Everything below concerns REV-ERB agonist. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Updated 2025-12-17. Numbers and descriptions here follow the published literature rather than marketing material.
Detection in biological samples can be complicated by rapid metabolism and low circulating concentrations. Some studies report phase I and phase II metabolites, and analytical methods may need to target those species in addition to the parent compound. Immunoassays are not broadly available, so mass spectrometry remains the main confirmatory approach. For anti-doping testing, laboratories look for SR9009 and its metabolites using validated LC-MS methods. Open questions include how long metabolites remain detectable and how different routes of administration alter detection windows.
In laboratory settings, SR9009 is typically characterized by liquid chromatography–mass spectrometry (LC-MS) or high-performance liquid chromatography with ultraviolet detection (HPLC-UV). These methods can confirm identity and estimate purity, but they require reference standards for accurate quantification. Because SR9009 is not a licensed pharmaceutical, no harmonized pharmacopeial monograph exists. Laboratories often validate in-house methods for matrices such as plasma, urine, or cell culture media. Sample preparation may involve protein precipitation or liquid-liquid extraction before analysis.
Physicochemical behavior influences handling. SR9009 is described as a solid with limited aqueous solubility, so organic solvents such as dimethyl sulfoxide or ethanol are common in research stock solutions. Aqueous dilution can produce precipitates if the organic content is too low. Light, heat, and repeated freeze-thaw cycles may affect stability. Storage recommendations usually specify a desiccated freezer environment protected from light, but exact stability data depend on the formulation and matrix.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Appearance | Off-white to pale yellow solid | Visual description varies with purity and source |
| Solubility | Soluble in DMSO and ethanol; poorly soluble in water | Organic stock solutions are common in research |
| Typical storage | -20 °C, desiccated, protected from light | Avoid repeated freeze-thaw cycles |
| Typical analytical method | LC-MS or HPLC-UV | Reference standards are needed for quantification |
| Molar mass | Approximately 437.9 g/mol | Calculated from the reported free-base formula |
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.
SR9009 is often grouped with compounds studied for circadian and metabolic regulation rather than with classical anabolic steroids. Its interactions with nuclear receptors differ from those of androgen receptor ligands, and its proposed mechanisms involve transcriptional control rather than direct hormone signaling. Some sources classify it as a metabolic modulator because of observed effects on energy utilization. The distinction matters for regulation and for interpreting research results across different compound classes.
SR9009 is a synthetic small molecule developed as a REV-ERB agonist. It binds to REV-ERBα and REV-ERBβ, nuclear receptors that help regulate circadian rhythms and metabolic gene expression. In cell and animal studies, the compound alters lipid and glucose handling and influences skeletal muscle oxidative capacity. Its exact effects in humans remain largely uncharacterized because controlled clinical trials have not been reported. The molecule is frequently described in preclinical literature as a metabolic modulator.
Research interest in SR9009 grew from studies showing improved running endurance in mice after short treatment periods. Those experiments linked the compound to increased mitochondrial content and fatty acid oxidation in muscle, but the findings come from animal models and specific dosing schedules. Independent replication has been limited, and the pathways connecting REV-ERB activation to exercise performance are still being mapped. Whether similar responses occur in humans is an open question.
==== Dentistry ==== Soviet dental technology and dental health were considered extremely bad; in 1991, the average 35-year-old had 12 to 14 cavities, fillings or missing teeth. Toothpaste was often not available, and toothbrushes did not conform to standards of modern dentistry.
==== Comparisons ==== Its healing efficacy against ulceration is significantly greater than that of other zinc complexes, free L-carnosine, and zinc D-carnosine (which is not sold as a supplement to consumers). The pharmacological activity of zinc L-carnosine seems attributable mainly to zinc ion, presumably transported effectively into the ulcer by means of L-carnosine together with the action of L-carnosine itself. In contrast, a simple mixture of L-carnosine and zinc had a lesser effect, presumably due to rapid diffusion of L-carnosine and zinc ion in the entire stomach. Per preclinical data, zinc L-carnosine is superior to zinc sulfide for mucositis.
Pentalenolactone D synthase (EC 1.14.13.170, penE (gene), pntE (gene)) is an enzyme with systematic name 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (pentalenolactone-D forming). It catalyses the following chemical reaction
The number of PPIs identified is usually low because of a high false negative rate; and, understates membrane proteins, for example. During his studies, Molecular biologist Anton Yuryev used yeast two-hybrid screening to identify novel protein interactions linking transcription with post‑transcriptional modification, demonstrating the utility of these methods for revealing functional, isoform‑specific PPIs. In initial studies that utilized Y2H, proper controls for false positives (e.g. when DB-X activates the reporter gene without the presence of AD-Y) were frequently not done, leading to a higher than normal false positive rate. An empirical framework must be implemented to control for these false positives. Limitations in lower coverage of membrane proteins have been overcoming by the emergence of yeast two-hybrid variants, such as the membrane yeast two-hybrid (MYTH) and the split-ubiquitin system, which are not limited to interactions that occur in the nucleus; and, the bacterial two-hybrid system, performed in bacteria;
=== Toxicity due to size of nanoparticles === Toxicity in certain systems can also be dependent on the size of the nanoparticle. AuNSs size 1.4 nm were found to be toxic in human skin cancer cells (SK-Mel-28), human cervical cancer cells (HeLa), mouse fibroblast cells (L929), and mouse macrophages (J774A.1), while 0.8, 1.2, and 1.8 nm sized AuNSs were less toxic by a six-fold amount and 15 nm AuNSs were nontoxic. There is some evidence for AuNP buildup after injection in in vivo studies, but this is very size dependent. 1.8 nm AuNPs were found to be almost totally trapped in the lungs of rats. Different sized AuNPs were found to build-up in the blood, brain, stomach, pancreas, kidneys, liver, and spleen. Biosafety and biokinetics investigations on biodegradable ultrasmall-in-nano architectures have demonstrated that gold nanoparticles are able to avoid metal accumulation in organisms through escaping by the renal pathway.
Sources: en.wikipedia.org
Now EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming] and EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming] EC 1.1.1.6: glycerol dehydrogenase EC 1.1.1.7: propanediol-phosphate dehydrogenase EC 1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD+) EC 1.1.1.9: D-xylulose reductase EC 1.1.1.10: L-xylulose reductase EC 1.1.1.11: D-arabinitol 4-dehydrogenase EC 1.1.1.12: L-arabinitol 4-dehydrogenase EC 1.1.1.13: L-arabinitol 2-dehydrogenase EC 1.1.1.14: L-iditol 2-dehydrogenase EC 1.1.1.15: D-iditol 2-dehydrogenase EC 1.1.1.16: galactitol 2-dehydrogenase EC 1.1.1.17: mannitol-1-phosphate 5-dehydrogenase EC 1.1.1.18: inositol 2-dehydrogenase EC 1.1.1.19: glucuronate reductase EC 1.1.1.20: glucuronolactone reductase EC 1.1.1.207: (-)-menthol dehydrogenase EC 1.1.1.208: (+)-neomenthol dehydrogenase EC 1.1.1.21: aldose reductase EC 1.1.1.22: UDP-glucose 6-dehydrogenase EC 1.1.1.222: (R)-4-hydroxyphenyllactate dehydrogenase EC 1.1.1.23: histidinol dehydrogenase| EC 1.1.1.24: quinate/shikimate dehydrogenase (NAD+) EC 1.1.1.25: shikimate dehydrogenase (NADP+) EC 1.1.1.26: glyoxylate reductase EC 1.1.1.27: L-lactate dehydrogenase EC 1.1.1.28: D-lactate dehydrogenase EC 1.1.1.29: glycerate dehydrogenase EC 1.1.1.30: 3-hydroxybutyrate dehydrogenase EC 1.1.1.31: 3-hydroxyisobutyrate dehydrogenase EC 1.1.1.32: mevaldate reductase EC 1.1.1.33: mevaldate reductase (NADPH) EC 1.1.1.34: hydroxymethylglutaryl-CoA reductase (NADPH) EC 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase EC 1.1.1.36: acetoacetyl-CoA reductase EC 1.1.1.37: malate dehydrogenase EC 1.1.1.38: malate dehydrogenase (oxaloacetate-decarboxylating) EC 1.1.1.39: malate dehydrogenase (decarboxylating) EC 1.1.1.40: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) EC 1.1.1.41: isocitrate dehydrogenase (NAD+) EC 1.1.1.42: isocitrate dehydrogenase (NADP+) EC 1.1.1.43: phosphogluconate 2-dehydrogenase EC 1.1.1.44: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) EC 1.1.1.45: L-gulonate 3-dehydrogenase EC 1.1.1.46: L-arabinose 1-dehydrogenase EC 1.1.1.47: glucose 1-dehydrogenase [NAD(P)+)] EC 1.1.1.48: D-galactose 1-dehydrogenase EC 1.1.1.49: glucose-6-phosphate dehydrogenase (NADP+) EC 1.1.1.50: 3α-hydroxysteroid 3-dehydrogenase (Si-specific) EC 1.1.1.51: 3(or 17)β-hydroxysteroid dehydrogenase EC 1.1.1.52: 3α-hydroxycholanate dehydrogenase (NAD+) EC 1.1.1.53: 3α(or 20β)-hydroxysteroid dehydrogenase EC 1.1.1.54: allyl-alcohol dehydrogenase EC 1.1.1.55: lactaldehyde reductase (NADPH) EC 1.1.1.56: ribitol 2-dehydrogenase EC 1.1.1.57: fructuronate reductase EC 1.1.1.58: tagaturonate reductase EC 1.1.1.59: 3-hydroxypropionate dehydrogenase EC 1.1.1.60: 2-hydroxy-3-oxopropionate reductase EC 1.1.1.61: 4-hydroxybutyrate dehydrogenase EC 1.1.1.62: 17β-estradiol 17-dehydrogenase EC 1.1.1.63: testosterone 17β-dehydrogenase. Now EC 1.1.1.239, 3α(17β)-hydroxysteroid dehydrogenase (NAD+) EC 1.1.1.64: testosterone 17β-dehydrogenase (NADP+) EC 1.1.1.65: pyridoxine 4-dehydrogenase EC 1.1.1.66: ω-hydroxydecanoate dehydrogenase EC 1.1.1.67: mannitol 2-dehydrogenase EC 1.1.1.68: 5,10-methylenetetrahydrofolate reductase. Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H] EC 1.1.1.69: gluconate 5-dehydrogenase EC 1.1.1.70: D-glucuronolactone dehydrogenase. Now included with EC 1.2.1.3 aldehyde dehydrogenase (NAD+) EC 1.1.1.71: alcohol dehydrogenase [NAD(P)+] EC 1.1.1.72: glycerol dehydrogenase (NADP+) EC 1.1.1.73: octanol dehydrogenase EC 1.1.1.74: D-aminopropanol dehydrogenase (reaction due to EC 1.1.1.4 (R,R)-butanediol dehydrogenase) EC 1.1.1.75: (R)-aminopropanol dehydrogenase EC 1.1.1.76: (S,S)-butanediol dehydrogenase EC 1.1.1.77: lactaldehyde reductase EC 1.1.1.78: methylglyoxal reductase (NADH-dependent) EC 1.1.1.79: glyoxylate reductase (NADP+) EC 1.1.1.80: isopropanol dehydrogenase (NADP+) EC 1.1.1.81: hydroxypyruvate reductase EC 1.1.1.82: malate dehydrogenase (NADP+) EC 1.1.1.83: D-malate dehydrogenase (decarboxylating) EC 1.1.1.84: dimethylmalate dehydrogenase EC 1.1.1.85: 3-isopropylmalate dehydrogenase EC 1.1.1.86: ketol-acid reductoisomerase (NADP+) EC 1.1.1.87: homoisocitrate dehydrogenase EC 1.1.1.88: hydroxymethylglutaryl-CoA reductase EC 1.1.1.89: dihydroxyisovalerate dehydrogenase (isomerizing). Now included with EC 1.1.1.86 ketol-acid reductoisomerase EC 1.1.1.90: aryl-alcohol dehydrogenase EC 1.1.1.91: aryl-alcohol dehydrogenase (NADP+) EC 1.1.1.92: oxaloglycolate reductase (decarboxylating) EC 1.1.1.93: tartrate dehydrogenase EC 1.1.1.94: glycerol-3-phosphate dehydrogenase [NAD(P)+] EC 1.1.1.95: phosphoglycerate dehydrogenase EC 1.1.1.96: diiodophenylpyruvate reductase EC 1.1.1.97: 3-hydroxybenzyl-alcohol dehydrogenase EC 1.1.1.98: (R)-2-hydroxy-fatty-acid dehydrogenase EC 1.1.1.99: (S)-2-hydroxy-fatty-acid dehydrogenase EC 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase EC 1.1.1.101: acylglycerone-phosphate reductase EC 1.1.1.102: 3-dehydrosphinganine reductase EC 1.1.1.103: L-threonine 3-dehydrogenase EC 1.1.1.104: 4-oxoproline reductase EC 1.1.1.105: all-trans-retinol dehydrogenase (NAD+) EC 1.1.1.106: pantoate 4-dehydrogenase EC 1.1.1.107: pyridoxal 4-dehydrogenase EC 1.1.1.108: carnitine 3-dehydrogenase EC 1.1.1.109: Now EC 1.3.1.28, 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase EC 1.1.1.110: aromatic 2-oxoacid reductase EC 1.1.1.111: 3-(imidazol-5-yl)lactate dehydrogenase EC 1.1.1.112: indanol dehydrogenase EC 1.1.1.113: L-xylose 1-dehydrogenase EC 1.1.1.114: apiose 1-reductase EC 1.1.1.115: ribose 1-dehydrogenase (NADP+) EC 1.1.1.116: D-arabinose 1-dehydrogenase (NAD+) EC 1.1.1.117: D-arabinose 1-dehydrogenase [NAD(P)+] EC 1.1.1.118: glucose 1-dehydrogenase (NAD+) EC 1.1.1.119: glucose 1-dehydrogenase (NADP+) EC 1.1.1.120: galactose 1-dehydrogenase (NADP+) EC 1.1.1.121: aldose 1-dehydrogenase (NAD+) EC 1.1.1.122: D-threo-aldose 1-dehydrogenase EC 1.1.1.123: sorbose 5-dehydrogenase (NADP+) EC 1.1.1.124: fructose 5-dehydrogenase (NADP+) EC 1.1.1.125: 2-deoxy-D-gluconate 3-dehydrogenase EC 1.1.1.126: 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase EC 1.1.1.127: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase EC 1.1.1.128: The reaction described is covered by EC 1.1.1.264, L-idonate 5-dehydrogenase. EC 1.1.1.129: L-threonate 3-dehydrogenase EC 1.1.1.130: 3-dehydro-L-gulonate 2-dehydrogenase EC 1.1.1.131: mannuronate reductase EC 1.1.1.132: GDP-mannose 6-dehydrogenase EC 1.1.1.133: dTDP-4-dehydrorhamnose reductase EC 1.1.1.134: dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+) EC 1.1.1.135: GDP-6-deoxy-D-talose 4-dehydrogenase EC 1.1.1.136: UDP-N-acetylglucosamine 6-dehydrogenase EC 1.1.1.137: ribitol-5-phosphate 2-dehydrogenase EC 1.1.1.138: mannitol 2-dehydrogenase (NADP+) EC 1.1.1.139: polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase EC 1.1.1.140: sorbitol-6-phosphate 2-dehydrogenase EC 1.1.1.141: 15-hydroxyprostaglandin dehydrogenase (NAD+) EC 1.1.1.142: D-pinitol dehydrogenase EC 1.1.1.143: sequoyitol dehydrogenase EC 1.1.1.144: perillyl-alcohol dehydrogenase EC 1.1.1.145: 3β-hydroxy-Δ5-steroid dehydrogenase EC 1.1.1.146: 11β-hydroxysteroid dehydrogenase EC 1.1.1.147: 16α-hydroxysteroid dehydrogenase EC 1.1.1.148: estradiol 17α-dehydrogenase EC 1.1.1.149: 20α-hydroxysteroid dehydrogenase EC 1.1.1.150: 21-hydroxysteroid dehydrogenase (NAD+) EC 1.1.1.151: 21-hydroxysteroid dehydrogenase (NADP+) EC 1.1.1.152: 3α-hydroxy-5β-androstane-17-one 3α-dehydrogenase EC 1.1.1.153: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) EC 1.1.1.154: ureidoglycolate dehydrogenase EC 1.1.1.155: homoisocitrate dehydrogenase. The enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase EC 1.1.1.156: glycerol 2-dehydrogenase (NADP+) EC 1.1.1.157: 3-hydroxybutyryl-CoA dehydrogenase EC 1.1.1.158: Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase EC 1.1.1.159: 7α-hydroxysteroid dehydrogenase EC 1.1.1.160: dihydrobunolol dehydrogenase EC 1.1.1.161: The activity is part of EC 1.14.13.15, cholestanetriol 26-monooxygenase EC 1.1.1.162: erythrulose reductase EC 1.1.1.163: cyclopentanol dehydrogenase EC 1.1.1.164: hexadecanol dehydrogenase EC 1.1.1.165: 2-alkyn-1-ol dehydrogenase EC 1.1.1.166: hydroxycyclohexanecarboxylate dehydrogenase EC 1.1.1.167: hydroxymalonate dehydrogenase EC 1.1.1.168: 2-dehydropantolactone reductase (Re-specific) EC 1.1.1.169: 2-dehydropantoate 2-reductase EC 1.1.1.170: 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating) EC 1.1.1.171: Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H] EC 1.1.1.172: 2-oxoadipate reductase EC 1.1.1.173: L-rhamnose 1-dehydrogenase EC 1.1.1.174: cyclohexane-1,2-diol dehydrogenase EC 1.1.1.175: D-xylose 1-dehydrogenase EC 1.1.1.176: 12α-hydroxysteroid dehydrogenase EC 1.1.1.177: glycerol-3-phosphate 1-dehydrogenase (NADP+) EC 1.1.1.178: 3-hydroxy-2-methylbutyryl-CoA dehydrogenase EC 1.1.1.179: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) EC 1.1.1.180: Now included with EC 1.1.1.131 mannuronate reductase EC 1.1.1.181: cholest-5-ene-3β,7α-diol 3β-dehydrogenase EC 1.1.1.182: Now included with EC 1.1.1.198 (+)-borneol dehydrogenase, EC 1.1.1.227 (-)-borneol dehydrogenase and EC 1.1.1.228 (+)-sabinol dehydrogenase EC 1.1.1.183: geraniol dehydrogenase (NADP+) EC 1.1.1.184: carbonyl reductase (NADPH) EC 1.1.1.185: L-glycol dehydrogenase EC 1.1.1.186: dTDP-galactose 6-dehydrogenase EC 1.1.1.187: GDP-4-dehydro-D-rhamnose reductase EC 1.1.1.188: prostaglandin-F synthase EC 1.1.1.189: prostaglandin-E2 9-reductase EC 1.1.1.190: indole-3-acetaldehyde reductase (NADH) EC 1.1.1.191: indole-3-acetaldehyde reductase (NADPH) EC 1.1.1.192: long-chain-alcohol dehydrogenase EC 1.1.1.193: 5-amino-6-(5-phosphoribosylamino)uracil reductase EC 1.1.1.194: coniferyl-alcohol dehydrogenase EC 1.1.1.195: cinnamyl-alcohol dehydrogenase EC 1.1.1.196: 15-hydroxyprostaglandin-D dehydrogenase (NADP+) EC 1.1.1.197: 15-hydroxyprostaglandin dehydrogenase (NADP+) EC 1.1.1.198: (+)-borneol dehydrogenase EC 1.1.1.199: (S)-usnate reductase EC 1.1.1.200: aldose-6-phosphate reductase (NADPH) EC 1.1.1.228: (+)-sabinol dehydrogenase EC 1.1.1.251: galactitol-1-phosphate 5-dehydrogenase EC 1.1.1.252: tetrahydroxynaphthalene reductase EC 1.1.1.253: Now EC 1.5.1.33, pteridine reductase EC 1.1.1.254: (S)-carnitine 3-dehydrogenase EC 1.1.1.255: mannitol dehydrogenase EC 1.1.1.256: fluoren-9-ol dehydrogenase EC 1.1.1.257: 4-(hydroxymethyl)benzenesulfonate dehydrogenase EC 1.1.1.258: 6-hydroxyhexanoate dehydrogenase EC 1.1.1.259: 3-hydroxypimeloyl-CoA dehydrogenase EC 1.1.1.260: sulcatone reductase EC 1.1.1.261: sn-glycerol-1-phosphate dehydrogenase EC 1.1.1.262: 4-hydroxythreonine-4-phosphate dehydrogenase EC 1.1.1.263: 1,5-anhydro-D-fructose reductase EC 1.1.1.264: L-idonate 5-dehydrogenase EC 1.1.1.265: 3-methylbutanal reductase EC 1.1.1.266: dTDP-4-dehydro-6-deoxyglucose reductase EC 1.1.1.267: 1-deoxy-D-xylulose-5-phosphate reductoisomerase EC 1.1.1.268: 2-(R)-hydroxypropyl-CoM dehydrogenase EC 1.1.1.269: 2-(S)-hydroxypropyl-CoM dehydrogenase EC 1.1.1.270: 3β-hydroxysteroid 3-dehydrogenase EC 1.1.1.271: GDP-L-fucose synthase EC 1.1.1.272: D-2-hydroxyacid dehydrogenase (NADP+) EC 1.1.1.273: vellosimine dehydrogenase EC 1.1.1.274: 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming) EC 1.1.1.275: (+)-trans-carveol dehydrogenase EC 1.1.1.276: serine 3-dehydrogenase (NADP+) EC 1.1.1.277: 3β-hydroxy-5β-steroid dehydrogenase EC 1.1.1.278: 3β-hydroxy-5α-steroid dehydrogenase EC 1.1.1.279: (R)-3-hydroxyacid-ester dehydrogenase EC 1.1.1.280: (S)-3-hydroxyacid-ester dehydrogenase EC 1.1.1.281: GDP-4-dehydro-6-deoxy-D-mannose reductase EC 1.1.1.282: Quinate/shikimate dehydrogenase EC 1.1.1.283: methylglyoxal reductase (NADPH-dependent) EC 1.1.1.284: S-(hydroxymethyl)glutathione dehydrogenase EC 1.1.1.285: 3′′-deamino-3′′-oxonicotianamine reductase EC 1.1.1.286: isocitrate—homoisocitrate dehydrogenase EC 1.1.1.287: D-arabinitol dehydrogenase (NADP+) EC 1.1.1.288: xanthoxin dehydrogenase EC 1.1.1.289: sorbose reductase EC 1.1.1.290: 4-phosphoerythronate dehydrogenase EC 1.1.1.291: 2-hydroxymethylglutarate dehydrogenase EC 1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) EC 1.1.1.293: tropinone reductase I. This enzyme was already in the Enzyme List as EC 1.1.1.206, tropine dehydrogenase so EC 1.1.1.293 has been withdrawn at the public-review stage EC 1.1.1.294: chlorophyll(ide) b reductase EC 1.1.1.295: momilactone-A synthase EC 1.1.1.296: dihydrocarveol dehydrogenase EC 1.1.1.297: limonene-1,2-diol dehydrogenase EC 1.1.1.298: 3-hydroxypropionate dehydrogenase (NADP+) EC 1.1.1.299: malate dehydrogenase [NAD(P)+)] EC 1.1.1.300: NADP-retinol dehydrogenase EC 1.1.1.301: D-arabitol-phosphate dehydrogenase EC 1.1.1.302: 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5′-phosphate reductase EC 1.1.1.303: Diacetyl reductase ((R)-acetoin forming) EC 1.1.1.304: Diacetyl reductase ((S)-acetoin forming) EC 1.1.1.305: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) EC 1.1.1.306: S-(hydroxymethyl)mycothiol dehydrogenase EC 1.1.1.307: D-xylose reductase EC 1.1.1.308: sulfopropanediol 3-dehydrogenase EC 1.1.1.309: phosphonoacetaldehyde reductase (NADH) EC 1.1.1.310: (S)-sulfolactate dehydrogenase EC 1.1.1.311: (S)-1-phenylethanol dehydrogenase EC 1.1.1.312: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase EC 1.1.1.313: sulfoacetaldehyde reductase EC 1.1.1.314: Now known to be catalyzed by EC 1.14.14.95, germacrene A hydroxylase EC 1.1.1.315: 11-cis-retinol dehydrogenase EC 1.1.1.316: L-galactose 1-dehydrogenase EC 1.1.1.317: perakine reductase EC 1.1.1.318: eugenol synthase EC 1.1.1.319: isoeugenol synthase EC 1.1.1.320: benzil reductase [(S)-benzoin forming] EC 1.1.1.321: benzil reductase [(R)-benzoin forming] EC 1.1.1.322: (–)-endo-fenchol dehydrogenase EC 1.1.1.323: (+)-thujan-3-ol dehydrogenase EC 1.1.1.324: 8-hydroxygeraniol dehydrogenase EC 1.1.1.325: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming) EC 1.1.1.326: zerumbone synthase EC 1.1.1.327: 5-exo-hydroxycamphor dehydrogenase EC 1.1.1.328: nicotine blue oxidoreductase EC 1.1.1.329: 2-deoxy-scyllo-inosamine dehydrogenase EC 1.1.1.330: very-long-chain 3-oxoacyl-CoA reductase EC 1.1.1.331: secoisolariciresinol dehydrogenase EC 1.1.1.332: chanoclavine-I dehydrogenase EC 1.1.1.333: decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase EC 1.1.1.334: methylecgonone reductase EC 1.1.1.335: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase EC 1.1.1.336: UDP-N-acetyl-D-mannosamine dehydrogenase EC 1.1.1.337: L-2-hydroxycarboxylate dehydrogenase (NAD+) EC 1.1.1.338: (2R)-3-sulfolactate dehydrogenase (NADP+) EC 1.1.1.339: dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+) EC 1.1.1.340: 1-deoxy-11β-hydroxypentalenate dehydrogenase EC 1.1.1.341: CDP-abequose synthase EC 1.1.1.342: CDP-paratose synthase EC 1.1.1.343: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) EC 1.1.1.344: dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+] EC 1.1.1.345: D-2-hydroxyacid dehydrogenase (NAD+) EC 1.1.1.346: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming) EC 1.1.1.347: geraniol dehydrogenase (NAD+) EC 1.1.1.348: (3R)-2′-hydroxyisoflavanone reductase EC 1.1.1.349: norsolorinic acid ketoreductase EC 1.1.1.350: ureidoglycolate dehydrogenase (NAD+) EC 1.1.1.351: phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating] EC 1.1.1.352: 5′-hydroxyaverantin dehydrogenase EC 1.1.1.353: versiconal hemiacetal acetate reductase EC 1.1.1.354: farnesol dehydrogenase (NAD+) EC 1.1.1.355: 2′-dehydrokanamycin reductase EC 1.1.1.356: GDP-L-colitose synthase EC 1.1.1.357: 3α-hydroxysteroid 3-dehydrogenase EC 1.1.1.358: 2-dehydropantolactone reductase EC 1.1.1.359: aldose 1-dehydrogenase [NAD(P)+] EC 1.1.1.360: glucose/galactose 1-dehydrogenase EC 1.1.1.361: glucose-6-phosphate 3-dehydrogenase EC 1.1.1.362: aklaviketone reductase EC 1.1.1.363: glucose-6-phosphate dehydrogenase [NAD(P)+] EC 1.1.1.364: dTDP-4-dehydro-6-deoxy-α-D-gulose 4-ketoreductase EC 1.1.1.365: D-galacturonate reductase EC 1.1.1.366: L-idonate 5-dehydrogenase (NAD+) EC 1.1.1.367: UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase EC 1.1.1.368: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase EC 1.1.1.369: D-chiro-inositol 1-dehydrogenase EC 1.1.1.370: scyllo-inositol 2-dehydrogenase (NAD+) EC 1.1.1.371: scyllo-inositol 2-dehydrogenase (NADP+) EC 1.1.1.372: D/L-glyceraldehyde reductase EC 1.1.1.373: sulfolactaldehyde 3-reductase EC 1.1.1.374: UDP-N-acetylglucosamine 3-dehydrogenase EC 1.1.1.375: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+] EC 1.1.1.376: L-arabinose 1-dehydrogenase [NAD(P)+] EC 1.1.1.377: L-rhamnose 1-dehydrogenase (NADP+) EC 1.1.1.378: L-rhamnose 1-dehydrogenase [NAD(P)+] EC 1.1.1.379: (R)-mandelate dehydrogenase EC 1.1.1.380: L-gulonate 5-dehydrogenase EC 1.1.1.381: 3-hydroxy acid dehydrogenase EC 1.1.1.382: ketol-acid reductoisomerase (NAD+) EC 1.1.1.383: ketol-acid reductoisomerase [NAD(P)+] EC 1.1.1.384: dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase EC 1.1.1.385: dihydroanticapsin dehydrogenase EC 1.1.1.386: ipsdienol dehydrogenase EC 1.1.1.387: L-serine 3-dehydrogenase (NAD+) EC 1.1.1.388: glucose-6-phosphate dehydrogenase (NAD+) EC 1.1.1.389: 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase EC 1.1.1.390: sulfoquinovose 1-dehydrogenase EC 1.1.1.391: 3β-hydroxycholanate 3-dehydrogenase (NAD+) EC 1.1.1.392: 3α-hydroxycholanate dehydrogenase (NADP+) EC 1.1.1.393: 3β-hydroxycholanate 3-dehydrogenase (NADP+) EC 1.1.1.394: aurachin B dehydrogenase EC 1.1.1.395: 3α-hydroxy bile acid-CoA-ester 3-dehydrogenase EC 1.1.1.396: bacteriochlorophyllide a dehydrogenase EC 1.1.1.397: β-methylindole-3-pyruvate reductase EC 1.1.1.398: 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase EC 1.1.1.399: 2-oxoglutarate reductase EC 1.1.1.400: 2-methyl-1,2-propanediol dehydrogenase EC 1.1.1.401: 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+) EC 1.1.1.402: D-erythritol 1-phosphate dehydrogenase EC 1.1.1.403: D-threitol dehydrogenase (NAD+) EC 1.1.1.404: tetrachlorobenzoquinone reductase EC 1.1.1.405: ribitol-5-phosphate 2-dehydrogenase (NADP+) EC 1.1.1.406: galactitol 2-dehydrogenase (L-tagatose-forming) EC 1.1.1.407: D-altritol 5-dehydrogenase EC 1.1.1.408: 4-phospho-D-threonate 3-dehydrogenase EC 1.1.1.409: 4-phospho-D-erythronate 3-dehydrogenase EC 1.1.1.410: D-erythronate 2-dehydrogenase EC 1.1.1.411: L-threonate 2-dehydrogenase EC 1.1.1.412: 2-alkyl-3-oxoalkanoate reductase EC 1.1.1.413: A-factor type γ-butyrolactone 1′-reductase (1S-forming) EC 1.1.1.414: L-galactonate 5-dehydrogenase EC 1.1.1.415: noscapine synthase EC 1.1.1.416: isopyridoxal dehydrogenase (5-pyridoxolactone-forming) EC 1.1.1.417: 3β-hydroxysteroid-4β-carboxylate 3-dehydrogenase (decarboxylating) EC 1.1.1.418: plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating) EC 1.1.1.419: nepetalactol dehydrogenase EC 1.1.1.420: D-apiose dehydrogenase EC 1.1.1.421: D-apionate oxidoisomerase EC 1.1.1.422: pseudoephedrine dehydrogenase EC 1.1.1.423: (1R,2S)-ephedrine 1-dehydrogenase EC 1.1.1.424: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming) EC 1.1.1.425: levoglucosan dehydrogenase EC 1.1.1.426: UDP-N-acetyl-α-D-quinovosamine dehydrogenase
Eccles, Jessica A.; Cadar, Dorina; Quadt, Lisa; Hakim, Alan J.; Gall, Nicholas; Bowyer, Vicky; Cheetham, Nathan; Steves, Claire J.; Critchley, Hugo D.; Davies, Kevin A. (2024). "Is joint hypermobility linked to self-reported non-recovery from COVID-19? Case–control evidence from the British COVID Symptom Study Biobank". BMJ Public Health. 2 (1) e000478. doi:10.1136/bmjph-2023-000478. PMC 11812800. PMID 40018183.
=== Men's physique === Due to those who found open-bodybuilding to be "too big" or "ugly" and unhealthy, a new category was started in 2013. The first Men's Physique Olympia winner was Mark Wingson, who was followed by Jeremy Buendia for four consecutive years. Like open-bodybuilding, the federations in which bodybuilders can compete are natural divisions as well as normal ones. The main difference between the two is that men's physique competitors pose in board shorts rather than a traditional posing suit and open-bodybuilders are much larger and are more muscular than the men's physique competitors. Open-bodybuilders have an extensive routine for posing while the Physique category is primarily judged by the front and back poses. Many of the men's physique competitors are not above 200 lbs and have a bit of a more attainable and aesthetic physique in comparison to open-bodybuilders. Although this category started off slowly, it has grown tremendously, and currently men's physique seems to be a more popular class than open-bodybuilding.
When the band emerged yet again in 1993, Hartman and Porter had retired from the road for good but Knudsen and McFee rejoined the Doobie Brothers on a full-time basis after Southern Pacific disbanded. Joined by Ockerman, Bumpus and Weeks, the group toured with Four Wheel Drive as the opening act. After Weeks left the tour to resume his session work, Cowan played bass for both bands. Bumpus also left to join the reunited Steely Dan, giving way to saxophonist, keyboardist and harmonica player Danny Hull. Former band member Chet McCracken temporarily filled in for an injured Hossack in July 1993. Their 1994 tour included co-headlining appearances with Foreigner. With renewed energy in the mid-1990s, the band began to experiment with different arrangements of several tunes. They even pulled from McDonald's songbook from time to time, eventually restoring "Takin' it to the Streets" to the setlist with Simmons and new bass guitarist Skylark (who joined in 1995) substituting for McDonald on lead vocals.
==== Top-fed deep water culture ==== Top-fed deep water culture is a technique involving delivering highly oxygenated nutrient solution direct to the root zone of plants. While deep water culture involves the plant roots hanging down into a reservoir of nutrient solution, in top-fed deep water culture the solution is pumped from the reservoir up to the roots (top feeding). The water is released over the plant's roots and then runs back into the reservoir below in a constantly recirculating system. As with deep water culture, there is an airstone in the reservoir that pumps air into the water via a hose from outside the reservoir. The airstone helps add oxygen to the water. Both the airstone and the water pump run 24 hours a day. The biggest advantage of top-fed deep water culture over standard deep water culture is increased growth during the first few weeks. With deep water culture, there is a time when the roots have not reached the water yet. With top-fed deep water culture, the roots get easy access to water from the beginning and will grow to the reservoir below much more quickly than with a deep water culture system. Once the roots have reached the reservoir below, there is not a huge advantage with top-fed deep water culture over standard deep water culture. However, due to the quicker growth in the beginning, grow time can be reduced by a few weeks.
Sources: en.wikipedia.org
== Formation == Aβ is formed after sequential cleavage of the amyloid precursor protein (APP), a transmembrane glycoprotein of undetermined function. APP can be cleaved by the proteolytic enzymes α-, β- and γ-secretase; Aβ protein is generated by successive action of the β and γ secretases. The γ secretase, which produces the C-terminal end of the Aβ peptide, cleaves within the transmembrane region of APP and can generate a number of isoforms of 30–51 amino acid residues in length. The most common isoforms are Aβ40 and Aβ42; the longer form is typically produced by cleavage that occurs in the endoplasmic reticulum, while the shorter form is produced by cleavage in the trans-Golgi network.
The body of a fish is divided into a head, trunk and tail, although the divisions between the three are not always externally visible. The skeleton, which forms the support structure inside the fish, is either made of cartilage, in cartilaginous fish, or bone in bony fish. The main skeletal element is the vertebral column, composed of articulating vertebrae which are lightweight yet strong. The ribs attach to the spine and there are no limbs or limb girdles. The main external features of the fish, the fins, are composed of either bony or soft spines called rays, which with the exception of the caudal fins, have no direct connection with the spine. They are supported by the muscles which compose the main part of the trunk. The heart has two chambers and pumps the blood through the respiratory surfaces of the gills and on round the body in a single circulatory loop. The eyes are adapted for seeing underwater and have only local vision. There is an inner ear but no external or middle ear. Low frequency vibrations are detected by the lateral line system of sense organs that run along the length of the sides of fish, and these respond to nearby movements and to changes in water pressure. Sharks and rays are basal fish with numerous primitive anatomical features similar to those of ancient fish, including skeletons composed of cartilage. Their bodies tend to be dorso-ventrally flattened, they usually have five pairs of gill slits and a large mouth set on the underside of the head. The dermis is covered with separate dermal placoid scales.
== History == Creatine was first identified in 1832 when Michel Eugène Chevreul isolated the precipitate from the basified water-extract of skeletal muscle. He later named the crystallized precipitate after the Greek word for meat, κρέας (kreas). In 1928, creatine was shown to exist in equilibrium with creatinine. Studies in the 1920s showed that consumption of large amounts of creatine did not result in its excretion. This result pointed to the ability of the body to store creatine, which in turn suggested its use as a dietary supplement. In 1912, Harvard University researchers Otto Folin and Willey Glover Denis found evidence that ingesting creatine can dramatically boost the creatine content of the muscle. The discovery of phosphocreatine was reported in 1927. In the 1960s, the enzyme creatine kinase was shown to phosphorylate ADP using phosphocreatine to generate ATP and thus buffering the ATP/ADP ratio. While creatine's influence on physical performance has been well documented since the early twentieth century, it came into public view following the 1992 Olympics in Barcelona. An 7 August 1992 article in The Times reported that Linford Christie, the gold medal winner at 100 metres, had used creatine before the Olympics. An article in Bodybuilding Monthly named Sally Gunnell, who was the gold medalist in the 400-metre hurdles, as another creatine user. In addition, The Times also noted that 110 metre hurdler Colin Jackson began taking creatine before the Olympics.
The decision to release the declaration was taken by the British War Cabinet on 31 October 1917. This followed discussion at four War Cabinet meetings (including the 31 October meeting) over the space of the previous two months. In order to aid the discussions, the War Cabinet Secretariat, led by Maurice Hankey, the Cabinet Secretary and supported by his Assistant Secretaries – primarily Sykes and his fellow Conservative MP and pro-Zionist Leo Amery – solicited outside perspectives to put before the Cabinet. These included the views of government ministers, war allies – notably from President Woodrow Wilson – and in October, formal submissions from six Zionist leaders and four non-Zionist Jews. British officials asked President Wilson for his consent on the matter on two occasions – first on 3 September, when he replied the time was not ripe, and later on 6 October, when he agreed with the release of the declaration.
== Uses == Salts have long had a wide variety of uses and applications. Many minerals are ionic. Humans have processed common salt (sodium chloride) for over 8000 years, using it first as a food seasoning and preservative, and now also in manufacturing, agriculture, water conditioning, for de-icing roads, and many other uses. Many salts are so widely used in society that they go by common names unrelated to their chemical identity. Examples of this include borax, calomel, milk of magnesia, muriatic acid, oil of vitriol, saltpeter, and slaked lime. Soluble salts can easily be dissolved to provide electrolyte solutions. This is a simple way to control the concentration and ionic strength. The concentration of solutes affects many colligative properties, including increasing the osmotic pressure, and causing freezing-point depression and boiling-point elevation. Because the solutes are charged ions they also increase the electrical conductivity of the solution. The increased ionic strength reduces the thickness of the electrical double layer around colloidal particles, and therefore the stability of emulsions and suspensions. The chemical identity of the ions added is also important in many uses. For example, fluoride containing compounds are dissolved to supply fluoride ions for water fluoridation. Solid salts have long been used as paint pigments, and are resistant to organic solvents, but are sensitive to acidity or basicity. Since 1801 pyrotechnicians have described and widely used metal-containing salts as sources of colour in fireworks.
Sources: en.wikipedia.org
It is usually detected by LC-MS or HPLC-UV against a reference standard. In biological matrices, metabolite targeting can improve detection. No universal immunoassay is widely available.
The compound is generally handled as light-sensitive and stored cold and dry. Stability in solution depends on solvent, concentration, and storage time. Specific degradation rates are not fully standardized.
Limited water solubility affects formulation for cell and animal studies. Organic co-solvents are often used to dissolve it. Precipitation can confound assay results if not controlled.
Legality depends on the country and the intended use. In many places it is sold as a research chemical, but sports and medicine regulations restrict it.