This is a working overview of research chemical, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2026-06-13. Anything still debated is marked as such rather than presented as settled.
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.
In rodent studies, SR9009 has been reported to increase mitochondrial content in skeletal muscle and improve exercise endurance under some conditions. These findings led to popular descriptions such as an exercise mimetic, although that term oversimplifies the biology. Effects vary by dose, timing, tissue, and model. The compound's influence on circadian pathways means that time of administration can matter in experiments. Whether similar metabolic changes occur in humans remains largely unexplored in controlled published trials.
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.
Laboratory identification of SR9009 typically relies on chromatographic separation coupled to mass spectrometry, often with ultraviolet detection as a secondary check. Nuclear magnetic resonance spectroscopy can confirm molecular structure when a reference standard is available. Because many suppliers sell the compound as a research chemical, independent identity testing is important for experimental reproducibility. A single retention time is not sufficient proof of identity, especially when related compounds may be present. Purity assessments usually report a percentage based on area normalization.
SR9009 is generally described as poorly soluble in water and more soluble in organic solvents such as dimethyl sulfoxide and ethanol. Stock solutions are commonly prepared in an organic solvent before dilution into an aqueous buffer or vehicle. Precipitation can occur if the organic fraction is reduced too quickly or if the final concentration exceeds the compound's solubility limit. Sonication or gentle warming may aid dissolution in some protocols, but excessive heat can promote degradation. Container material and pH can also influence observed solubility.
| 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 |
Regulatory status varies by country and intended use. Major drug agencies have not granted marketing authorization for SR9009 as a medicine, and it is not listed as a controlled substance in many jurisdictions. It is often sold as a research chemical, a category that may fall outside pharmaceutical manufacturing rules. Buyers should verify local laws and supplier documentation, including certificates of analysis. The lack of standardized quality controls raises concerns about identity, purity, and actual content in products marketed online.
In laboratory settings, SR9009 is commonly identified by its molecular structure and its interaction with REV-ERB receptors. Vendors may list it under synonyms such as Stenabolic or REV-ERB agonist, but those names do not define purity or identity. Analytical confirmation typically uses high-performance liquid chromatography with ultraviolet detection or liquid chromatography–mass spectrometry. A reference standard is needed to compare retention time and mass spectrum, because the compound can be confused with related research chemicals.
Handling practices for SR9009 focus on minimizing degradation and contamination. The solid is generally stored desiccated at or below -20 °C, protected from light and moisture. Stock solutions are often prepared in dimethyl sulfoxide or ethanol, then aliquoted to avoid repeated freeze–thaw cycles. Aqueous solubility is low, so formulations for animal studies may require cosolvents or suspending agents. Personnel should follow institutional chemical safety procedures, because toxicological data for humans are incomplete.
The MEROPS protease database includes the following ten families of asparagine peptide lyases, which are included in 6 different clans of proteases. Proteolytic enzymes are classified into families based on sequence similarity. Each family includes proteolytic enzymes with homologous sequences and common catalytic type. Clans are groups of proteolytic enzymes families with related structures, where catalytic type is not conserved. *Not yet included in IUBMB recommendations. The ten different families of asparagine peptide lyases are distributed in three different types: Viral coat proteins Autotransporter proteins Intein-containing proteins There are five families of viral coat proteins (N1, N2, N8, N7 and N5), two families of autotransporter proteins (N6 and N4) and three families of intein-containing proteins (N9, N10 and N11).
Two additional amino acids are in some species coded for by codons that are usually interpreted as stop codons: In addition to the specific amino acid codes, placeholders are used in cases where chemical or crystallographic analysis of a peptide or protein cannot conclusively determine the identity of a residue. They are also used to summarize conserved protein sequence motifs. The use of single letters to indicate sets of similar residues is similar to the use of abbreviation codes for degenerate bases.
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC, EDAC or EDCI) is a water-soluble carbodiimide usually handled as the hydrochloride, which is a white solid. It is typically employed in the 4.0-6.0 pH range. It is generally used as a carboxyl activating agent for the coupling of primary amines to yield amide bonds. While other carbodiimides like dicyclohexylcarbodiimide (DCC) or diisopropylcarbodiimide (DIC) are also employed for this purpose, EDC has the advantage that the urea byproduct formed (often challenging to remove in the case of DCC or DIC) can be washed away from the amide product using dilute acid. Additionally, EDC can also be used to activate phosphate groups in order to form phosphomonoesters and phosphodiesters. Common uses for this carbodiimide include peptide synthesis, protein crosslinking to nucleic acids, but also in the preparation of immunoconjugates. EDC is often used in combination with N-hydroxysuccinimide (NHS) for the immobilisation of large biomolecules. Recent work has also used EDC to assess the structure state of uracil nucleobases in RNA.
Archives of Biochemistry and Biophysics is a biweekly peer-reviewed scientific journal that covers research in biochemistry and biophysics. It is published by Elsevier. As of 2012, the editors-in-chief were Paul Fitzpatrick (University of Texas Health Science Center at San Antonio), Helmut Sies (University of Düsseldorf), Jian-Ping Jin (Wayne State University School of Medicine), and Henry Jay Forman (University of Southern California). The journal was established in 1942 by Academic Press as the Archives of Biochemistry, obtaining its current name in 1952. It absorbed the journal Molecular Cell Biology Research Communications (formerly section B of Biochemical and Biophysical Research Communications), which was published from 1999 to 2001. An index to authors for the first 75 volumes, covering the period from 1943 to 1958, was published in October 1959.
Aside from the 22 proteinogenic amino acids, many non-proteinogenic amino acids are known. These either are not found in proteins (for example carnitine, GABA, ornithine) or are not produced directly and in isolation by standard cellular machinery. For example, hydroxyproline is synthesized from proline, and selenomethionine is produced by metabolic modification of methionine. Non-proteinogenic amino acids that are found in proteins are formed by post-translational modification. Such modifications can also determine the localization of the protein, e.g., the addition of long hydrophobic groups can cause a protein to bind to a phospholipid membrane. Examples:
Sources: en.wikipedia.org
On-line mass spectrometry was develop to solve some of the limitations and problem that develop from off-line analysis, such as evaporation and chemical reactions of particles in the filters during long analysis time. On-line Mass spectrometry solves these problems through the collection and analysis of aerosol particles in real time. On-line instruments are very portable and allow for spatial variability to be examined. These portable instruments can be put on many different platforms such as boats, planes, and mobile platforms (e.g. car trailers). An example of this is in the picture at the beginning with the instrumentation attached to an aircraft. Like off-line, on-line mass spectrometry has many different type of instruments, which can be broken up into two types; instruments that measures the chemistry of the particle ensemble (bulk measurement) and those that measure the chemistry of individual particles (single-particle measurement). Thus based on analytical need different instrumentation is used in analysis of the aerosol particles.
Microscale manipulation and patterning of biological materials such as proteins, cells and tissues have been used in the development of cell-based arrays, microarrays, microfabrication based tissue engineering, and artificial organs. Biological micropatterning can be used for high-throughput single cell analysis, precise control of cellular microenvironment, as well as controlled integration of cells into appropriate multi-cellular architectures to recapitulate in vivo conditions. Photolithography, microcontact printing, selective microfluidic delivery, and self-assembled monolayers are some methods used to pattern biological molecules onto surfaces. Cell micropatterning can be done using microcontact patterning of extracellular matrix proteins, cellular electrophoresis, optical tweezer arrays, dielectrophoresis, and electrochemically active surfaces.
As of 2026, there is no cure or effective treatment for CJD. Some of the symptoms, like twitching, can be managed, but otherwise treatment is palliative care. Psychiatric symptoms like anxiety and depression can be treated with sedatives and antidepressants. Myoclonic jerks can be handled with clonazepam or sodium valproate. Opiates can help with pain. Seizures are very uncommon but can nevertheless be treated with antiepileptic drugs. In 2022, results of an early-stage trial of PRN100, a monoclonal antibody against PrP, were reported: the drug appeared safe and reached the brain, but treated patients did not show clearly improved survival compared to historical controls. While not curative, this trial demonstrated the feasibility of immunotherapy for prion disease. In 2025, preclinical research demonstrated that oral, low-dose treatment with the antiretroviral medication efavirenz extended survival and slowed disease progression in a humanized mouse model of sporadic CJD (sCJD). The drug acts as an allosteric activator of the brain-specific cholesterol-metabolizing enzyme CYP46A1. This mechanism promotes brain cholesterol turnover, reduces the neurotoxic accumulation of pathological prion proteins (PrPSc), and alleviates metabolic lipid alterations in the brain.
Ansuvimab is a monoclonal antibody therapy that is infused intravenously into people with Ebola virus disease. Ansuvimab is a neutralizing antibody, meaning it binds to a protein on the surface of Ebola virus that is required to infect cells. Specifically, ansuvimab neutralizes infection by binding to a region of the Ebola virus envelope glycoprotein that, in the absence of ansuvimab, would interact with virus's cell receptor protein, Niemann-Pick C1 (NPC1). This "competition" by ansuvimab prevents Ebola virus from binding to NPC1 and "neutralizes" the virus's ability to infect the targeted cell.
In molecular biology, ATP10 protein (mitochondrial ATPase complex subunit ATP10) is an ATP synthase assembly factor. It is essential for the assembly of the mitochondrial F1-F0 complex. A yeast nuclear gene (ATP10) encodes a product that is essential for the assembly of a functional mitochondrial ATPase complex. Mutations in ATP10 induce a loss of rutamycin sensitivity in the mitochondrial ATPase, but do not affect the respiratory enzymes. ATP10 has a molecular weight of 30,293 Da and its primary structure is not related to any known subunit of the yeast or mammalian mitochondrial ATPase complexes. ATP10 is associated with the mitochondrial membrane. It is suggested that the ATP10 product is not a subunit of the ATPase complex but rather a protein required for the assembly of the F0 sector of the complex.
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.
Liquid chromatography with mass spectrometry is a common approach. Ultraviolet detection and nuclear magnetic resonance can support identification when suitable standards are available.