Registration Dossier
Registration Dossier
Data platform availability banner - registered substances factsheets
Please be aware that this old REACH registration data factsheet is no longer maintained; it remains frozen as of 19th May 2023.
The new ECHA CHEM database has been released by ECHA, and it now contains all REACH registration data. There are more details on the transition of ECHA's published data to ECHA CHEM here.
Diss Factsheets
Use of this information is subject to copyright laws and may require the permission of the owner of the information, as described in the ECHA Legal Notice.
EC number: 202-860-4 | CAS number: 100-52-7
- Life Cycle description
- Uses advised against
- Endpoint summary
- Appearance / physical state / colour
- Melting point / freezing point
- Boiling point
- Density
- Particle size distribution (Granulometry)
- Vapour pressure
- Partition coefficient
- Water solubility
- Solubility in organic solvents / fat solubility
- Surface tension
- Flash point
- Auto flammability
- Flammability
- Explosiveness
- Oxidising properties
- Oxidation reduction potential
- Stability in organic solvents and identity of relevant degradation products
- Storage stability and reactivity towards container material
- Stability: thermal, sunlight, metals
- pH
- Dissociation constant
- Viscosity
- Additional physico-chemical information
- Additional physico-chemical properties of nanomaterials
- Nanomaterial agglomeration / aggregation
- Nanomaterial crystalline phase
- Nanomaterial crystallite and grain size
- Nanomaterial aspect ratio / shape
- Nanomaterial specific surface area
- Nanomaterial Zeta potential
- Nanomaterial surface chemistry
- Nanomaterial dustiness
- Nanomaterial porosity
- Nanomaterial pour density
- Nanomaterial photocatalytic activity
- Nanomaterial radical formation potential
- Nanomaterial catalytic activity
- Endpoint summary
- Stability
- Biodegradation
- Bioaccumulation
- Transport and distribution
- Environmental data
- Additional information on environmental fate and behaviour
- Ecotoxicological Summary
- Aquatic toxicity
- Endpoint summary
- Short-term toxicity to fish
- Long-term toxicity to fish
- Short-term toxicity to aquatic invertebrates
- Long-term toxicity to aquatic invertebrates
- Toxicity to aquatic algae and cyanobacteria
- Toxicity to aquatic plants other than algae
- Toxicity to microorganisms
- Endocrine disrupter testing in aquatic vertebrates – in vivo
- Toxicity to other aquatic organisms
- Sediment toxicity
- Terrestrial toxicity
- Biological effects monitoring
- Biotransformation and kinetics
- Additional ecotoxological information
- Toxicological Summary
- Toxicokinetics, metabolism and distribution
- Acute Toxicity
- Irritation / corrosion
- Sensitisation
- Repeated dose toxicity
- Genetic toxicity
- Carcinogenicity
- Toxicity to reproduction
- Specific investigations
- Exposure related observations in humans
- Toxic effects on livestock and pets
- Additional toxicological data
Additional toxicological data
Administrative data
- Endpoint:
- additional toxicological information
- Type of information:
- experimental study
- Adequacy of study:
- supporting study
- Reliability:
- 2 (reliable with restrictions)
- Rationale for reliability incl. deficiencies:
- other: Publication intended to develop an alternative in vitro method for sensitization, test substance used as example of non-sensitizer.
Data source
Reference
- Reference Type:
- publication
- Title:
- Unnamed
- Year:
- 2 006
- Report date:
- 2006
Materials and methods
- Type of study / information:
- Covalent modification of skin proteins by electrophiles is a key event in the induction of skin sensitisation but not skin irritation although the exact nature of the binding mechanisms has not been determined empirically for the vast majority of sensitisers. It is also unknown whether immunologically relevant protein targets exist in the skin contributing to effecting skin sensitisation.
Test guideline
- Qualifier:
- no guideline followed
- Principles of method if other than guideline:
- The aim of this work was to verify for selected non-sensitisers that no protein haptenation occurs even under forcing conditions. The test substance solubilised in 3:2 dimethylsulphoxide: water (v/v). Samples were prepared using solutions of test chemicals and solution of human serum albumin (HAS) at a 1:100 and 1:1000 molar ratio of protein: chemical in 50 mM ammonium acetate. Samples were incubated at 37 ℃. Incubation length varied between 24 h and 28 days, depending on the experiment.
- GLP compliance:
- not specified
Test material
- Reference substance name:
- Benzaldehyde
- EC Number:
- 202-860-4
- EC Name:
- Benzaldehyde
- Cas Number:
- 100-52-7
- Molecular formula:
- C7H6O
- IUPAC Name:
- benzaldehyde
- Details on test material:
- Batch No.: not specified
Purity: > 95% pure
Constituent 1
Results and discussion
Any other information on results incl. tables
HSA peptide mapping and assessment of experimental variability:
On average, more than 90% of the native HSA sequence was observed in any one MALDI-ToF spectrum of the control samples. Relative signal intensities changed depending on the position of the laser beam on the sample-matrix mixture as well as laser intensity at the time of data acquisition, thus only semiquantitative information can be derived when MALDI-MS spectra are compared. Although observing reduced signal intensity could potentially mean that the relevant peptide is modified by a hapten, covalent adducts could reliably be detected only by appearance of new signals with mass shifts of modified peptides corresponding to hapten adducts.
Analyses of samples incubated with the test substance:
MALDI-MS analyses of the HSA-the test substance samples did not show the appearance of any new signals when compared to the control sample spectrum. Additionally, all samples were subjected to RP-HPLC separation and rigorous ES-MS/MS analyses of the collected fractions failed to produce any evidence of covalent modifications of HSA by the test substance.
Applicant's summary and conclusion
- Conclusions:
- It was concluded that the test substance do not covalently modify HSA in this test system under any incubation conditions. This is indicative for the absence of haptenation of the test substance, which is expected for a non sensitizer.
- Executive summary:
The aim of this work was to verify for selected non-sensitisers (the test substance is considered to be a non-sensitizer by the authors of the report) that no protein haptenation occurs even under forcing conditions (binding to any of the nucleophilic centra in intact human serum albumin (HSA)). The test substance solubilised in 3:2 dimethylsulphoxide: water (v/v). Samples were prepared using solutions of test chemicals and solution of human serum albumin (HSA) at a 1:100 and 1:1000 molar ratio of protein: chemical in 50 mM ammonium acetate (as HSA has 125 nucleophilic side chains the molar ratios of nucleophile: electrophile are effectively 1:0.8 and 1:8, respectively). Samples were incubated at 37 ℃. Incubation length varied between 24 h and 28 days, depending on the experiment.
It was concluded that the test substance do not covalently modify HSA in this test system under any incubation conditions. This is indicative for the absence of haptenation of the test substance, which is expected for a non sensitizer (although in theory reaction with nucleophils via Schiff base formation may be possible for the test substance).
Information on Registered Substances comes from registration dossiers which have been assigned a registration number. The assignment of a registration number does however not guarantee that the information in the dossier is correct or that the dossier is compliant with Regulation (EC) No 1907/2006 (the REACH Regulation). This information has not been reviewed or verified by the Agency or any other authority. The content is subject to change without prior notice.
Reproduction or further distribution of this information may be subject to copyright protection. Use of the information without obtaining the permission from the owner(s) of the respective information might violate the rights of the owner.