein (GFP), in recent years many other fluorescent proteins have been cloned. Unlike GFPs, which are derived from the luminescent jellyfish Aequorea victoria, fluorescent proteins derived from anthozoa, including Eos, emit fluorescence in the red spectral range. The novel property of photoinduced green-to-red conversion in Eos is useful because it allows for localized tracking of proteins in living cells. EosFP is unique because it has a large separation in the wavelengths it can emit which allows for easy identification of peak colours. All green-to-red photoinducible fluorescent proteins, including Eos, contain a chromophoric unit derived from the tripeptide his-tyr-gly.
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.
Liquid chromatography with mass spectrometry is a common approach. Ultraviolet detection and nuclear magnetic resonance can support identification when suitable standards are available.