Stenabolic is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Updated 2026-03-22. Numbers and descriptions here follow the published literature rather than marketing material.
Pharmacokinetic data for SR9009 are limited in published literature. Some reports indicate low oral bioavailability and rapid clearance in animals, which complicates interpretation of exposure and effect. Researchers often use injected routes in preclinical work to achieve measurable systemic levels. Analytical studies rely on mass spectrometry to detect the parent compound and its metabolites. Questions about tissue distribution, active metabolites, and long-term consequences remain open. Species differences in metabolism can affect observed half-life and target engagement.
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 and metabolic gene expression. In laboratory experiments, SR9009 binds these receptors and alters transcription of genes involved in lipid handling, glucose metabolism, and mitochondrial function. It is not a naturally occurring compound and has no approved therapeutic use. Research interest stems from its ability to modify energy metabolism in cells and animal models.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Synthetic small-molecule REV-ERB agonist | Not a hormone or natural product |
| Primary targets | REV-ERBα and REV-ERBβ | Nuclear receptors involved in circadian and metabolic regulation |
| Appearance | White to off-white solid | Typical for purified research samples |
| Solubility | Soluble in DMSO and ethanol; low water solubility | Laboratory solubility depends on solvent and purity |
| Common synonyms | SR9009; Stenabolic | Stenabolic is a colloquial name, not a formal chemical name |
Scientific discussion of SR9009 often separates animal evidence from human anecdote. Rodent studies provide controlled data on endurance, metabolism, and gene expression, but they use specific strains, doses, and treatment durations. Human reports are mostly uncontrolled and cannot establish cause and effect. Open questions include oral bioavailability, tissue distribution, metabolic stability, and long-term effects. Review articles generally call for more rigorous pharmacokinetic and safety research before any clinical use could be considered.
Analytical methods for SR9009 typically rely on liquid chromatography coupled with tandem mass spectrometry. The technique can separate the parent compound from related substances and detect low concentrations in biological matrices. Urine and blood are common samples in anti-doping testing, while in vitro studies may use cell culture media. Rapid metabolism and low expected concentrations make method validation important for reliable identification. Exact metabolite patterns can vary by species and are not fully mapped.
Regulatory treatment of SR9009 reflects its investigational status. The compound has no approved human therapeutic indication, and sports authorities prohibit its use. It appears on anti-doping lists as a non-approved substance or metabolic modulator, depending on the list version. Products sold online as research chemicals are not quality-controlled medicines, so their identity and purity can differ from the label. Such products may also contain unlisted compounds, which complicates both testing and safety assessment.
Quality control for research materials includes identity confirmation by nuclear magnetic resonance and purity assessment by high-performance liquid chromatography. Mass spectrometry provides molecular weight confirmation and can detect related impurities. Purchasers should request a certificate of analysis that lists lot-specific data. Online products advertised for human use often lack such documentation. Distinguishing legitimate research material from mislabeled or contaminated samples is a recurring challenge in independent testing, and independent laboratories may use orthogonal methods to verify identity.
Detection of SR9009 in biological samples usually relies on liquid chromatography coupled to tandem mass spectrometry. This approach separates the compound from matrix components and identifies it by mass transitions. Because SR9009 can undergo metabolism, laboratories often look for both parent drug and specific metabolites. Sample preparation may involve protein precipitation or solid-phase extraction. Method validation examines sensitivity, carryover, and interference from related substances, and reference standards are required for accurate calibration.
Storage recommendations for SR9009 reference material typically specify a freezer at -20 °C or lower, with protection from moisture and light. Repeated freeze-thaw cycles can degrade small molecules and introduce variability. Stock solutions in dimethyl sulfoxide are often aliquoted to avoid repeated handling. Stability studies may examine degradation under heat, humidity, and light exposure. The compound's thiophene and nitro groups can participate in reactions that alter analytical signals over time, so such changes affect quantitative results.
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.
SR9009 is a synthetic small molecule that acts on the nuclear receptors REV-ERBα and REV-ERBβ. These receptors are part of the circadian clock machinery and normally repress transcription of certain target genes. In laboratory research, SR9009 is used as a chemical tool to study how REV-ERB activity influences metabolism, inflammation, and daily biological rhythms. The compound is not an approved medicine, and its effects in humans remain largely uncharacterized. It is often described as an investigational agent rather than a therapeutic product.
The history of BCG is tied to that of smallpox. By 1865 Jean Antoine Villemin had demonstrated that rabbits could be infected with tuberculosis from humans; by 1868 he had found that rabbits could be infected with tuberculosis from cows and that rabbits could be infected with tuberculosis from other rabbits. Thus, he concluded that tuberculosis was transmitted via some unidentified microorganism (or "virus", as he called it). In 1882 Robert Koch regarded human and bovine tuberculosis as identical. But in 1895, Theobald Smith presented differences between human and bovine tuberculosis, which he reported to Koch. By 1901 Koch distinguished Mycobacterium bovis from Mycobacterium tuberculosis. Following the success of vaccination in preventing smallpox, established during the 18th century, scientists thought to find a corollary in tuberculosis by drawing a parallel between bovine tuberculosis and cowpox: it was hypothesized that infection with bovine tuberculosis might protect against infection with human tuberculosis. In the late 19th century, clinical trials using M. bovis were conducted in Italy with disastrous results, because M. bovis was found to be just as virulent as M. tuberculosis. Albert Calmette, a French physician and bacteriologist, and his assistant and later colleague, Camille Guérin, a veterinarian, were working at the Institut Pasteur de Lille (Lille, France) in 1908. Their work included subculturing virulent strains of the tuberculosis bacillus and testing different culture media.
Rogue taxidermy (sometimes referred to as "taxidermy art" or "botched taxidermy") is a form of mixed media sculpture. Rogue taxidermy art references traditional trophy or natural history museum taxidermy, but is not always constructed out of taxidermied animals; it can be constructed entirely from synthetic materials. Additionally, rogue taxidermy is not necessarily figurative, as it can be abstract and does not need to resemble an animal. It can be a small decorative object or a large-scale room-sized installation. There is a very broad spectrum of styles within the genre, some of which falls into the category of mainstream art. "Rogue taxidermy" describes a wide variety of work, including work that is classified and exhibited as fine art. Neither the term, nor the genre, emerged from the world of traditional taxidermy. The genre was born from forms of fine art that utilize some of the components found in the construction of a traditional taxidermy mount. The term "rogue taxidermy" was coined in 2004 by an artist collective called The Minnesota Association of Rogue Taxidermists. The Minneapolis-based group was founded by artists Sarina Brewer, Scott Bibus, and Robert Marbury as a means to unite their respective mediums and differing styles of sculpture. The definition of rogue taxidermy set forth by the individuals who formed the genre (Brewer, Bibus, and Marbury) is: "A genre of pop-surrealist art characterized by mixed media sculptures containing conventional taxidermy-related materials that are used in an unconventional manner".
== Metabolism == Thiopental rapidly and easily crosses the blood–brain barrier as it is a lipophilic molecule. As with all lipid-soluble anaesthetic drugs, the short duration of action of sodium thiopental is due almost entirely to its redistribution away from central circulation into muscle and fatty tissue, due to its very high lipid–water partition coefficient (approximately 10), leading to sequestration in fatty tissue. Once redistributed, the free fraction in the blood is metabolized in the liver by zero-order kinetics. Sodium thiopental is mainly metabolized to pentobarbital, 5-ethyl-5-(1'-methyl-3'-hydroxybutyl)-2-thiobarbituric acid, and 5-ethyl-5-(1'-methyl-3'-carboxypropyl)-2-thiobarbituric acid.
=== Celebrations and festivals === Lefse is celebrated in cities and towns with large Scandinavian populations. Fargo, North Dakota, hosts the popular Lutefisk and Lefse Festival in August each year. Fosston, Minnesota, invites area lefse makers to compete for the title of Champion Lefse Maker at its Lefse Fest in November. In Mankato, Minnesota, Minnesotans of Scandinavian descent celebrate lefse day, a day for cooking lefse, on the Sunday after Thanksgiving. The Potato Days festival has been taking place in Barnesville, Minnesota, since the early 1930s; this festival also takes part in the National Lefse Cookoff.
Surf City Squeeze was started in the early 1980s by Kevin Blackwell and his wife Kathi, and later became a franchise. Later, in 1998/1999, Sports Group International, Inc. (a company that was originally formed to distributed Spalding-branded sports drinks) merged with Surf City Squeeze with Surf City Squeeze's management taking over full control of the company. Also in 1999, Sports Group International purchased Frullati Cafe & Bakery Chain, bringing the total number of its franchised locations to 200. In 2001, Kevin Blackwell changed the name of his company from Sports Group International to Kahala Corp. after terminating an agreement with Spalding. Also in 2000, Kahala Corp. then developed the Rollerz brand. From 2002 to 2006, Kahala Corp. purchased Ranch One Grilled Chicken, Samurai Sam's Teriyaki Grill, Taco Time, Great Steak, Johnnie's New York Pizzeria, and Blimpie. Kahala also acquired the license to Wafflo. In 2007, Kahala Corp and Cold Stone Creamery agreed to merge creating a combined company holding 13 diversified brands. The combined company generated more than $1.1 billion in system wide sales in partnership with 3,000-plus franchisees and more than 4,600 retail locations. As a result of the merger, Kahala's CEO Kevin Blackwell and Cold Stone Creamery's CEO and chairman Doug Ducey were respectively appointed chairman and CEO of the new combined company, Kahala-Cold Stone. Ducey left a few months later to join tech start-up iMemories after being forced out by Blackwell. In July 2007, Kahala-Cold Stone acquired Cereality Cereal Bar & Cafe.
Sources: en.wikipedia.org
=== Human Chorionic Gonadotropin === Like relaxin, hCG may be measured, although the effects on the neonate are not well understood. It is posited that it may act as an LH paralogue to affect the development of neonatal gonads, although further research is required.
On 1 January 1971, commercial production of the first portable digital tablet counters in the world began. John Kirby had filed U.K. Patent number GB1358378(A) on 8 September 1970 and U.S. patent number 3789194 on 9 August 1971. These early electronic counters were designed to help pharmacies replace the common (but often inaccurate) practice of counting medications by hand.
Elongation depends on elongation factors. At the end of the initiation step, the mRNA is positioned so that the next codon can be translated during the elongation stage of protein synthesis. The initiator TRNA occupies the P site in the ribosome, and the A site is ready to receive an aminoacyl-TRNA. During chain elongation, each additional amino acid is added to the nascent polypeptide chain in a three-step micro cycle. The steps in this micro cycle are (1) positioning the correct aminoacyl-TRNA in the A site of the ribosome, which is brought into that site by eEF1, (2) forming the peptide bond, and (3) shifting the mRNA by one codon relative to the ribosome with the help of eEF2. Unlike bacteria, in which translation initiation occurs as soon as the 5' end of an mRNA is synthesized, in eukaryotes, such tight coupling between transcription and translation is not possible because transcription and translation are carried out in separate compartments of the cell (the nucleus and cytoplasm). Eukaryotic mRNA precursors must be processed in the nucleus (e.g., capping, polyadenylation, splicing) in ribosomes before they are exported to the cytoplasm for translation. Translation can also be affected by ribosomal pausing, which can trigger endo nucleolytic attack of the TRNA, a process termed mRNA no-go decay. Ribosomal pausing also aids co-translational folding of the nascent polypeptide on the ribosome, and delays protein translation while it is encoding TRNA. This can trigger ribosomal frameshifting.
=== Pharmacodynamics === Research has shown that salvinorin A is a potent κ-opioid receptor (KOR) agonist (Ki = 2.4 nM, EC50 = 1.8 nM). It has a high affinity for the receptor, indicated by the low dissociation constant of 1.0 nanomolar (nM). It shows atypical properties as an agonist of the KOR relative to other KOR agonists. In addition to its KOR agonism, salvinorin A has been found to act as a dopamine D2 receptor partial agonist, with an affinity of 5–10 nM, an intrinsic activity of 40–60%, and an EC50 of 48 nM. As such, the dopamine D2 receptor might also play a role in its effects. Salvinorin A has no action at the 5-HT2A serotonin receptor, the principal molecular target responsible for the actions of 'classical' psychedelics such as LSD and mescaline. Salvinorin A has also been shown to have effect on cannabinoid CB1 receptors. It significantly increases prolactin and inconsistently increases cortisol. It causes dysphoria by stopping release of dopamine in the striatum. Salvinorin A increases activity of DAT while decreasing activity of SERT. Salvinorin A is capable of inhibiting excess intestinal motility (e.g. diarrhea), through its potent κ-opioid-activating effects. The mechanism of action for salvinorin A on ileal tissue has been described as 'prejunctional', as it was able to modify electrically induced contractions, but not those of exogenous acetylcholine.
=== ES-SCLC === In ES-SCLC, platinum-based combination chemotherapy is the standard of care. Combination chemotherapy consists of a wide variety of agents, including cisplatin, cyclophosphamide, vincristine and carboplatin. Response rates are high even in extensive disease, with between 15% and 30% of subjects having a complete response to a combination chemotherapy, and the vast majority having at least some objective response. Responses in ES-SCLC are often of short duration, and the evidence surrounding the risk of treatment compared to the potential benefit of chemotherapy for people who have extensive SCLC is not clear.
Sources: en.wikipedia.org
=== Vitrification === Vitrification is a flash-freezing (ultra-rapid cooling) process that helps to prevent the formation of ice crystals and helps prevent cryopreservation damage. Researchers Greg Fahy and William F. Rall helped to introduce vitrification to reproductive cryopreservation in the mid-1980s. As of 2000, researchers claim vitrification provides the benefits of cryopreservation without damage due to ice crystal formation. The situation became more complex with the development of tissue engineering as both cells and biomaterials need to remain ice-free to preserve high cell viability and functions, integrity of constructs and structure of biomaterials. Vitrification of tissue engineered constructs was first reported by Lilia Kuleshova, who also was the first scientist to achieve vitrification of oocytes, which resulted in live birth in 1999. For clinical cryopreservation, vitrification usually requires the addition of cryoprotectants before cooling. Cryoprotectants are macromolecules added to the freezing medium to protect cells from the detrimental effects of intracellular ice crystal formation or from the solution effects, during the process of freezing and thawing. They permit a higher degree of cell survival during freezing, to lower the freezing point, to protect cell membrane from freeze-related injury. Cryoprotectants have high solubility, low toxicity at high concentrations, low molecular weight and the ability to interact with water via hydrogen bonding. Instead of crystallizing, the syrupy solution becomes an amorphous ice—it vitrifies.
=== EC 2.1.1: Methyltransferases === EC 2.1.1.1: nicotinamide N-methyltransferase EC 2.1.1.2: guanidinoacetate N-methyltransferase EC 2.1.1.3: thetin—homocysteine S-methyltransferase EC 2.1.1.4: acetylserotonin O-methyltransferase EC 2.1.1.5: betaine—homocysteine S-methyltransferase EC 2.1.1.6: catechol O-methyltransferase EC 2.1.1.7: nicotinate N-methyltransferase EC 2.1.1.8: histamine N-methyltransferase EC 2.1.1.9: thiol S-methyltransferase EC 2.1.1.10: homocysteine S-methyltransferase EC 2.1.1.11: magnesium protoporphyrin IX methyltransferase EC 2.1.1.12: methionine S-methyltransferase EC 2.1.1.13: methionine synthase EC 2.1.1.14: 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase EC 2.1.1.15: fatty-acid O-methyltransferase EC 2.1.1.16: methylene-fatty-acyl-phospholipid synthase EC 2.1.1.17: phosphatidylethanolamine N-methyltransferase EC 2.1.1.18: polysaccharide O-methyltransferase EC 2.1.1.19: trimethylsulfonium—tetrahydrofolate N-methyltransferase EC 2.1.1.20: glycine N-methyltransferase EC 2.1.1.21: methylamine—glutamate N-methyltransferase EC 2.1.1.22: carnosine N-methyltransferase EC 2.1.1.23: now covered by EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126 EC 2.1.1.24: now covered by EC 2.1.1.77, EC 2.1.1.80 and EC 2.1.1.100 EC 2.1.1.25: phenol O-methyltransferase EC 2.1.1.26: iodophenol O-methyltransferase EC 2.1.1.27: tyramine N-methyltransferase EC 2.1.1.28: phenylethanolamine N-methyltransferase EC 2.1.1.29: Now covered by EC 2.1.1.202, EC 2.1.1.203 and EC .1.1.204 EC 2.1.1.30: tRNA (purine-2- or -6-)-methyltransferase: Reactions previously described are due to EC 2.1.1.32 EC 2.1.1.31: Now covered by EC 2.1.1.221 and EC 2.1.1.228 EC 2.1.1.32: Now covered by EC 2.1.1.213, EC 2.1.1.214, EC 2.1.1.215 and EC 2.1.1.216 EC 2.1.1.33: tRNA (guanine46-N7)-methyltransferase EC 2.1.1.34: tRNA (guanosine18-2′-O)-methyltransferase EC 2.1.1.35: tRNA (uracil54-C5)-methyltransferase EC 2.1.1.36: Now covered by EC 2.1.1.217, EC 2.1.1.218, EC 2.1.1.219, EC 2.1.1.220 EC 2.1.1.37: DNA (cytosine-5-)-methyltransferase EC 2.1.1.38: O-demethylpuromycin O-methyltransferase EC 2.1.1.39: inositol 3-methyltransferase EC 2.1.1.40: inositol 1-methyltransferase EC 2.1.1.41: sterol 24-C-methyltransferase EC 2.1.1.42: flavone 3′-O-methyltransferase EC 2.1.1.43: Now described by EC 2.1.1.354, EC 2.1.1.355, EC 2.1.1.356, EC 2.1.1.357, EC 2.1.1.358, EC 2.1.1.359, EC 2.1.1.360, EC 2.1.1.361 and EC 2.1.1.362 EC 2.1.1.44: L-histidine Nα-methyltransferase EC 2.1.1.45: thymidylate synthase EC 2.1.1.46: isoflavone 4′-O-methyltransferase EC 2.1.1.47: indolepyruvate C-methyltransferase EC 2.1.1.48: Now covered by EC 2.1.1.181, EC 2.1.1.182, EC 2.1.1.183 and EC 2.1.1.184 EC 2.1.1.49: amine N-methyltransferase EC 2.1.1.50: loganate O-methyltransferase EC 2.1.1.51: Now covered by EC 2.1.1.187 and EC 2.1.1.188 EC 2.1.1.52: Now covered by EC 2.1.1.171, EC 2.1.1.172, EC 2.1.1.173 and EC 2.1.1.174 EC 2.1.1.53: putrescine N-methyltransferase EC 2.1.1.54: deoxycytidylate C-methyltransferase EC 2.1.1.55: tRNA (adenine-N6-)-methyltransferase EC 2.1.1.56: mRNA (guanine-N7)-methyltransferase EC 2.1.1.57: methyltransferase cap1 EC 2.1.1.58: deleted, included in EC 2.1.1.57 EC 2.1.1.59: [cytochrome c]-lysine N-methyltransferase EC 2.1.1.60: calmodulin-lysine N-methyltransferase EC 2.1.1.61: tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase EC 2.1.1.62: mRNA (2′-O-methyladenosine-N6-)-methyltransferase EC 2.1.1.63: methylated-DNA—[protein]-cysteine S-methyltransferase EC 2.1.1.64: 3-demethylubiquinol 3-O-methyltransferase EC 2.1.1.65: licodione 2′-O-methyltransferase EC 2.1.1.66: Now covered by EC 2.1.1.230 EC 2.1.1.67: thiopurine S-methyltransferase EC 2.1.1.68: caffeate O-methyltransferase EC 2.1.1.69: 5-hydroxyfuranocoumarin 5-O-methyltransferase EC 2.1.1.70: 8-hydroxyfuranocoumarin 8-O-methyltransferase EC 2.1.1.71: phosphatidyl-N-methylethanolamine N-methyltransferase EC 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific) EC 2.1.1.73: deleted: reaction is that of EC 2.1.1.37, DNA (cytosine-5-)-methyltransferase EC 2.1.1.74: methylenetetrahydrofolate—tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing] EC 2.1.1.75: apigenin 4′-O-methyltransferase EC 2.1.1.76: quercetin 3-O-methyltransferase EC 2.1.1.77: protein-L-isoaspartate(D-aspartate) O-methyltransferase EC 2.1.1.78: isoorientin 3′-O-methyltransferase EC 2.1.1.79: cyclopropane-fatty-acyl-phospholipid synthase EC 2.1.1.80: protein-glutamate O-methyltransferase EC 2.1.1.81: deleted, included in EC 2.1.1.49 EC 2.1.1.82: 3-methylquercetin 7-O-methyltransferase EC 2.1.1.83: 3,7-dimethylquercetin 4′-O-methyltransferase EC 2.1.1.84: methylquercetagetin 6-O-methyltransferase EC 2.1.1.85: protein-histidine N-methyltransferase EC 2.1.1.86: Now covered by EC 7.2.1.4 EC 2.1.1.87: pyridine N-methyltransferase EC 2.1.1.88: 8-hydroxyquercetin 8-O-methyltransferase EC 2.1.1.89: tetrahydrocolumbamine 2-O-methyltransferase EC 2.1.1.90: methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase EC 2.1.1.91: isobutyraldoxime O-methyltransferase EC 2.1.1.92: Now included with EC 2.1.1.69 EC 2.1.1.93: is identical to EC 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase EC 2.1.1.94: tabersonine 16-O-methyltransferase EC 2.1.1.95: tocopherol C-methyltransferase EC 2.1.1.96: thioether S-methyltransferase EC 2.1.1.97: 3-hydroxyanthranilate 4-C-methyltransferase EC 2.1.1.98: diphthine synthase EC 2.1.1.99: 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase EC 2.1.1.100: protein-S-isoprenylcysteine O-methyltransferase EC 2.1.1.101: macrocin O-methyltransferase EC 2.1.1.102: demethylmacrocin O-methyltransferase EC 2.1.1.103: phosphoethanolamine N-methyltransferase EC 2.1.1.104: caffeoyl-CoA O-methyltransferase EC 2.1.1.105: N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase EC 2.1.1.106: tryptophan 2-C-methyltransferase EC 2.1.1.107: uroporphyrinogen-III C-methyltransferase EC 2.1.1.108: 6-hydroxymellein O-methyltransferase EC 2.1.1.109: demethylsterigmatocystin 6-O-methyltransferase EC 2.1.1.110: sterigmatocystin 8-O-methyltransferase EC 2.1.1.111: anthranilate N-methyltransferase EC 2.1.1.112: glucuronoxylan 4-O-methyltransferase EC 2.1.1.113: site-specific DNA-methyltransferase (cytosine-N4-specific) EC 2.1.1.114: polyprenyldihydroxybenzoate methyltransferase EC 2.1.1.115: (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase EC 2.1.1.116: 3′-hydroxy-N-methyl-(S)-coclaurine 4′-O-methyltransferase EC 2.1.1.117: (S)-scoulerine 9-O-methyltransferase EC 2.1.1.118: columbamine O-methyltransferase EC 2.1.1.119: 10-hydroxydihydrosanguinarine 10-O-methyltransferase EC 2.1.1.120: 12-hydroxydihydrochelirubine 12-O-methyltransferase EC 2.1.1.121: 6-O-methylnorlaudanosoline 5′-O-methyltransferase EC 2.1.1.122: (S)-tetrahydroprotoberberine N-methyltransferase EC 2.1.1.123: [cytochrome-c]-methionine S-methyltransferase EC 2.1.1.124: Now covered by EC 2.1.1.319, EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322 EC 2.1.1.125: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 EC 2.1.1.126: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 EC 2.1.1.127: [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase EC 2.1.1.128: (RS)-norcoclaurine 6-O-methyltransferase EC 2.1.1.129: inositol 4-methyltransferase EC 2.1.1.130: precorrin-2 C20-methyltransferase EC 2.1.1.131: precorrin-2 C17-methyltransferase EC 2.1.1.132: precorrin-6B C5,15-methyltransferase (decarboxylating) EC 2.1.1.133: precorrin-4 C11-methyltransferase EC 2.1.1.134: now with EC 2.1.1.129 EC 2.1.1.135: now EC 1.16.1.8 EC 2.1.1.136: chlorophenol O-methyltransferase EC 2.1.1.137: arsenite methyltransferase EC 2.1.1.138: deleted: Reaction due to EC 2.1.1.137 EC 2.1.1.139: 3′-demethylstaurosporine O-methyltransferase EC 2.1.1.140: (S)-coclaurine-N-methyltransferase EC 2.1.1.141: jasmonate O-methyltransferase EC 2.1.1.142: cycloartenol 24-C-methyltransferase EC 2.1.1.143: 24-methylenesterol C-methyltransferase EC 2.1.1.144: trans-aconitate 2-methyltransferase EC 2.1.1.145: trans-aconitate 3-methyltransferase EC 2.1.1.146: (iso)eugenol O-methyltransferase EC 2.1.1.147: corydaline synthase EC 2.1.1.148: thymidylate synthase (FAD) EC 2.1.1.149: Now covered by EC 2.1.1.267, flavonoid 3′,5′-methyltransferase EC 2.1.1.150: isoflavone 7-O-methyltransferase EC 2.1.1.151: cobalt-factor II C20-methyltransferase EC 2.1.1.152: precorrin-6A synthase (deacetylating) EC 2.1.1.153: vitexin 2′′-O-rhamnoside 7-O-methyltransferase EC 2.1.1.154: isoliquiritigenin 2′-O-methyltransferase EC 2.1.1.155: kaempferol 4′-O-methyltransferase EC 2.1.1.156: glycine/sarcosine N-methyltransferase EC 2.1.1.157: sarcosine/dimethylglycine N-methyltransferase EC 2.1.1.158: 7-methylxanthosine synthase EC 2.1.1.159: theobromine synthase EC 2.1.1.160: caffeine synthase EC 2.1.1.161: dimethylglycine N-methyltransferase EC 2.1.1.162: glycine/sarcosine/dimethylglycine N-methyltransferase EC 2.1.1.163: demethylmenaquinone methyltransferase EC 2.1.1.164: demethylrebeccamycin-D-glucose O-methyltransferase EC 2.1.1.165: methyl halide transferase EC 2.1.1.166: 23S rRNA (uridine2552-2′-O)-methyltransferase EC 2.1.1.167: 27S pre-rRNA (guanosine2922-2′-O)-methyltransferase EC 2.1.1.168: 21S rRNA (uridine2791-2′-O)-methyltransferase EC 2.1.1.169: tricetin 3′,4′,5′-O-trimethyltransferase EC 2.1.1.170: 16S rRNA (guanine527-N7)-methyltransferase EC 2.1.1.171: 16S rRNA (guanine966-N2)-methyltransferase EC 2.1.1.172: 16S rRNA (guanine1207-N2))-methyltransferase EC 2.1.1.173: 23S rRNA (guanine2445-N2)-methyltransferase EC 2.1.1.174: 23S rRNA (guanine1835-N2)-methyltransferase EC 2.1.1.175: tricin synthase EC 2.1.1.176: 16S rRNA (cytosine967-C5)-methyltransferase EC 2.1.1.177: 23S rRNA (pseudouridine1915-N3)-methyltransferase EC 2.1.1.178: 16S rRNA (cytosine1407-C5)-methyltransferase EC 2.1.1.179: 16S rRNA (guanine1405-N7)-methyltransferase EC 2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase EC 2.1.1.181: 23S rRNA (adenine1618-N6)-methyltransferase EC 2.1.1.182: 16S rRNA (adenine1518-N6/adenineadenine1519-N6)-dimethyltransferase EC 2.1.1.183: 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase EC 2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase EC 2.1.1.185: 23S rRNA (guanosine2251-2′-O)-methyltransferase EC 2.1.1.186: 23S rRNA (cytidine2498-2′-O)-methyltransferase EC 2.1.1.187: 23S rRNA (guanine745-N1)-methyltransferase EC 2.1.1.188: 23S rRNA (guanine748-N1)-methyltransferase EC 2.1.1.189: 23S rRNA (uracil747-C5)-methyltransferase EC 2.1.1.190: 23S rRNA (uracil1939-C5)-methyltransferase EC 2.1.1.191: 23S rRNA (cytosine1962-C5)-methyltransferase EC 2.1.1.192: 23S rRNA (adenine2503-C2)-methyltransferase EC 2.1.1.193: 16S rRNA (uracil1498-N3)-methyltransferase EC 2.1.1.194: A mixture of EC 2.1.1.192 and EC 2.1.1.224 EC 2.1.1.195: cobalt-precorrin-5B (C1)-methyltransferase EC 2.1.1.196: cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) EC 2.1.1.197: malonyl-[acyl-carrier protein] O-methyltransferase EC 2.1.1.198: 16S rRNA (cytidine1402-2′-O)-methyltransferase EC 2.1.1.199: 16S rRNA (cytosine1402-N4)-methyltransferase EC 2.1.1.200: tRNA (cytidine32/uridine32-2′-O)-methyltransferase EC 2.1.1.201: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase EC 2.1.1.202: multisite-specific tRNA:(cytosine-C5)-methyltransferase EC 2.1.1.203: tRNA (cytosine34-C5)-methyltransferase EC 2.1.1.204: tRNA (cytosine38-C5)-methyltransferase EC 2.1.1.205: tRNA (cytidine32/guanosine34-2′-O)-methyltransferase EC 2.1.1.206: tRNA (cytidine56-2′-O)-methyltransferase EC 2.1.1.207: tRNA (cytidine34-2′-O)-methyltransferase EC 2.1.1.208: 23S rRNA (uridine2479-2′-O)-methyltransferase EC 2.1.1.209: 23S rRNA (guanine2535-N1)-methyltransferase EC 2.1.1.210: demethylspheroidene O-methyltransferase EC 2.1.1.211: tRNASer(uridine44-2′-O)-methyltransferase EC 2.1.1.212: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase EC 2.1.1.213: tRNA (guanine110-N2)-dimethyltransferase EC 2.1.1.214: tRNA (guanine10-N2)-methyltransferase EC 2.1.1.215: tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase EC 2.1.1.216: tRNA (guanine26-N2)-dimethyltransferase EC 2.1.1.217: tRNA (adenine22-N1)-methyltransferase EC 2.1.1.218: tRNA (adenine9-N1)-methyltransferase EC 2.1.1.219: tRNA (adenine57-N1/adenine58-N1)-methyltransferase EC 2.1.1.220: tRNA (adenine58-N1)-methyltransferase EC 2.1.1.221: tRNA (guanine9-N1)-methyltransferase EC 2.1.1.222: 2-polyprenyl-6-hydroxyphenyl methylase EC 2.1.1.223: tRNA1Val (adenine937-N6)-methyltransferase EC 2.1.1.224: 23S rRNA (adenine2503-C8)-methyltransferase EC 2.1.1.225: tRNA:m4X modification enzyme EC 2.1.1.226: 23S rRNA (cytidine1920-2′-O)-methyltransferase EC 2.1.1.227: 16S rRNA (cytidine1409-2′-O)-methyltransferase EC 2.1.1.228: tRNA (guanine37-N1)-methyltransferase EC 2.1.1.229: tRNA (carboxymethyluridine34-5-O)-methyltransferase EC 2.1.1.230: 23S rRNA (adenosine1067-2′-O)-methyltransferase EC 2.1.1.231: flavonoid 4′-O-methyltransferase EC 2.1.1.232: naringenin 7-O-methyltransferase EC 2.1.1.233: [phosphatase 2A protein]-leucine-carboxy methyltransferase EC 2.1.1.234: dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase EC 2.1.1.235: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase EC 2.1.1.236: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose N,N-dimethyltransferase EC 2.1.1.237: mycinamicin III 3′′-O-methyltransferase EC 2.1.1.238: mycinamicin VI 2′′-O-methyltransferaseD EC 2.1.1.239: L-olivosyl-oleandolide 3-O-methyltransferase EC 2.1.1.240: trans-resveratrol di-O-methyltransferase EC 2.1.1.241: 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase EC 2.1.1.242: 16S rRNA (guanine1516-N2)-methyltransferase EC 2.1.1.243: 2-ketoarginine methyltransferase EC 2.1.1.244: protein N-terminal methyltransferase EC 2.1.1.245: 5-methyltetrahydrosarcinapterin—corrinoid/iron-sulfur protein Co-methyltransferase EC 2.1.1.246: [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.247: (methyl-Co(III) methylamine-specific corrinoid protein)—coenzyme M methyltransferase EC 2.1.1.248: methylamine—corrinoid protein Co-methyltransferase EC 2.1.1.249: dimethylamine—corrinoid protein Co-methyltransferase EC 2.1.1.250: trimethylamine—corrinoid protein Co-methyltransferase EC 2.1.1.251: methylated-thiol—coenzyme M methyltransferase EC 2.1.1.252: tetramethylammonium—corrinoid protein Co-methyltransferase EC 2.1.1.253: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.254: erythromycin 3′′-O-methyltransferase EC 2.1.1.255: geranyl diphosphate 2-C-methyltransferase EC 2.1.1.256: tRNA (guanine6-N6-methyltransferase) EC 2.1.1.257: tRNA (pseudouridine54-N1)-methyltransferase EC 2.1.1.258: 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase EC 2.1.1.259: [fructose-bisphosphate aldolase]-lysine N-methyltransferase EC 2.1.1.260: rRNA small subunit pseudouridine methyltransferase Nep1 EC 2.1.1.261: 4-dimethylallyltryptophan N-methyltransferase EC 2.1.1.262: squalene methyltransferase EC 2.1.1.263: botryococcene C-methyltransferase EC 2.1.1.264: 23S rRNA (guanine2069-N7)-methyltransferase EC 2.1.1.265: tellurite methyltransferase EC 2.1.1.266: 23S rRNA (adenine2030-N6)-methyltransferase EC 2.1.1.267: flavonoid 3′,5′-methyltransferase EC 2.1.1.268: tRNAThr (cytosine32-N3)-methyltransferase EC 2.1.1.269: dimethylsulfoniopropionate demethylase EC 2.1.1.270: (+)-6a-hydroxymaackiain 3-O-methyltransferase EC 2.1.1.271: cobalt-precorrin-4 methyltransferase EC 2.1.1.272: cobalt-factor III methyltransferase EC 2.1.1.273: benzoate O-methyltransferase EC 2.1.1.274: salicylate 1-O-methyltransferase EC 2.1.1.275: gibberellin A9 O-methyltransferase EC 2.1.1.276: gibberellin A4 carboxyl methyltransferase EC 2.1.1.277: anthranilate O-methyltransferase EC 2.1.1.278: indole-3-acetate O-methyltransferase EC 2.1.1.279: trans-anol O-methyltransferase EC 2.1.1.280: selenocysteine Se-methyltransferase EC 2.1.1.281: phenylpyruvate C3-methyltransferase EC 2.1.1.282: tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase EC 2.1.1.283: emodin O-methyltransferase EC 2.1.1.284: 8-demethylnovobiocic acid C8-methyltransferase EC 2.1.1.285: demethyldecarbamoylnovobiocin O-methyltransferase EC 2.1.1.286: 25S rRNA (adenine2142-N1)-methyltransferase EC 2.1.1.287: 25S rRNA (adenine645-N1)-methyltransferase EC 2.1.1.288: aklanonic acid methyltransferase EC 2.1.1.289: cobalt-precorrin-7 (C5)-methyltransferase EC 2.1.1.290: tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase EC 2.1.1.291: (R,S)-reticuline 7-O-methyltransferase EC 2.1.1.292: carminomycin 4-O-methyltransferase EC 2.1.1.293: 6-hydroxytryprostatin B O-methyltransferase EC 2.1.1.294: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase EC 2.1.1.295: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase EC 2.1.1.296: methyltransferase cap2 EC 2.1.1.297: peptide chain release factor N5-glutamine methyltransferase EC 2.1.1.298: ribosomal protein L3 N5-glutamine methyltransferase EC 2.1.1.299: protein N-terminal monomethyltransferase EC 2.1.1.300: pavine N-methyltransferase EC 2.1.1.301: cypemycin N-terminal methyltransferase EC 2.1.1.302: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase EC 2.1.1.303: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase EC 2.1.1.304: L-tyrosine C3-methyltransferase EC 2.1.1.305: 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2′-O-methyltransferase EC 2.1.1.306: 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3′-O-methyltransferase EC 2.1.1.307: 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4′-O-methyltransferase EC 2.1.1.308: cytidylyl-2-hydroxyethylphosphonate methyltransferase EC 2.1.1.309: 18S rRNA (guanine1575-N7)-methyltransferase EC 2.1.1.310: 25S rRNA (cytosine2870-C5)-methyltransferase EC 2.1.1.311: 25S rRNA (cytosine2278-C5)-methyltransferase EC 2.1.1.312: 25S rRNA (uracil2843-N3)-methyltransferase EC 2.1.1.313: 25S rRNA (uracil2634-N3)-methyltransferase EC 2.1.1.314: diphthine methyl ester synthase EC 2.1.1.315: 27-O-demethylrifamycin SV methyltransferase EC 2.1.1.316: mitomycin 6-O-methyltransferase EC 2.1.1.317: sphingolipid C9-methyltransferase EC 2.1.1.318: [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase EC 2.1.1.319: type I protein arginine methyltransferase EC 2.1.1.320: type II protein arginine methyltransferase EC 2.1.1.321: type III protein arginine methyltransferase EC 2.1.1.322: type IV protein arginine methyltransferase EC 2.1.1.323: (–)-pluviatolide 4-O-methyltransferase EC 2.1.1.324: dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase EC 2.1.1.325: juvenile hormone-III synthase EC 2.1.1.326: N-acetyldemethylphosphinothricin P-methyltransferase EC 2.1.1.327: phenazine-1-carboxylate N-methyltransferase EC 2.1.1.328: N-demethylindolmycin N-methyltransferase EC 2.1.1.329: demethylphylloquinol methyltransferase EC 2.1.1.330: 5′-demethylyatein 5′-O-methyltransferase EC 2.1.1.331: bacteriochlorophyllide d C-121-methyltransferase EC 2.1.1.332: bacteriochlorophyllide d C-82-methyltransferase EC 2.1.1.333: bacteriochlorophyllide d C-20 methyltransferase EC 2.1.1.334: methanethiol S-methyltransferase EC 2.1.1.335: 4-amino-anhydrotetracycline N4-methyltransferase EC 2.1.1.336: norbelladine O-methyltransferase EC 2.1.1.337: reticuline N-methyltransferase EC 2.1.1.338: desmethylxanthohumol 6′-O-methyltransferase EC 2.1.1.339: xanthohumol 4-O-methyltransferase EC 2.1.1.340: 3-aminomethylindole N'-methyltransferase EC 2.1.1.341: vanillate/3-O-methylgallate O-demethylase EC 2.1.1.342: anaerobilin synthase EC 2.1.1.343: 8-amino-8-demethylriboflavin N,N-dimethyltransferase EC 2.1.1.344: ornithine lipid N-methyltransferase EC 2.1.1.345: psilocybin synthase EC 2.1.1.346: U6 snRNA m6A methyltransferase EC 2.1.1.347: (+)-O-methylkolavelool synthase EC 2.1.1.348: mRNA m6A methyltransferase EC 2.1.1.349: toxoflavin synthase EC 2.1.1.350: menaquinone C8-methyltransferase EC 2.1.1.351: nocamycin O-methyltransferase EC 2.1.1.352: 3-O-acetyl-4′-O-demethylpapaveroxine 4′-O-methyltransferase EC 2.1.1.353: demethylluteothin O-methyltransferase EC 2.1.1.354: [histone H3]-lysine4 N-trimethyltransferase EC 2.1.1.355: [histone H3]-lysine9 N-trimethyltransferase EC 2.1.1.356: [histone H3]-lysine27 N-trimethyltransferase EC 2.1.1.357: [histone H3]-lysine36 N-dimethyltransferase EC 2.1.1.358: [histone H3]-dimethyl-L-lysine36 N-methyltransferase. Now known to have the activity of EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase. EC 2.1.1.359: [histone H3]-lysine36 N-trimethyltransferase EC 2.1.1.360: [histone H3]-lysine79 N-trimethyltransferase EC 2.1.1.361: [histone H4]-lysine20 N-methyltransferase EC 2.1.1.362: [histone H4]-N-methyl-L-lysine20 N-methyltransferase EC 2.1.1.363: pre-sodorifen synthase EC 2.1.1.364: [histone H3]-lysine4 N-methyltransferase EC 2.1.1.365: MMP 1-O-methyltransferase EC 2.1.1.366: [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase EC 2.1.1.367: [histone H3]-lysine9 N-methyltransferase EC 2.1.1.368: [histone H3]-lysine9 N-dimethyltransferase EC 2.1.1.369: [histone H3]-lysine27 N-methyltransferase EC 2.1.1.370: [histone H3]-lysine4 N-dimethyltransferase EC 2.1.1.371: [histone H3]-lysine27 N-dimethyltransferase EC 2.1.1.372: [histone H4]-lysine20 N-trimethyltransferase EC 2.1.1.373: 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase EC 2.1.1.374: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase EC 2.1.1.375: NNS virus cap methyltransferase EC 2.1.1.376: glycine betaine—corrinoid protein Co-methyltransferase EC 2.1.1.377: [methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.378: [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase EC 2.1.1.379: [methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
Strategic Air Command (1946–1992) SACAT – (a) Semi Attended Customer Activated Terminal (Supermarket checkout) SACEUR – (p) Supreme Allied Commander EURope SACF - Semi Automatic Capsule Filler source SACLANT – (p) Supreme Allied Commander atLANTic SACLOS – (a) Semi-Automatic Command to Line of Sight SAD (s) Safford Regional Airport (IATA code) (a) Seasonal Affective Disorder Situational Awareness Display SADD – (a) originally Students Against Drunk Driving, now Students Against Destructive Decisions (U.S.
== Use and toxicity == The European species did not enter into the herbalists' pharmacopeia. In the American Old West, the Western white clematis, Clematis ligusticifolia, was called pepper vine by early travelers and pioneers, who took a tip from Spanish colonials and used seeds and the acrid leaves of yerba de chivato as a pepper substitute. The entire genus contains essential oils and compounds which are extremely irritating to the skin and mucous membranes. Unlike black pepper or Capsicum, however, the compounds in clematis cause internal bleeding of the digestive tract if ingested in large amounts. C. ligusticifolia is essentially toxic. When pruning them, it is a good idea to wear gloves. Despite its toxicity, Native Americans used very small amounts of clematis as an effective treatment for migraine headaches and nervous disorders. It was also used as an effective treatment of skin infections. Clematis is also a constituent of Bach's Rescue Remedy. Leaf extracts from two Ethiopian species (Clematis longicauda steud ex A. Rich. and Clematis burgensis Engl.) are used locally to treat ear disorders and eczema. Phytochemical screening of the extracts from both of these species showed antibacterial and antifungal activity. The extracts of these plants also possess wound healing and anti-inflammatory activities which could also be attributed to the phytoconstituents. Clematis has been listed as one of the 38 plants used to prepare Bach flower remedies, a kind of alternative medicine promoted for its effect on health.
Half-Life: C.A.G.E.D. (also stylized as Half-Life: Caged) is a game modification of Half-Life by Cayle George and Future Games Select released on September 21, 2017. Made using the GoldSrc engine, the mod includes a single-player campaign in which the player must escape from a closely guarded prison. The mod was released on Microsoft Windows via Steam and was made available on macOS and Linux in December 2017.
Sources: en.wikipedia.org
It is a synthetic research compound that activates REV-ERB nuclear receptors. It is not an approved drug or dietary supplement. Most information comes from cell and animal studies.
It binds REV-ERBα and REV-ERBβ and changes transcription of metabolic genes. This can affect circadian rhythm, lipid use, and mitochondrial function. The full downstream effects are still under study.
No. Some rodent studies show increased endurance, but controlled human trials are lacking. Claims about human performance are not established by published evidence.
SR9009 is a synthetic research compound that acts on REV-ERB nuclear receptors. It is not approved for human use and is sold only as a research chemical. Its effects have been studied mainly in cells and rodents.