Everything below concerns research chemical. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Updated 2025-09-09. Numbers and descriptions here follow the published literature rather than marketing material.
Analytical identification of SR9009 typically relies on liquid chromatography coupled with tandem mass spectrometry. In biological samples, researchers first separate the compound from matrix components using protein precipitation, liquid-liquid extraction, or solid-phase extraction. High-performance liquid chromatography with ultraviolet detection and nuclear magnetic resonance spectroscopy can support structural confirmation of reference materials. Because SR9009 is a small, relatively lipophilic molecule, reverse-phase columns and acidic mobile phases are common. Laboratories often include isotope-labeled internal standards to improve quantification and to correct for ion suppression.
Stability depends on physical form, temperature, light exposure, and solvent. Solid SR9009 is generally stored cold and dry, with protection from light to limit degradation. Dimethyl sulfoxide stocks are common for laboratory work, but repeated freeze-thaw cycles can reduce compound integrity. Aqueous solutions may be less stable than organic stocks, and the ethyl ester in the structure can be susceptible to hydrolysis under certain conditions. Researchers typically validate storage conditions and recheck purity before quantitative experiments, especially when using archived material.
At the molecular level, SR9009 binds the ligand-binding domain of REV-ERB and strengthens recruitment of corepressor proteins such as NCoR and HDAC3. This increases repression of target genes, including Bmal1 and other clock-controlled and metabolic genes. In rodent studies, such changes have been linked to altered lipid handling, glucose metabolism, and energy expenditure. The precise chain of events between receptor binding and whole-body effects remains an active area of research. Findings in animals do not automatically translate to humans.
Laboratory studies often administer SR9009 by injection because oral absorption appears poor in rodents. Reported pharmacokinetic properties include rapid metabolism and low systemic exposure after oral dosing. Human pharmacokinetic data are sparse, so absorption, distribution, metabolism, and excretion in people are not well defined. Some research explores related REV-ERB compounds with improved drug-like properties. Regulatory approval for any REV-ERB agonist as a human medicine has not been granted to date.
SR9009 is a synthetic small molecule studied as an agonist of the nuclear receptors REV-ERBα and REV-ERBβ, also called NR1D1 and NR1D2. These receptors help regulate circadian rhythms and metabolic gene programs. The compound was developed for laboratory research, not as an approved therapeutic. Its identity is distinct from steroid hormones and selective androgen receptor modulators. Scientific interest centers on how REV-ERB activation changes gene expression in cells and animal models.
| Property | Value | Notes |
|---|---|---|
| Common synonyms | SR9009; Stenabolic | Nickname is not a chemical name. |
| Typical analytical method | LC-MS/MS | Often with isotope-labeled internal standard. |
| Storage temperature | -20 °C | Desiccated and protected from light. |
| Solution stability | DMSO stock; avoid freeze-thaw | Store at -20 to -80 °C. |
| Regulatory status | Not approved; varies by country | May be restricted as research chemical. |
Identity and purity testing for SR9009 commonly uses liquid chromatography coupled with tandem mass spectrometry. This method separates the compound from matrix components and detects it by mass-to-charge transitions, providing sensitive and specific confirmation. Nuclear magnetic resonance spectroscopy can support structural identification, while high-performance liquid chromatography with ultraviolet detection may estimate purity. Because online products labeled as SR9009 may contain other substances or no active compound at all, independent verification is important in research settings. Certificates of analysis are useful but not a substitute for in-house testing.
Laboratory samples of SR9009 are typically supplied as a white to off-white powder. The compound dissolves readily in organic solvents such as dimethyl sulfoxide and ethanol, while its solubility in water is low. Because of this solubility profile, researchers often prepare concentrated stock solutions in an organic solvent before diluting them into aqueous assay buffers. Light exposure, moisture, and repeated freeze-thaw cycles can degrade many small molecules, so handling procedures usually aim to minimize these factors. Purity is commonly checked before use.
Storage conditions for research-grade SR9009 generally involve a freezer at approximately minus twenty degrees Celsius, sometimes lower for long-term preservation. Containers should remain tightly closed and protected from light. Desiccants may be used to limit moisture uptake. Solutions are often stored in aliquots to avoid repeated warming and cooling. Stability data for the compound under various conditions are limited, so laboratories typically follow supplier recommendations and verify performance through periodic analytical checks rather than assuming indefinite stability.
Subfamily ABCC contains thirteen members and nine of these transporters are referred to as the Multidrug Resistance Proteins (MRPs). The MRP proteins are found throughout nature and they mediate many important functions. They are known to be involved in ion transport, toxin secretion, and signal transduction. Of the nine MRP proteins, four of them, MRP4, 5, 8, 9, (ABCC4, 5, 11, and 12), have a typical ABC structure with four domains, comprising two membrane spanning domains, with each spanning domain followed by a nucleotide binding domain. These are referred to as short MRPs. The remaining 5 MRP's (MRP1, 2, 6, 7) (ABCC1, 2, 3, 6 and 10) are known as long MRPs and feature an additional fifth domain at their N terminus. CFTR, the transporter involved in the disease cystic fibrosis, is also considered part of this subfamily. Cystic fibrosis occurs upon mutation and loss of function of CFTR. The sulfonylurea receptors (SUR), involved in insulin secretion, neuronal function, and muscle function, are also part of this family of proteins. Mutations in SUR proteins are a potential cause of Neonatal diabetes mellitus. SUR is also the binding site for drugs such as sulfonylureas and potassium-channel openers activators such as diazoxide.
The Department was founded in 1934 in Kazan Teachers’ Institute to educate future teachers of chemistry. In November, 2011 the Department of Chemical Education became a structural unit of A. M. Butlerov Institute of Chemistry of Kazan (Volga Region) Federal University. Educational research was combined with fundamental and applied research in chemistry. International, All-Russian and regional research-to-practice conferences on chemical education organized by the Department are of the utmost interest. The Department has received letters of gratitude from school principals for instructing students in research and methodology in their preparation for teaching practice. Today 3 Doctors of Science and 5 Doctors of Philosophy are involved in the educational and bringing-up process at the Department. Since 2010 teachers have been retrained in the field of “Teacher of Chemistry”.The head of the Department is Suria I. Gilmanshina, Doctor of Philosophy in Chemistry, Doctor of Science in Education. The Department conducts research in the following fields:
HA (aq) + H2O (l) ⇌ H3O+ (aq) + A− (aq) Ka Common examples of monoprotic acids in mineral acids include hydrochloric acid (HCl) and nitric acid (HNO3). On the other hand, for organic acids the term mainly indicates the presence of one carboxylic acid group and sometimes these acids are known as monocarboxylic acid. Examples in organic acids include formic acid (HCOOH), acetic acid (CH3COOH) and benzoic acid (C6H5COOH). Polyprotic acids, also known as polybasic acids, are able to donate more than one proton per acid molecule, in contrast to monoprotic acids that only donate one proton per molecule. Specific types of polyprotic acids have more specific names, such as diprotic (or dibasic) acid (two potential protons to donate), and triprotic (or tribasic) acid (three potential protons to donate). Some macromolecules such as proteins and nucleic acids can have a very large number of acidic protons. A diprotic acid (here symbolized by H2A) can undergo one or two dissociations depending on the pH. Each dissociation has its own dissociation constant, Ka1 and Ka2.
ProIAPP consists of 67 amino acids, which follow a 22 amino acid signal peptide which is rapidly cleaved after translation of the 89 amino acid coding sequence. The human sequence (from N-terminus to C-terminus) is: (MGILKLQVFLIVLSVALNHLKA) TPIESHQVEKR^ KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYG^ KR^ NAVEVLKREPLNYLPL. The signal peptide is removed during translation of the protein and transport into the endoplasmic reticulum. Once inside the endoplasmic reticulum, a disulfide bond is formed between cysteine residues numbers 2 and 7. Later in the secretory pathway, the precursor undergoes additional proteolysis and posttranslational modification (indicated by ^). 11 amino acids are removed from the N-terminus by the enzyme proprotein convertase 2 (PC2) while 16 are removed from the C-terminus of the proIAPP molecule by proprotein convertase 1/3 (PC1/3). At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues. The terminal glycine amino acid that results from this cleavage allows the enzyme peptidylglycine alpha-amidating monooxygenase (PAM) to convert the terminal glycine to an amine group (releasing glycolate). After this step, the transformation from the precursor protein proIAPP to the biologically active IAPP (amylin) is complete (IAPP sequence: KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH2).
Sources: en.wikipedia.org
Enzymes incur catalysis by binding more strongly to transition states than substrates and products. At the catalytic binding site, several different interactions may act upon the substrate. These range from electric catalysis, acid and base catalysis, covalent catalysis, and metal ion catalysis. These interactions decrease the activation energy of a chemical reaction by providing favorable interactions to stabilize the high energy molecule. Enzyme binding allows for closer proximity and exclusion of substances irrelevant to the reaction. Side reactions are also discouraged by this specific binding. Types of enzymes that can perform these actions include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. For instance, the transferase hexokinase catalyzes the phosphorylation of glucose to make glucose-6-phosphate. Active site residues of hexokinase allow for stabilization of the glucose molecule in the active site and spur the onset of an alternative pathway of favorable interactions, decreasing the activation energy.
The bacterial outer membrane is found in gram-negative bacteria. Gram-negative bacteria form two lipid bilayers in their cell envelopes - an inner membrane (IM) that encapsulates the cytoplasm, and an outer membrane (OM) that encapsulates the periplasm. The composition of the outer membrane is distinct from that of the inner cytoplasmic cell membrane - among other things, the outer leaflet of the outer membrane of many gram-negative bacteria includes a complex lipopolysaccharide whose lipid portion acts as an endotoxin - and in some bacteria such as E. coli it is linked to the cell's peptidoglycan by Braun's lipoprotein. Porins can be found in this layer.
As there are two carbon atoms available for substitution, β-amino acids have four sites (chirality included; as opposed to two in α-amino acids) for attaching the organic residue group. Accordingly, two main types β-amino acids exist differing by which carbon the residue is attached to: ones with the organic residue (R) next to the amine are called β3 and those with position next to the carbonyl group are called β2. A β-peptide can consist of only one kind of these amino acids (β2-peptides and β3-peptides), or have a combination of the two. Furthermore, a β-amino acid can form a ring using both of its sites and also be incorporated into a peptide. β-Amino acids have been prepared by many routes, including some based on the Arndt-Eistert synthesis.
No chromosome translocations, chimeric genes, or fusion proteins have been described in BIA-ALCL although the neoplastic cells in the disease have been described to have gene copy number variations involving gains in gene copies on the p arm of chromosome 19 and losses of gene copies in the p arms of chromosome 10 and 1. The neoplastic cells in BIA-ALCL show mutations of the STAT3 gene in 64% of cases and reports of mutations in JAK1, JAK3, DNMT3A, and TP53 genes. The development of BIA-ALCL, it has often been suggested, may be at least in part a T-cell-induced, inflammation-driven cancer response to the implant.
Reactions of acids are often generalized in the form HA ⇌ H+ + A−, where HA represents the acid and A− is the conjugate base. This reaction is referred to as protolysis. The protonated form (HA) of an acid is also sometimes referred to as the free acid. Acid–base conjugate pairs differ by one proton, and can be interconverted by the addition or removal of a proton (protonation and deprotonation, respectively). The acid can be the charged species and the conjugate base can be neutral in which case the generalized reaction scheme could be written as HA+ ⇌ H+ + A. In solution there exists an equilibrium between the acid and its conjugate base. The equilibrium constant K is an expression of the equilibrium concentrations of the molecules or the ions in solution. Brackets indicate concentration, such that [H2O] means the concentration of H2O. The acid dissociation constant Ka is generally used in the context of acid–base reactions. The numerical value of Ka is equal to the product (multiplication) of the concentrations of the products divided by the concentration of the reactants, where the reactant is the acid (HA) and the products are the conjugate base and H+.
Sources: en.wikipedia.org
The most common approach is liquid chromatography-tandem mass spectrometry, often after extraction from blood, urine, or tissue. Ultraviolet detection and nuclear magnetic resonance spectroscopy are used mainly for reference material characterization. Isotope-labeled internal standards improve accuracy.
Solid material is usually kept at -20 °C, desiccated, and protected from light. Dimethyl sulfoxide stocks should be stored cold and subjected to minimal freeze-thaw cycles. Aqueous solutions are generally less stable and should be prepared fresh when possible.
Legality depends on the country and the intended use. It is not an approved medicine, and some places restrict or ban sales for human consumption. Buyers should verify local rules and product documentation before procurement.
SR9009 is a synthetic research compound that activates the REV-ERBα and REV-ERBβ nuclear receptors. It is not an approved drug and has no established human therapeutic use. Most published biological data come from cell and rodent studies.