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3β-Hydroxysteroid Dehydrogenase (3β-HSD) caught the attention of biochemists in the mid-20th century, back when unlocking the steps of steroid biosynthesis felt something like finding new continents. This enzyme didn’t take the limelight in big, bold headlines, but plenty of groundbreaking hormonal research would have crumbled without it. As teams mapped out metabolic pathways, 3β-HSD surfaced time and again—turns out, it converts pregnenolone to progesterone and DHEA to androstenedione. It’s the gatekeeper for moving steroids between chemical classes. Whether the research was happening in academic labs or hospitals tracking congenital adrenal hyperplasia, those who dug into hormone metabolism constantly ran into 3β-HSD and its many isoforms through tissue studies and clever enzyme assays. With genomics and cloning, new waves of research cracked open the genes behind the enzyme, leading to the understanding that mutations throw steroid production out of balance and create real-world health problems.
Wherever people still study steroid hormones, 3β-HSD gets respect. In pure form it’s a workhorse enzyme for researchers probing biosynthetic steps, drug developers looking for enzyme inhibitors, and diagnostics companies checking hormone imbalances. The protein comes in several isoforms in humans, each with its role—there’s Type I in peripheral tissues for things like skin, and Type II in adrenal glands and gonads. If someone tests enzyme activity in a tube, color changes linked to NAD+ or NADH often reveal its conversion process. The biochemical influence of 3β-HSD stretches from the development of new therapies for hormone-sensitive diseases to better understanding of stress, reproduction, and metabolic health. Unlike some curiosity compounds, it keeps proving its worth across areas that really matter: endocrinology, oncology, reproductive science, psychiatry.
In the lab, 3β-HSD isn’t flashy or dramatic. Its behavior tracks with a typical globular protein, generally showing stability in pH ranges similar to that of most mammalian physiological processes. Researchers usually describe its molecular mass in the ballpark of 42–45 kDa per subunit, and it often operates as a dimer. Solubility comes down to how the enzyme was purified—proteins from bacterial overexpression might need a little co-solvent, while those isolated from mammalian cells can often go straight into buffered saline. Its activity peaks around human body temperature. Used in tubes, its action depends on the right presence of cofactors, like NAD+ or NADH, and researchers always keep an eye on their buffer salt concentrations, since subtle shifts can slow catalytic speed or even denature the protein.
Labs sourcing 3β-HSD are wise to scrutinize enzyme activity per mg of protein, expressed in international units (often measured by steroid conversion per minute at 37°C). Protein integrity needs proof, usually by SDS-PAGE. Specificity and purity mean everything: cross-contamination by related dehydrogenases can send research off the rails. Documentation usually lists contaminating activities at less than 1% and often tags for expression source, since bacterial, yeast, and mammalian versions show subtle behavior differences. Some researchers want the recombinant version from E. coli; others push for mammalian cell expression to keep post-translational modifications intact, making all the difference in experiments mimicking what happens in the body.
Reliable enzyme supply doesn’t just fall from the sky. Cloning the gene into expression vectors marked a turning point—it let scientists produce 3β-HSD in E. coli, yeast, or CHO cells by the milligram, instead of struggling to isolate tiny amounts from animal tissue. But purification isn’t simple; the enzyme can denature if rushed or exposed to harsh chemicals. Most trusted protocols rely on affinity chromatography and careful buffer exchanges. Some researchers still use traditional isolation from animal tissues, which sometimes preserves subtle nuances lost in recombinant methods. Still, chromosomal manipulation and improved cell factories opened new discovery doors, all thanks to smarter prep methods. Every detail shapes the enzyme’s function in a real-world assay: how long it lasts, how it folds, how the active site reacts to tiny structural changes in nearby molecules.
Experimenting with 3β-HSD goes beyond just watching it push pregnenolone or DHEA along the metabolic cascade. Chemists use site-directed mutagenesis to tweak active site residues, mapping out which amino acids drive specificity and catalytic speed. Some researchers modify cysteines to study how redox states influence activity. Enzyme inhibitors, both natural and synthetic, let people dissect reaction pathways. In disease models, researchers sometimes introduce point mutations—either to mimic inherited conditions or to block the enzyme and observe downstream hormone changes. Common lab reactions tap into 3β-HSD’s strict requirement for the 3β-hydroxysteroid substrate structure; shifting a hydroxyl to a different position or tweaking the steroid backbone often cuts the enzyme’s catalytic efficiency to nearly nothing, a fact that shapes drug design and basic research alike.
Those who navigate research papers on steroids quickly learn to track a handful of names for 3β-HSD. The literature also calls it 3β-hydroxysteroid oxidoreductase, occasionally just “3β-OH dehydrogenase,” with numerical gene designations like HSD3B1 or HSD3B2 for the different isoforms. International enzyme commission numbers help textbook readers (EC 1.1.1.145), though in the heat of research, people stick to shorthand names. Whether mentioned in lab notebooks, regulatory filings, or clinical texts, the synonyms boil down to the same crucial actor, even if the terminology keeps shifting as research moves from benchtop to bedside.
Using 3β-HSD in a lab environment doesn’t mean bracing for daily hazards, but there’s no room for being casual. Researchers keep solutions chilled and avoid repeated freeze-thaw cycles, since the active enzyme gets knocked out quickly if treated carelessly. All work happens in standard protective gear—lab coats, gloves, eye shields—since any biological preparation can pose infection risks, especially if cell lines or animal tissue entered the supply chain. Enzymes prepared by recombinant tech or animal sources carry the faint but serious risk of allergenic reactions, so anyone with a history of allergies around protein powders pays attention. Spills cleaned with detergent and bleach, not just wiped away. Long-term, proper labeling prevents mix-ups; one wrong tube can waste months of research. Disposal of unused enzyme follows institutional rules for protein waste, with the assumption that nobody wants stray steroid-modifying activity floating around.
3β-HSD earned its spots in applications that cross department and industry lines. Clinical labs rely on knowledge of this enzyme for diagnosing rare genetic disorders and evaluating hormone imbalances. Drug companies have a sharp eye on its role in conditions like prostate cancer, endometriosis, or adrenal disorders—either as a target or as a pathway checkpoint for experimental compounds. In animal science, researchers use its measurement to assess reproductive health or stress responses. These bridges between lab, clinic, and animal medicine reflect how much society depends on precise steroid chemistry, whether people notice it or not. In academic settings, students measure its activity as a rite of passage in biochemistry courses, often tying their results back to living systems where hormonal balance determines everything from mood to growth.
Despite decades of work, 3β-HSD research still throws out surprises. Genomic studies show how certain gene variants can predispose some people to adrenal or gonadal dysfunctions, and labs keep identifying subtle post-translational modifications that tune activity up or down. High-throughput drug screening has found plenty of molecules that dampen its activity, setting the stage for new cancer and metabolic disease drugs that block hormone production at the right moment. Scientists race to unravel allosteric regulators, natural inhibitors, and unknown cofactors that might expand the enzyme’s clinical impact. Investment in recombinant technologies means more researchers can dig into structure–function relationships with better reproducibility. Each stride promises better disease models, sharper diagnostics, or smarter therapies that tune hormonal output with surgical precision.
Some might think studying enzyme toxicity only matters for big pharmaceutical players, but everyday environmental exposures make this a front-burner issue for public health. Inhibitors or environmental disruptors that block 3β-HSD can unbalance everything from cortisol to testosterone, opening doors to developmental disorders or metabolic problems. Animal research points to the risks of certain endocrine disruptors in water supplies that alter 3β-HSD function, and investigators look for safe thresholds so regulators can step in when exposures spike. At the same time, therapeutic inhibitors face the challenge of being selective: block too much 3β-HSD, and downstream hormonal chaos spills into the real world. Careful work in cell lines, animal models, and clinical trials aims to balance enzyme blocking with maintaining a healthy hormonal baseline.
The horizon for 3β-HSD research keeps advancing. Interest grows in gene therapy or small RNA approaches that shift enzyme expression to fix genetic bottlenecks. The possibility of personalizing therapies based on someone’s HSD3B1 or HSD3B2 genotype is no longer just wishful thinking—it’s a fast-approaching reality as whole-genome sequencing moves into the clinic. Drug screens keep expanding as artificial intelligence models predict next-generation inhibitors with better selectivity. Stem cell applications reach for tissue-specific modulation of 3β-HSD to create better models for hormone-dependent cancers or congenital diseases. Environmental health studies raise new red flags, warning of unknown disruptors that threaten the balance so many people take for granted. For researchers, physicians, and anyone relying on optimal hormonal health, the story of 3β-HSD hasn’t crested yet; more chapters are coming, and its legacy keeps shaping science, medicine, and daily life in ways that feel invisible until things go wrong.
In the world of biology and medicine, enzymes rarely get their moment in the spotlight. Still, 3β-Hydroxysteroid Dehydrogenase (3β-HSD) carries weight in understanding how the body works. This enzyme plays a hands-on part in steroid hormone production. Without such enzyme, the human body would grind to a halt in many ways. I came across 3β-HSD for the first time in a medical biochemistry class, tracing hormone pathways. The complexity of what 3β-HSD manages impressed me — tiny changes with big consequences.
3β-HSD takes center stage, especially in making important hormones like cortisol, aldosterone, progesterone, testosterone, and estrogen. These hormones regulate stress response, salt and water balance, reproductive health, and even mood. The enzyme turns pregnenolone into progesterone, paving the way for many hormone conversions downstream. If 3β-HSD stalls, the entire system becomes unbalanced. Children might face issues such as ambiguous genitalia or salt-wasting crises, which could become life-threatening if not identified early. Adults often deal with fatigue, blood pressure swings, or infertility.
So why do researchers and doctors spend time tracking 3β-HSD activity? On one hand, issues in the enzyme’s action help diagnose conditions such as congenital adrenal hyperplasia (CAH). This genetic disorder changes the way adrenal glands work, leading to either not enough or too much hormone production. Clinicians often turn to specific lab tests that measure 3β-HSD activity or the hormone levels affected by it.
On another front, pharmaceutical research keeps a close eye on 3β-HSD. Blocking this enzyme, or kickstarting its function at just the right time, offers new therapies for diseases tied to steroid hormones. For example, breast and prostate cancers sometimes thrive on sex hormones, and blocking hormone production at a step involving 3β-HSD could slow tumor growth. Several studies show experimental drugs targeting 3β-HSD can lower excessive hormone production in animal models, with hopes to bring better drugs to market.
As far as clinicians, those of us in the field keep an eye on new findings related to 3β-HSD because patients sometimes present with vague symptoms — fatigue, dark skin patches, blood pressure problems — which require careful investigation. Understanding this enzyme’s faithful contribution helps sort out the causes faster. For medical students, a clear grasp of this enzyme’s steps in the hormone manufacturing line helps make sense of treatment options for CAH and certain hormone-driven cancers.
Addressing enzyme defects early helps patients live healthier lives and avoid unnecessary suffering. Pediatricians screen newborns for hormone problems tied to enzymes like 3β-HSD. Early treatment, such as hormone replacement or salt supplements, can be life-saving. Ongoing research into how to modulate 3β-HSD activity brings hope for tackling long-standing issues in endocrinology, oncology, and rare genetic conditions.
I’ve seen firsthand how detailed work at the cellular level — often overlooked — can dramatically change the bigger picture in public health and medicine. As more focus lands on precision medicine, 3β-HSD will keep finding its spot on the roster of crucial biological players.
3β-Hydroxysteroid dehydrogenase, often called HSD3B, doesn’t just help scientists in the lab—it forms the foundation for drug development, clinical diagnostics, and endocrinology research. Anybody working in these fields learns quickly that mishandling this enzyme ends in wasted money, lost time, and, even worse, unreliable results. I’ve seen labs struggle with irreproducible data, only to trace the issue back to careless enzyme storage. Treating these sensitive proteins with respect starts at the freezer.
Working with HSD3B made me rethink how little changes in temperature and environment cause big problems. Enzymes like this one break down easily with heat, humidity, or exposure to air. Most reputable sources—Sigma-Aldrich, Thermo Fisher, and research literature—agree: keeping HSD3B active depends on strict temperature control and avoiding repeated freeze-thaw cycles.
The smart choice is to store HSD3B at -20°C or below, preferably in a dedicated enzyme freezer. Ultra-low temperatures slow degradation and help preserve enzyme shape, keeping its catalytic punch for future experiments. I always portion out working aliquots in sterile, screw-cap microtubes. This step reduces the risk of contamination and stops waste—over and over, I’ve seen whole lots go bad from careless pipetting or someone trying to stretch a single vial over months.
I’ve learned not to overlook humidity. Desiccant packs or storage in a sealed container add extra protection. HSD3B’s structure can also take a hit from light. Wrapping tubes in foil or keeping them in an opaque box blocks out damaging rays. It pays to look over the technical sheet for specific warnings, but keeping things dark and dry usually pays off.
Storage is more than temperature. Stabilizing agents—often found in commercial enzyme preps—keep HSD3B safe, but freshly prepared glycerol stocks at 50% glycerol (v/v) work well for homemade enzymes. Glycerol not only stabilizes the structure but keeps things semi-liquid at -20°C, which means I can scoop out small portions without a risky thaw. Careful selection of pH and adding protective proteins like bovine serum albumin can make a world of difference. It’s easy to see why experienced researchers favor these tricks.
Sometimes people worry if their stored HSD3B still works. Running a control assay—using a known substrate and checking for activity—gives straight answers. I encourage others to label everything carefully with date and batch number. If you work in a teaching or clinical lab, training every new user on best practices lowers risks of mix-ups and accidents.
I once lost a batch simply from a freezer power blip over the weekend. Now, I use probes for temperature logging and keep backup freezers ready. Insurance against disaster can mean running duplicate stocks in separate freezers, especially for crucial projects. Every extra step I’ve built into storage protocols has paid off through better reliability and less waste.
Handling HSD3B can make or break an experiment. Respect for storage, sound aliquoting, and attention to environmental threats guarantee better, repeatable results—and less heartbreak after weeks of work. The care taken behind the scenes makes the most difference on the bench, and the small habits learned early end up saving years of frustration.
Researchers hunt for answers about steroids, cell signaling, and metabolism. One pivotal tool they use involves measuring the activity of 3β-Hydroxysteroid Dehydrogenase (3β-HSD), a key enzyme in steroid biosynthesis. Getting trustworthy data starts with dialing in the right assay protocol—something I learned the hard way during endless late nights at the lab bench.
The smallest changes in a protocol can flip results on their head. I’ve seen colleagues chase ghosts, blaming cell lines or reagents, only to realize their enzyme kinetics didn’t make sense because of sloppy assay setup. The assay for 3β-HSD hinges on tight control and honest attention to detail. False peaks or lagging rates often point back to mismatched buffers, unstable substrates, or forgettable controls. Accuracy here means we can track hormone synthesis, troubleshoot metabolic disease models, or validate drug screens without guesswork undercutting the findings.
Anyone tracing steroid biosynthesis typically starts with tissue extracts or recombinant protein. The most direct readout leverages the conversion of dehydroepiandrosterone (DHEA) to androstenedione or pregnenolone to progesterone. NAD+ is essential as a cofactor, serving as the hydrogen acceptor. In practice, I always set up parallel blanks—leaving out substrate or enzyme—to catch accidental background noise from NAD+ reduction or non-enzymatic processes. Skipping this step leads to headaches later.
I stick with a 96-well plate format for throughput, using a reaction mix of phosphate buffer (pH 7.2–7.5, typically 100 mM), with DHEA (40–100 µM) and NAD+ (500 µM or slightly less, based on pilot runs). Enzyme amounts are kept low, enough to see a steady rate but avoiding the plateau you get with substrate exhaustion. I start reactions by adding the enzyme and track NADH production spectrophotometrically at 340 nm, as the reduced cofactor absorbs light there. This readout is fast, and quantitating with kinetic data keeps results honest.
Solvent effects sneak in if someone uses too much DMSO or ethanol dissolving substrates. Even 2% DMSO has tanked my reactions before. Ambient temperature swings can double apparent rates overnight, so using a plate reader with temperature control saves headaches. I run assays at 37°C to stay close to physiological reality, and I use standard curves for NADH to translate absorbance into meaningful numbers. Several classic papers highlight the risk of artifactual activity in crude lysates—contaminating dehydrogenases easily chew up NAD+ in the absence of steroid substrate. That’s why running blanks, and occasionally heat-inactivating controls, helps flag false positives.
Taking the time to optimize the buffer, titrate cofactor and substrate, and validate with known inhibitors separates meaningful results from background chatter. Competitive inhibitors, like trilostane, belong in every validation run to confirm specificity. Reproducibility isn’t just a buzzword; I keep lab notes packed with details on batch numbers, pipetting order, and timing to track down surprises when rates suddenly drift off a known baseline. This attention to protocol keeps data credible—whether the goal is a new drug target or untangling some knot in endocrinology.
3β-HSD assays work best with a mindset that respects every reagent and variable. The optimal protocol doesn’t come from a single trial. It evolves through iteration, skepticism, and a willingness to trace each unexpected result back to the bench. A careful assay builds scientific trust, letting our answers stand up to the next challenge.
Enzyme selection rarely sounds exciting, but in a working lab with real deadlines, the wrong match blows up good science as fast as a poorly calibrated pipette. 3β-Hydroxysteroid Dehydrogenase (3β-HSD) stands out whenever steroid biosynthesis comes up. As someone who’s spent more late nights with tissue samples than friends, dodging pitfalls starts with asking if this enzyme is fit for the material you’re testing.
Think about what you’re actually working with—species, tissue, sample treatment. Most published success stories around 3β-HSD point to adrenal and gonadal tissues. That’s not a fluke. Mammalian tissue, especially from humans or rats, has enzyme levels other models just don’t match. Try mapping 3β-HSD in a microbiology sample or a plant leaf, and the signal drops so low the data looks made up. My first semester in grad school I tried it in yeast outbreaks to save money, and the results tanked. Sometimes corners don’t cut.Boom: context changes everything.
Everybody likes a quick protocol, but quick methods with rough solvents strip or denature 3β-HSD’s activity. Researchers, including ones at the NIH, have found that even a mid-level ethanol wash can wipe out most of the enzyme in the blink of an eye. I ruined promising adrenal gland lysates just by taking shortcuts to speed up the extraction. Mild buffers and keeping things at low temperature preserve what the enzyme brings to the table.So, keep cold and gentle if the enzyme matters to your data.
Matrix isn’t just a sci-fi film. Blood, urine, cell culture—each sample background has quirks. For anyone running LC-MS downstream, inhibitors floating in blood can choke 3β-HSD. I’ve watched signal drop by more than half after running whole blood versus plasma, no matter the enzyme batch. Spiking your standards directly into the test matrix, not just buffer, shows what’s going wrong before you burn through precious samples.
Don’t just grab an enzyme kit off the shelf and hope for miracles. Check if the kit or reagent’s made for human, mouse, or something wild like bovine. Kits optimized for humans, labeled with published Km and Vmax values, usually play well with common tissue samples, but start drifting from that and results skew fast. I’ve watched colleagues get thrown off by kit inserts with vague “universal” claims, only to find huge data gaps later.
Reach for literature that shares protocols matched to your sample, not just generic reviews. Lab forums and tech support chat lines from reagent providers hand out sample-specific advice, sometimes better than published protocols. Use initial sample pooling and test runs to see if you even pick up activity worth quantifying. Gathering pilot data beats trusting a PDF. If things flounder, request lots and reference kits from different suppliers.Mistakes cost samples and budgets, but trial runs save headaches.
Chasing down the right enzyme is about more than matching cas numbers. Knowing the weird quirks of your sample—tissue type, source, treatment, what the sample has chewed through before hitting your bench—drives whether 3β-Hydroxysteroid Dehydrogenase fits your needs. In my lab, sharing mistakes and test data has saved everyone time. Relying on evidence and sharing insights pushes all of us forward, no matter where the next sample comes from.
Most people outside of labs rarely think about enzymes like 3β-Hydroxysteroid Dehydrogenase. Scientists rely on this enzyme to piece together much of what we know about hormones, especially steroid biosynthesis. A lot rides on whether or not the enzyme batch is pure. Small amounts of impurities can wreck cell assays, mask real results, or send a research project down the wrong road. Labs working with human, animal, or plant tissue want an enzyme product that gives them straight answers. I’ve watched experiments hinge on whether the “purified” enzymes still hold traces of other proteins, or worse yet, no activity at all.
Most commercial suppliers report purity based on SDS-PAGE analysis, and you’ll often see a figure over 90%. For certain applications, like structural biology or pharmaceutical testing, researchers push for 95%-98% or higher. Anything less and the risks begin to stack up: rogue contaminating enzymes, degraded samples, and inconsistent batch-to-batch behavior.
People exploring the source of their 3β-Hydroxysteroid Dehydrogenase should know the story behind each bottle. The enzyme typically comes from animal tissues such as porcine or bovine adrenal glands, or from recombinant expression systems using bacteria or yeast. Original animal sources provided some of the earliest insight into how steroid hormones get produced, but animal-based enzymes bring allergen concerns and often fall short on purity. I’ve known researchers who had to drop promising projects because their batch contained unexpected animal residues or lacked the stability they needed.
Recombinant production has become the gold standard for many scientists. With gene cloning and bacterial or yeast systems, companies offer more consistent results and avoid ethical issues tied to animal harvest. Recombinant sources also lead to better batch consistency and bigger scale production, propelling many pharmaceutical and diagnostic advances. For anyone running enzyme-linked assays or developing drugs, that reliability turns into real research progress.
It takes more than glossy supplier claims to build trust around a research enzyme. I look for suppliers who show a certificate of analysis (CoA) and quality sheets listing purity, specific activity, and origin details. Real lab work relies on clear, independent data. High-performance liquid chromatography (HPLC) data, SDS-PAGE imagery, and mass spectrometry findings speak louder than marketing blurbs.
In my experience, researchers who invest time into reviewing this data set themselves up for smoother results. Teams also call suppliers and request samples for their own side-by-side comparisons. With budgets tighter than ever, no one wants to learn too late that their enzyme batch was a dud. Lab reproducibility lives and dies by these details.
Better awareness about the source and purity of 3β-Hydroxysteroid Dehydrogenase can shape smarter science. Scientists should reach out directly to suppliers, ask hard questions, and request analytical data upfront. Collaborating with providers who back up claims with transparent information builds confidence and keeps research moving in the right direction. Whether someone is optimizing an assay or scaling up for a clinical project, understanding exactly what’s in the bottle gives real peace of mind and helps sidestep costly setbacks.
| Names | |
| Preferred IUPAC name | 3β-hydroxysteroid:NAD⁺ oxidoreductase |
| Other names |
3β-HSD 3β-Hydroxy-Δ5-steroid dehydrogenase 3β-hydroxysteroid dehydrogenase/isomerase Steroid Δ5-isomerase 3-beta-hydroxysteroid dehydrogenase |
| Pronunciation | /ˈθriː ˈbeɪtə ˌhaɪdrɒksiˌstɛrɔɪd diːˌhaɪdrəˈdʒɛnˌeɪs/ |
| Identifiers | |
| CAS Number | 9021-57-4 |
| Beilstein Reference | 1812302 |
| ChEBI | CHEBI:132943 |
| ChEMBL | CHEMBL2046 |
| ChemSpider | 20570684 |
| DrugBank | DB07935 |
| ECHA InfoCard | 03e5f370-79e3-4788-9930-2b75175e6ff3 |
| EC Number | 1.1.1.145 |
| Gmelin Reference | 156639 |
| KEGG | K00003 |
| MeSH | D006713 |
| PubChem CID | 123805 |
| RTECS number | OV9253000 |
| UNII | M3I9L233G5 |
| UN number | UN1230 |
| CompTox Dashboard (EPA) | DTXSID0047402 |
| Properties | |
| Chemical formula | C27H44O2 |
| Molar mass | 34905.55 g/mol |
| Appearance | White to off-white lyophilized powder |
| Odor | Odorless |
| Solubility in water | Insoluble in water |
| log P | -0.47 |
| Basicity (pKb) | 8.50 |
| Dipole moment | 4.0 D |
| Thermochemistry | |
| Std molar entropy (S⦵298) | 260 J·mol⁻¹·K⁻¹ |
| Std enthalpy of combustion (ΔcH⦵298) | −1435 kJ/mol |
| Hazards | |
| Main hazards | May cause allergy or asthma symptoms or breathing difficulties if inhaled. |
| GHS labelling | GHS labelling: "No GHS label elements |
| Pictograms | GHS07,GHS08 |
| Signal word | Warning |
| Hazard statements | H315: Causes skin irritation. H319: Causes serious eye irritation. H335: May cause respiratory irritation. |
| Precautionary statements | P261, P280, P304+P340, P342+P311 |
| NFPA 704 (fire diamond) | NFPA 704: 1-0-0 |
| NIOSH | Not Listed |
| PEL (Permissible) | Not established |
| REL (Recommended) | 10 µg/ml |
| IDLH (Immediate danger) | Not established |
| Related compounds | |
| Related compounds |
17β-Hydroxysteroid dehydrogenase Aldo-keto reductase Cholesterol side-chain cleavage enzyme Steroid 5α-reductase Steroidogenic acute regulatory protein |
