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Carboxypeptidase B sits among those scientific workhorses that built the foundation for today’s advancements in biochemistry and medicine. Back in the 1930s and 1940s, researchers dug into animal tissues and fluids, searching for enzymes that break down proteins. Their focus was on enzymes from the pancreas, where Carboxypeptidase B burst onto the scene. Scientists observed it could snip off basic amino acids like lysine and arginine from the end of peptide chains. This specificity stood out. The enzyme soon helped scientists map out how proteins break down, opening doors in both clinical diagnostics and industrial prep. Over decades, advancements in protein purification, chromatography, and later, genetic engineering, made the enzyme widely available. Industrial-scale production grew out of demand from hospitals, labs, and production facilities, and by the late 20th century, Carboxypeptidase B appeared as a staple for both research and product manufacturing.
Today’s Carboxypeptidase B typically comes as a purified, white to off-white powder. Most suppliers source it from porcine or bovine pancreas, although recombinant versions, often expressed in microbes like E. coli, are gaining popularity. Key buyers care about homogeneity, high specific activity, and the absence of unwanted protease contaminants. Standard containers include glass vials for lab work or bulk plastic-lined drums for factories. Manufacturers provide units of activity, which refer to how much enzyme needed to liberate a micromole of L-lysine per minute at a given temperature and pH, willing buyers know that not all products labeled Carboxypeptidase B work at the same rate or purity. This difference translates straight into cost and reliability.
Carboxypeptidase B carries a molecular weight of about 34 kDa for the monomer, which combines into characteristic dimers under certain conditions. The enzyme holds up best around pH 7.6 to 8.0, finding its sweet spot at human body temperature, 37°C. At colder temps, activity drops but storage stability improves, and high heat denatures the protein, wrecking function. Structurally, Carboxypeptidase B owes much to its zinc atom, bound in the active site, necessary for hydrolytic activity. The enzyme dissolves well in most aqueous buffers but suffers rapid inactivation in acidic or highly alkaline solutions. Some users blend it with stabilizers or glycerol before freezing, keeping it viable in the long term. Loss of moisture, exposure to heavy metals, or contamination with oxidants can damage its structure, pushing users to pay attention during handling and storage.
Manufacturers spell out Carboxypeptidase B’s technical specs with details that go well beyond basic activity. Labels typically report enzyme units per milligram, buffer composition, protein content, absence of trypsin and chymotrypsin, and heavy metal contamination. Regulatory compliance means products carry lot numbers, expiry dates, and storage instructions. Some suppliers go the extra mile with certificates of analysis, offering batch records and amino acid sequence verification. Lyophilized powder or liquid forms remain standard, each bringing trade-offs in ease of use and shelf life. For regulated spaces, users demand compliance with codes like USP, EP, or JP, depending on target markets. This level of detail lets buyers compare product options, but also introduces complexity that calls for careful recordkeeping.
The classic path to Carboxypeptidase B starts with porcine or bovine pancreas, minced and homogenized in chilled acidic buffer to halt other proteases. Next, salt fractions proteins, picking off unwanted enzymes. Column chromatography follows, with ion-exchange and gel filtration steps singling out Carboxypeptidase B. Modern recombinant methods sidestep animal products, instead inserting the gene for Carboxypeptidase B into bacteria or yeast. Harvested cells get lysed, and affinity or nickel columns pluck out the enzyme. These systems reduce risk of contaminating animal viruses or prions, a persistent worry in pharma-grade products. Once in hand, the enzyme undergoes desalting, sterilization, and lyophilization. This journey from tissue or bioreactor to final product calls for careful monitoring. Each tweak, from buffer to column, influences yield and quality, shaping how different lots behave in end use.
Carboxypeptidase B operates as a metalloenzyme, using its zinc-binding site to coordinate with substrates and catalyze hydrolysis at the peptide’s C-terminal. Active against basic residues, it shows almost no action on aromatic or aliphatic amino acids. Some researchers push for chemical modification—PEGylating the enzyme for better stability, tagging it with fluorescent labels for kinetics studies, or immobilizing it on solid supports. Each modification can influence the structure, raising or lowering activity, or tweaking substrate preferences. Under industrial conditions, Carboxypeptidase B handles repetitive cycles of hydrolysis and washing. Careful control of reaction time, temperature, and substrate load prevents loss of control and ensures consistent cleavage patterns, especially in applications where incomplete digestion risks product failure.
Across decades, Carboxypeptidase B picked up names like pancreatic carboxypeptidase B, peptidyl-L-lysine carboxypeptidase, and EC 3.4.17.2. Commercial names sometimes reflect the animal source or brand, like Pancreatic B (Sigma), Carboxypeptidase B bovine (Calbiochem), or Protease B (Roche). Scientific communities prefer either the standard name or the E.C. designation for clarity, while regulatory paperwork relies on precise taxonomy and batch information. In multinational settings, translation pushes variant nomenclature even further, but most researchers stick with Carboxypeptidase B, given its place in the literature. With so many product names on the market, researchers must double-check activity and purity data before swapping brands, as not every Carboxypeptidase B matches in performance.
Using Carboxypeptidase B doesn’t require the same handling as hazardous chemicals, but strict protocol keeps operators and products safe. Standard precautions include gloves, goggles, lab coats, and procedures to prevent breathing in powders during weighing or formulation. For industrial handlers, dust extraction and HEPA filtration keep the workspace free from enzyme dust, which can trigger allergies or respiratory issues over time. Regulatory agencies in the US, Europe, and Asia require that users record incident exposures, maintain SDS data onsite, and document employee training. Clean-up and disposal protocols seek to contain biological material and keep enzymes out of general waste streams, especially for recombinant material or lots intended for injection or clinical use. Workspaces with proper airflow, refrigeration, and restricted access make sure contamination or product degradation doesn’t creep in. Over years of working with enzyme powders, most operators see where slips in hygiene or recordkeeping cause recalls or batch losses. Best practices, built up through tough lessons, lock in operational safety and consistent outcomes.
Carboxypeptidase B finds heavy use across medical research, diagnostics, protein sequencing, and industrial biotechnology. In my own lab, we relied on it to sequence peptide hormones and clean up protein mixtures, trimming unwanted basic amino acids from synthetic peptides. Diagnostic labs utilize it to differentiate disease-linked peptides, given its reliable specificity. In manufacturing, Carboxypeptidase B finishes off biopharmaceutical intermediates or cleans up fusion proteins before formulation. In food and beverage spaces, careful use of the enzyme tweaks protein hydrolysates for special nutritional products. Schools and small labs use smaller aliquots for student projects in protein chemistry, highlighting real-world enzyme use for trainees. Industrial operations, aiming for tons of output, scale up to drums of powder, wiring in automated dosing and closed-system recovery. Each setting brings unique challenges—cost, uptime, batch-to-batch reproducibility—and the right preparation and storage methods improve performance over the long run.
Big strides in enzyme engineering and molecular biology redefined Carboxypeptidase B’s future. Labs now look for ways to customize substrate scope or boost resistance to temperature and pH extremes. Directed evolution and site-directed mutagenesis, tools that only hit full stride in the last two decades, led to variants that shrug off denaturants or operate over bigger temperature ranges. Researchers chase these changes for applications where everyday Carboxypeptidase B stalls. Academic labs report hundreds of new structures or modifications, much of it cataloged in international protein databases. Funding cycles prioritize projects that link enzyme work to medical diagnostics or treatments, keeping demand for new Carboxypeptidase B variants high. From my experience, teams willing to bridge synthetic biology, protein chemistry, and analytics make the fastest progress. Collaboration between disciplines beats isolated work every time. Some companies now license proprietary versions, locking down novel performance or targeting niche needs, a move that complicates purchasing decisions but drives steady innovation.
No evidence points to acute toxicity from Carboxypeptidase B under typical lab or industrial use. Most risks involve inhalation of dust or powder, which can prompt immune responses—mainly mild allergy symptoms or, rarely, occupational asthma in repeat-exposed workers. Animal safety studies, often required before new products get approved for medical use, show rapid digestion and clearance upon ingestion. This aligns with the enzyme’s status as a natural part of many animal foods and the human digestive tract. Some caution stays appropriate, since using large batches in poorly ventilated areas can drive up risk unintentionally. Chronic exposure, especially among workers not provided with PPE, can undermine safety. Regulators keep tabs through periodic reviews, and several companies fund updated toxicity studies as enzyme modifications introduce new variables. My own view is that daily vigilance, rather than raw data, drives real-world safety; good habits protect both workers and products much more reliably than quarterly audits alone.
Carboxypeptidase B’s role in both research and industry keeps shifting as new markets and scientific ambitions emerge. Synthetic biology teams look to tweak the enzyme’s active site, boosting its use in bioprocessing, pharma, or diagnostics. Companies pushing sustainable manufacturing see promise in enzymes that replace harsh chemicals, reducing waste and energy consumption. Diagnostic companies seek custom variants tuned to break down target proteins linked to disease markers, sharpening both speed and accuracy. As gene therapy and personalized medicine advance, better enzymes for protein modification and sequence analysis grow even more important. Regulatory demands for traceability and recombinant sourcing push producers to adopt safer, animal-free manufacturers. Advances in AI and computational biology are speeding up design cycles and reducing the guesswork in enzyme optimization. New global health challenges, shifts in market structure, and the drive for green chemistry guarantee that Carboxypeptidase B holds continued value, not as a relic, but as an evolving tool meeting the challenges of tomorrow’s science and industry.
Carboxypeptidase B slices the building blocks of proteins, specifically chopping off basic amino acids like lysine and arginine from the ends. In the body, the pancreas makes it to help finish off protein digestion. In the lab, people use it as a tool to break down proteins into tinier bits. That might sound simple, but the impact stretches into medicine, food science, and research.
Scientists who study proteins and how they work in cells lean on Carboxypeptidase B all the time. The enzyme lets a researcher trim proteins at those specific spots, revealing more about their structure. In my college days, I remember sitting in a biochemistry lab, watching a professor show how the enzyme helped map out a protein’s sequence. That hands-on moment hammered home how much easier analysis becomes with the right tool. Companies like Sigma-Aldrich and Thermo Fisher sell lab-grade Carboxypeptidase B by the bottle to help drive this type of discovery. Proteomics labs couldn’t function without reliable ways to break proteins into predictable pieces, and this enzyme provides just that.
Another big use pops up in healthcare—from emergency rooms to research clinics. Doctors track a protein fragment called C3a, which pops up in the immune response. Carboxypeptidase B can “clean up” C3a in blood samples, turning it into a less active form, C3a-desArg. Why care about this? Pathologists reading blood panels look at these fragments to help spot immune system problems or inflammation. My neighbor is a lab technician at a children’s hospital, and she explained how critical this process is when physicians want to understand allergic reactions or autoimmune disease flares.
Food manufacturers use Carboxypeptidase B to fine-tune ingredients and manage allergens. By treating protein-rich ingredients, food scientists reduce the allergy risk in formulas like infant milk powder. Whey protein, for instance, can be tough for babies with milk allergies. Companies treat it with Carboxypeptidase B so it loses trigger sites for allergy reactions. I once spoke to a food safety consultant who walked me through the process. He pointed out that using the right enzyme at just the right stage prevents many emergency room visits for families dealing with allergies.
The enzyme keeps popping up in discussions about future therapy. Researchers think Carboxypeptidase B might help limit the side effects of clot-busting drugs after heart attacks or strokes, because it can reduce over-active proteins driving inflammation. The research is early, but clinical trials are on the table. Funding into using the enzyme for managing hereditary angioedema (a rare immune disorder) shows promise, as it can knock down swelling in attacks.
Wider use of Carboxypeptidase B depends on reliable supply and safe handling. There’s always the risk of contamination if the enzyme gets into the wrong products or medical procedures. Labs follow strict protocols, and regulatory bodies watch closely. Rolling out better purity testing and traceability can protect patients and consumers. I’d like to see more collaboration between hospitals, food makers, and biotech firms to make sure the enzyme only lands where it’s needed.
Carboxypeptidase B might not sound glamorous, but it quietly supports daily life—from breakfast cereal to critical care units. When handled correctly, its benefits touch biology, diagnosis, patient care, and the fight against food allergies. Continuous investment in research, safety, and education will keep its uses both wide and safe.
I’ve seen what happens in labs when storage instructions for a protein like carboxypeptidase B get skipped or glossed over. One day the vial’s fine and clear, and a week later, the sample shows odd precipitates or the activity drops off. In science, those little setbacks cost not only money but also time, and trust me, no researcher enjoys repeating controls because an enzyme failed quietly in a freezer.
Carboxypeptidase B, straight from most suppliers, arrives as a lyophilized powder, tucked in sealed bottles. That keeps it stable while shipping. In my experience, the first mistake happens once the bottle enters the lab. Leaving it at room temperature, even for a few hours, can spark gradual breakdown, especially if humidity creeps in. Protein chemistry research and supplier data sheets agree—storing it at -20°C or lower stretches its shelf life. Freezers offer insurance against the slow, invisible creep of enzymatic breakdown.
Water’s the enemy of dry protein. Lyophilized powders soak up moisture from the air, and that’s bad news. Moisture encourages clumping, leading to gritty reconstitution and a headache for anyone who wants clean, reliable results. I’ve learned to cap bottles fast and store them in airtight containers, sometimes tossing in silica gel packets for extra protection. Labs that ignore this risk find themselves pitching batches into biohazard bins and writing urgent emails for replacements.
Every time a bottle or aliquot slides from freezer to bench and back again, tiny ice crystals can nick the protein’s structure. Over time, these bruises pile up, and activity fades. Instead of thawing big portions, splitting stocks into small aliquots prevents this. I’ve seen graduate students manage months of experiments simply because they avoided the “thaw-and-freeze roulette.” In the long run, portioning saves money and keeps experiments on track.
Solubility and activity get a boost from using the right buffer—commonly a neutral pH solution like Tris or phosphate with salt. Too high or too low pH tends to unravel the protein. Some protocols recommend a touch of glycerol if the enzyme will be kept in solution for more than a few days in the fridge, since glycerol helps cushion the structure. This tip isn’t just lab lore. Studies referenced in publications back the stabilizing effect of a bit of glycerol or even a reducing agent if long storage is the plan.
Keeping carboxypeptidase B away from direct light helps preserve it, since light can trigger changes in some proteins and speed up degradation. I take care not to leave vials exposed on a sunny bench. Warmth works against stability too. After reconstituting, I use ice buckets or specialized chill blocks, even during short work sessions, to keep the enzyme in top shape.
Planning ahead avoids panic. Before prepping big assays or new experiments, checking the enzyme’s batch number, expiration date, and appearance matters. I make a habit of logging freezer temperatures and batch usage in shared spaces, so nobody gets caught out by a dead enzyme pool. Simple habits like these cut troubleshooting sessions in half.
Storing carboxypeptidase B isn’t complicated, but a few missteps throw away good money and valuable time. Real results come from small changes: cold storage, moisture control, aliquoting, and some vigilance against light and warmth. It’s not about fancy equipment or high-tech solutions—just solid, careful lab practice and respect for what keeps these proteins working as they should.
Carboxypeptidase B is a familiar sight on the bench for anyone working with protein and peptide sequencing. It’s a staple in biochemical research because it snips off basic amino acids like lysine and arginine from the carboxy-terminal end of proteins. Getting the dosage right isn’t just a technical detail—it matters for anyone wanting repeatable, reliable outcomes in assays or industrial applications.
In enzyme reactions, a common working concentration for Carboxypeptidase B lands between 1 and 100 micrograms per milliliter, depending on substrate load and experimental design. For small-scale peptide profiling, I’ve found that 10 μg/mL in a controlled buffer at pH 7.6 (often Tris-HCl) with 10 mM CaCl2 gives steady, predictable cleavage without chewing up too much starting material. Larger proteins or more stubborn substrates sometimes call for bumping up the dose, but there’s a point where higher concentrations only pad the cost and can introduce unwanted side activity.
Too much enzyme won’t save a poorly optimized protocol. Side reactions or nonspecific cleaving will confuse data, especially in mass spectrometry workflows or mapping glycosylation. In a large lab, someone always tries to speed things up with a heavy hand, but excess just muddies analysis and wastes a reagent that isn’t cheap. Manufacturer guides usually stick to a safe middle ground: 10–20 units per reaction, translating to roughly 5–20 μg per milliliter. For blood plasma studies—where Carboxypeptidase B neutralizes inflammatory peptides—clinicians run at much lower doses, in the 0.05–1 μg/mL range, to avoid stripping off critical peptide ends that play roles in blood clotting.
The best way to calibrate? Start low, run a control, and titrate upwards if incomplete digestion lingers. In my own experiments with serum proteins, starting at 5 μg/mL gave clear fragment bands; doubling it made only a marginal difference and wasn’t worth twice the spend. For folks working in food or pharma quality labs, process optimization teams should run stability and recovery trials before settling on a dosage, since process impurities or buffer composition can mess with enzyme stability and output.
Peer-reviewed studies and supplier technical sheets echo these numbers, not out of habit but from repeated validation. For instance, Sigma-Aldrich, Thermo, and Worthington all publish recommendations in the 10–30 μg/mL range for in vitro digestion of standard proteins. Higher numbers exist for special cases, but those often mean extra cleanup steps, especially if downstream analysis needs sharp mass or charge separation.
In GMP production, teams test in the presence of final formulation components to adjust the dose for real-world complexity. My experience on a protein chemistry team proved that jumping straight from “textbook” numbers without testing on your own sample rarely works out cleanly. There’s no shame in reporting optimal ranges rather than exact numbers—biological systems have quirks that lab manuals can’t always predict.
For anyone setting up new protocols or onboarding new team members, keeping detailed records of concentration, substrate batch, and reaction conditions saves hours or days of troubleshooting. Talking across departments—biochemists, analytical chemists, and production—ensures enzyme lots are dosed right for safety, cost, and accuracy.
The push for clarity isn’t just a science tradition. It has real stakes for labs, patients, and food supply chains relying on Carboxypeptidase B. Carefully tracked dosing and reaction conditions, supported by peer data and hands-on experience, set a stronger foundation for both research and product safety.
Carboxypeptidase B breaks down proteins by chopping off basic amino acids like lysine or arginine from the end of peptide chains. Many labs use it to analyze, modify, or purify proteins, especially when precision matters. This makes it a staple for protein sequencing work, mass spectrometry prep, and sometimes removing tags from recombinant proteins. I’ve personally reached for Carboxypeptidase B during the tricky stage of processing plasma samples, where removing interfering peptides made or broke the experiment.
Description on a webpage won’t always tell you if this enzyme will work for your protocol. Dig into a few things before opening a new vial. First: what exactly are you trying to cleave? This enzyme works only on the C-terminal of proteins or peptides. If that’s not the target site in your application, you won’t get much use out of it.Some methods require clean breaks at those C-terminal ends, especially in diagnostics and biomarker research. If your sample prep step depends on that, there’s a good chance Carboxypeptidase B will come in handy. I’ve found it indispensable in prepping samples for MALDI-TOF, as it efficiently removes extra residues and reduces signal noise.
If your protocol is optimized for calcium-rich or phosphate-rich buffers, expect some headaches. Carboxypeptidase B performs at its peak only at certain pH ranges, usually pH 7.6-8.0, and it handles Tris buffers well. Zinc is vital for its activity, so make sure your buffer doesn’t strip away divalent ions or contain heavy metal chelators like EDTA. More than once, I’ve watched activity plummet due to some leftover EDTA from a wash step.
Temperature also affects yield. Routine incubations at 37°C make sense, but ramping up much higher will denature the enzyme. Cold rooms slow everything to a crawl. Run a small pilot test if your protocol deviates from standard conditions.
In applications involving sensitive downstream readouts—mass spectrometry stands out here—enzyme purity takes center stage. Trace contaminants cause background noise or even digest other protein fragments you hoped to keep intact. Look for Carboxypeptidase B lots certified as sequencing grade, which means minimal exogenous protease activity. Having clean starting reagent has rescued plenty of sample runs for me.
Don’t forget species matching either. Some labs use bovine Carboxypeptidase B; others lean on recombinant versions from E. coli. These can differ slightly in behavior. If your protocol hinges on lot-to-lot reproducibility, it’s best to stick with a single supplier and document batch numbers. We once saw unexplained data drift after switching vendors, only pinning it down thanks to fastidious lab records.
If digestion feels incomplete, try boosting enzyme concentration or extending the incubation. Sometimes an extra five or ten minutes makes a huge difference, especially with peptides stubbornly folded around their target sites. On the flip side, rapid over-digestion can trim too much from sensitive samples, so monitor progress with a test gel or LC trace.
Switching from animal to recombinant enzymes may cut down on unwanted side activity, especially in regulated or therapeutic prep. For clinical-facing work, always trace enzyme origin and use non-animal source certifications for peace of mind. I’ve seen regulatory audits dig deep into these details.
Check compatibility by weighing your protocol’s buffer, protein targets, and sensitivity to impurities. Match that list against the Carboxypeptidase B product page—don’t just trust generic compatibility claims. Test the conditions on a small scale first, then scale up confidently. It’s attention to these small details that separates successful protocols from frustrating ones.
Carboxypeptidase B comes up often in research and manufacturing, especially around protein analysis and some medical applications. Many scientists encounter it in the lab routine, but not everyone stops to consider what this enzyme could do outside its intended use. My early years in the lab taught me a simple lesson: pay attention to the small print on safety data sheets. Carboxypeptidase B, though used in small quantities, can cause allergic reactions and respiratory issues. Some reports link accidental exposure to irritation of the skin, eyes, and airways. Even the most experienced researchers slip into routines, but safety basics matter for everyone.
Proper handling of Carboxypeptidase B starts from the delivery box. I always kept my enzyme stocks at -20°C because enzymes like this lose function if stored warm. Still, safety isn't only about function—it’s also about limiting risk. A tightly sealed container stops spills and reduces moisture getting in, which can mess with the powder quality and increase risk of accidental inhalation.
We used to joke that lab coats and gloves made us look like movie surgeons, but after just one splash of enzyme solution on my arm, I never joked again. Simple PPE—gloves, goggles, and coats—saves time and misery. I kept a dedicated set of gloves for enzyme work to avoid cross-contamination. It's easy to forget, especially on busy days, but rinsing gloves and hands after use pays off in safety. Splash goggles offer real protection against accidental squirts during pipetting or vortexing, which happens far more than anyone admits.
Those using the enzyme in powder form face extra risk because powders go airborne. We always weighed and dissolved lyophilized Carboxypeptidase B inside a fume hood. Fume hoods keep particles out of the air in regular workspace. Mouth pipetting seems like an obvious no-go, but young scientists still forget—never do it, not even in a rush. Use only mechanical pipettors; it’s about keeping enzyme droplets out of your mouth and lungs.
I’ve seen small enzyme spills handled poorly because nobody thought the powder could do much harm. Cleanup should begin by clearing the area, putting on fresh gloves and a mask. Wetting down the powder before wiping it up keeps dust from spreading. Never sweep dry powders. Absorb solutions with paper towels, wash the spill site with plenty of water and detergent, and always report the incident. Eye and skin contact call for fifteen-minute flushes at the station, and accidental inhalation needs immediate fresh air plus medical advice if coughing or shortness of breath develops.
Unused Carboxypeptidase B doesn’t belong down the sink. We added waste enzyme solutions and contaminated materials to biohazard bins, following the local rules for lab chemical disposal. All containers got clear labels. I cannot stress enough how proper labeling saves confusion, especially when one team member steps out and another comes in. Regular safety training never feels urgent until something goes wrong; ongoing reminders in the workplace help catch casual mistakes before they turn into accidents. I believe open communication and easy access to up-to-date safety data sheets benefit every lab using enzymes like Carboxypeptidase B.
| Names | |
| Preferred IUPAC name | Carboxypeptidyl-L-arginine hydrolase |
| Other names |
Pancreas carboxypeptidase B Protaminase Tissue carboxypeptidase B |
| Pronunciation | /ˌkɑːrˌbɒk.siˈpeptɪdeɪz ˈbiː/ |
| Identifiers | |
| CAS Number | 9025-24-5 |
| Beilstein Reference | 35956 |
| ChEBI | CHEBI:60888 |
| ChEMBL | CHEMBL2049 |
| ChemSpider | 5312658 |
| DrugBank | DB02529 |
| ECHA InfoCard | 07d6f9f6-6a84-4125-9164-c2dcaf149048 |
| EC Number | 3.4.17.2 |
| Gmelin Reference | 8777 |
| KEGG | ec:3.4.17.2 |
| MeSH | D002374 |
| PubChem CID | 64758 |
| RTECS number | CY1409000 |
| UNII | 355FM74D7T |
| UN number | UN2814 |
| Properties | |
| Chemical formula | C2200H3458N606O655S17 |
| Molar mass | 34704.77 g/mol |
| Appearance | White lyophilized powder |
| Odor | Odorless |
| Density | 0.98 g/cm³ |
| Solubility in water | Soluble in water |
| log P | -4.0 |
| Vapor pressure | Negligible |
| Acidity (pKa) | 7.9 |
| Basicity (pKb) | 7.9 |
| Dipole moment | 23.49 D |
| Thermochemistry | |
| Std molar entropy (S⦵298) | 854 J/(mol·K) |
| Pharmacology | |
| ATC code | B06AA03 |
| Hazards | |
| Main hazards | May cause allergy or asthma symptoms or breathing difficulties if inhaled. |
| GHS labelling | GHS labelling: "Not a hazardous substance or mixture according to the Globally Harmonized System (GHS) |
| Pictograms | ⟨PS00290⟩ |
| Signal word | Warning |
| Hazard statements | H315: Causes skin irritation. H319: Causes serious eye irritation. H334: May cause allergy or asthma symptoms or breathing difficulties if inhaled. H335: May cause respiratory irritation. |
| Precautionary statements | P280, P305+P351+P338, P337+P313 |
| NFPA 704 (fire diamond) | NFPA 704: 1-0-0 |
| NIOSH | Not Assigned |
| PEL (Permissible) | PEL (Permissible) for Carboxypeptidase B: Not established |
| REL (Recommended) | 0.01-1 mg/ml |
| Related compounds | |
| Related compounds |
Carboxypeptidase A Carboxypeptidase N Carboxypeptidase D Carboxypeptidase E |
