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CAS No. : | 71989-16-7 | MDL No. : | MFCD00037132 |
Formula : | C19H18N2O5 | Boiling Point : | - |
Linear Structure Formula : | - | InChI Key : | YUGBZNJSGOBFOV-INIZCTEOSA-N |
M.W : | 354.36 | Pubchem ID : | 2724774 |
Synonyms : |
|
Chemical Name : | (S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-4-amino-4-oxobutanoic acid |
Signal Word: | Warning | Class: | N/A |
Precautionary Statements: | P261-P264-P271-P280-P302+P352-P305+P351+P338 | UN#: | N/A |
Hazard Statements: | H315-H319-H335 | Packing Group: | N/A |
GHS Pictogram: |
* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
Bis(trifluoroacetoxy)iodobenzene (PIFA, 6.05 g, 14.1 mmol) was added to a suspension of Fmoc-Asn-OH (3.30 g, 9.3 mmol) in DMF-H2O (2:1, 66 mL). After 15 min, pyridine (1.57 g, 1.60 mL, 19.9 mmol) was added and the mixture was stirred at r.t. overnight. The solvent was removed and the oily residue was dissolved in H2O (50 mL). Concd HCl (1 mL) was added, and the aqueous phase was washed with Et2O (4 × 30 mL). The aqueous phase was adjusted to pH 6 with aq 2 M NaOH, and the resulting precipitate was collected by filtration, washed with H2O (5 × 30 mL), cold EtOH (10 mL), and Et2O (10 × 10 mL) to give Fmoc-Dap-OH; yield: 1.75 g (58%,5.4 mmol); beige solid; mp 222-223 C (Lit.22 mp 222-224 C). LC-MS (ESI): 96.3% purity; m/z = 327.22 ([M + H]+). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate; N-ethyl-N,N-diisopropylamine; In DMF (N,N-dimethyl-formamide); at 20℃; for 12h;Combinatorial reaction / High throughput screening (HTS); | Split & Mix Procedure for the Resin Bound HexapeptideP-Glu (OAll)-Gly-X1X2X3X4-H sublibrary The resin was suspended in 3:1 mixture of 1,2-dichloroethane (DCE) and DMF and equally partitioned into 17 4 mL Alltech tubes. Each tube thus contained 0.1/17 mmol=5.88 10-6 mol of resin-bound dipeptide. Excess solvent was removed in vacuo, and the resin was suspended in DMF (200 mL) and agitated for 30 minutes. The 17 amino acids (1.76 10-5 mmol, 3 eq for each step, 7.04 10-5 mmol for 4 steps) were weighed into 17 vials: 1. Fmoc-Ala-OH 22 mg 2. Fmoc-Asn-OH 25 mg 3. Fmoc-Asp(OtBu)-OH 29 mg 4. Fmoc-Gln-OH 26 mg 5. <strong>[104091-08-9]Fmoc-Glu(OtBu)-OH</strong> 30 mg 6. Fmoc-Gly-OH 21 mg 7. Fmoc-Ile-OH 25 mg 8. Fmoc-Leu-OH 25 mg 9. Fmoc-Lys(BOC)-OH 33 mg 10. Fmoc-Met-OH 26 mg 11. Fmoc-Phe-OH 27 mg 12. Fmoc-Pro-OH 24 mg 13. Fmoc-Ser(tBu)-OH 27 mg 14. Fmoc-Thr(tBu)-OH 28 mg 15. Fmoc-Trp(BOC)-OH 37 mg 16. Fmoc-Tyr(tBu)-OH 32 mg 17. Fmoc-Val-OH 24 mg Each amino acid was dissolved in DMF (2 mL); an aliquot of each solution (0.5 mL, corresponding to 1.76 10-5 mmol, 3 eq of each amino acid) was added to the appropriate tube. TBTU (1.76 10-5 mmol×17=2.99 10-4, 96 mg) and DIPEA (1.76 10-5 mmol×17=2.99 10-4, 52 mL) were separately dissolved in DMF (1.7 mL) and each solution was evenly distributed, delivering 3 eq of each reagent, to each one of the 17 tubes.The reaction tubes were agitated at room temperature for 12 hours, then the reagents and solvents were removed in vacuo and the resin was rinsed with DMF (2×1 mL each tube), DCM (2×1 mL each tube) and methanol (2×1 mL each tube). The resin was then suspended in 3:1 mixture of 1,2-dichloroethane and DMF and recombined. The recombined resin was acetylated (3 mL of acetylating reagent, 1 hour, room temperature) and deprotected (3 mL of 20% piperidine in DMF, 2 hours, room temperature).The procedure was repeated 3 more times. At the end of the 4th amino acid coupling the deprotection step was not executed. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: Cyclic peptides 18-23 were synthesised on 2-chlorotritylchloride (2CTC) resin on a 0.1 m equiv. scale. Couplings were performed using 3 equiv. of Fmoc-protected amino acid, 3 equiv. of HCTU, and 6 equiv. of DIPEA in DMF (0.1 M in amino acid) for 50 min. Fmoc deprotection was carried out with 30% (v/v) piperidine in DMF (2 x 5 min). After each coupling and deprotection step, the resin was washed six times with DMF. Peptides were cleaved from the resin using 1% (v/v) TFA in DCM. Head-to-tail cyclisation of side-chain protected peptide was performed in DMF (4 mM final concentration of peptide) with 3 equiv. of DPPA and 4 equiv. of DIPEA. Following removal of the solvent, side-chain protecting groups were removed in 95 : 5 TFA/TIPS. After cyclisation, the peptides were purified by reverse-phase preparative HPLC. Purity of fractions was assessed using ESI-MS (Table 2) and analytical HPLC. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
Solid phase peptide synthesis was performed on a CEM Liberty Peptide Synthesizer using standard Fmoc chemistry. TentaGel S Ram resin (1 g; 0.25 mmol/g) was swelled in NMP (10 ml) prior to use and transferred between tube and reaction vessel using DCM and NMP. Coupling (0148) An Fmoc-amino acid in NMP/DMF/DCM (1:1:1; 0.2 M; 5 ml) was added to the resin in a CEM Discover microwave unit together with HATU/DMF or COMU/DMF (0.5 M; 2 ml) and DIPEA/NMP (2.0 M; 1 ml). The coupling mixture was heated to 75° C. for 5 min while nitrogen was bubbled through the mixture. The resin was then washed with NMP (4×10 ml). Deprotection (0149) Piperidine/DMF (20percent; 10 ml) was added to the resin for initial deprotection and the mixture was heated by microwaves (30 sec; 40° C.). The reaction vessel was drained and a second portion of piperidine/NMP (20percent; 10 ml) was added and heated (75° C.; 3 min.) again. The resin was then washed with DMF (6×10 ml). Side Chain Acylation (0150) Fmoc-Lys(ivDde)-OH or alternatively another amino acid with an orthogonal side chain protective group was introduced at the position of the acylation. The N-terminal of the peptide backbone was then Boc-protected using Boc2O or alternatively by using a Boc-protected amino acid in the last coupling. While the peptide was still attached to the resin, the orthogonal side chain protective group was selectively cleaved using freshly prepared hydrazine hydrate (2-4percent) in NMP for 2×15 min. The unprotected lysine side chain was first coupled with Fmoc-Glu-OtBu or another spacer amino acid, which was deprotected with piperidine and acylated with a lipophilic moiety using the peptide coupling methodology as described above. Alternatively, the acylation moiety was introduced as a premade building block e.g. Fmoc-Lys(hexadecanoyl-gamma-Glu)-OH where gamm-Glu is the coupling of Glutamic acid through the side-chain. Abbreviations employed are as follows: COMU: 1-[(1-(cyano-2-ethoxy-2-oxoethylideneaminooxy)-dimethylamino-morpholinomethylene)]methanaminium hexaflourophosphate ivDde: 1-(4,4-dimethyl-2,6-dioxocyclohexylidene)3-methyl-butyl Dde: 1-(4,4-dimethyl-2,6-dioxocyclohexylidene)-ethyl DCM: dichloromethane DMF: N,N-dimethylformamide (0151) DIPEA: diisopropylethylamine EtOH: ethanol Et2O: diethyl ether HATU: N-[(dimethylamino)-1H-1,2,3-triazol[4,5-b]pyridine-1-ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide MeCN: acetonitrile NMP: N-methylpyrrolidone (0152) TFA: trifluoroacetic acid TIS: triisopropylsilane Cleavage (0153) The resin was washed with EtOH (3×10 ml) and Et2O (3×10 ml) and dried to constant weight at room temperature (r.t.). The crude peptide was cleaved from the resin by treatment with TFA/TIS/water (95/2.5/2.5; 40 ml, 2 h; r.t.). Most of the TFA was removed at reduced pressure and the crude peptide was precipitated and washed three times with diethylether and dried to constant weight at room temperature. HPLC Purification of the Crude Peptide (0154) The crude peptide was purified to greater than 90percent by preparative reverse phase HPLC using a PerSeptive Biosystems VISION Workstation equipped with a C-18 column (5 cm; 10 mum) and a fraction collector and run at 35 ml/min with a gradient of buffer A (0.1percent TFA, aq.) and buffer B (0.1percent TFA, 90percent MeCN, aq.). Fractions were analyzed by analytical HPLC and MS and relevant fractions were pooled and lyophilized. The final product was characterized by HPLC and MS. (0155) The synthesized compounds are shown in Table 1 and Table 2 |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
Peptide monomers of the present invention were synthesized using the Merrifield solid phase synthesis techniques on Protein Technology's Symphony multiple channel synthesizer. The peptides were assembled using HBTU (0-Benzotriazole-N,N,N',N'-tetramethyl-uronium- hexafluoro-phosphate), Diisopropylethylamine(DIEA) coupling conditions. For some amino acid couplings PyAOP(7-Azabenzotriazol- 1 -yloxy)tripyrrolidinophosponium hexafluorophosphate) and DIEA conditions were used. Rink Amide MB HA resin (100-200 mesh, 0.57 mmol/g) was used for peptide with C-terminal amides and pre-loaded Wang Resin with N-a-Fmoc protected amino acid was used for peptide with C-terminal acids. The coupling reagents (HBTU and DIEA premixed) were prepared at lOOmmol concentration. Similarly amino acids solutions were prepared at 100 mmol concentration. Peptide inhibitors of the present invention were identified based on medical chemistry optimization and/or phage display and screened to identify those having superior binding and/or inhibitory properties.[00611] The peptides were assembled using standard Symphony protocols. The peptide sequences were assembled as follows: Resin (250 mg, 0.14 mmol) in each reaction vial was washed twice with 4ml of DMF followed by treatment with 2.5ml of 20% 4-methyl piped dine (Fmoc de- protection) for lOmin. The resin was then filtered and washed two times with DMF (4ml) and re -treated with N-methyl piperifine for additional 30 minute. The resin was again washed three times with DMF (4 ml) followed by addition 2.5ml of amino acid and 2.5ml of HBTU-DIEA mixture. After 45min of frequent agitations, the resin was filtered and washed three timed with DMF (4 ml each). For a typical peptide of the present invention, double couplings were performed. After completing the coupling reaction, the resin was washed three times with DMF (4 ml each) before proceeding to the next amino acid coupling. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: 100 mg 2-chlorotrityl resin (0.5 mmol/g) was placed in a 6 mL polypropylene syringe with a polyethylene filter in the bottom. It was swelled with DCM for 1 h. Then it was washed by DMF(3 2 mL) and DCM (3 2 mL). The first building block was added by using <strong>[118904-37-3]<strong>[118904-37-3]Fmoc-D-allo-Ile</strong>-OH</strong> (35.3 mg, 0.1 mmol) and DIEA(34.8 mL, 0.2 mmol) in 2 mL DCM and shaken for 1 h. Then 80 mL MeOH was added and shaken for another 20 min. Then the resin was washed by DCM (3 2 mL) and DMF (3 2 mL). The following amino acids were coupled through the general Fmoc-SPPS strategy. Then the resin was treated by a mixture of 3 mL DCM/AcOH/TFE(v/v/v = 8:1:1) for 1.5 h to obtain the crude linear peptide 3(36.7 mg, 0.037 mmol). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
6% | General procedure: The Fmoc-Ala-Wang Resin (0.1mmol/g) was swelled in DCM. The Fmoc group was deprotectedby 20% piperidine in DMF over 2 times. The Fmoc protected amino acid building blocks wereattached to resin by 2-(7-Aza-1H-benzotriazole-1-yl)-1,1,3,3- tetramethyluroniumhexafluorophosphate (HATU, 4 equiv)/1-Hydroxy-7- azabenzotriazole (HOAt, 3.8 equiv) asactivator, N,N-Diisopropylethylamine (DIEA, 8 equiv) as activator base, DMF as solvent for1hour. After coupling all amino acids, the crude peptides were cleaved from resin byTFA/TIS/H2O (88%/6%/6%, v/v/v) for 2 hours, purified by RP-HPLC and identified by ESI-MS.The purification was measured on Shimadzu LC-6AD with preparative C18 column (YMC, Japan,5mum, 20×250 mm), solution A (80% MeCN/H2O with 0.06% TFA) and solution B (100% H2Owith 0.06% TFA). The analysis was measured on Shimadzu LC-2010A with analytic C18 column(YMC, Japan, 5mum, 4.6×150 mm), solution A (80% MeCN/H2O with 0.06% TFA) and solution B(100% H2O with 0.06% TFA). The ESI-MS was measured on Thermo Scientific UltiMate 3000.After RP-HPLC purification, the peptide was obtained by lyophilization. The lyophilizedglycopeptides were redissolved in MeOH/MeONa solution with pH 9.5 to deprotect the acetylgroup on carbohydrate. The glycopeptide was obtained by further RP-HPLC purification andlyophilization. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
7% | General procedure: The Fmoc-Ala-Wang Resin (0.1mmol/g) was swelled in DCM. The Fmoc group was deprotectedby 20% piperidine in DMF over 2 times. The Fmoc protected amino acid building blocks wereattached to resin by 2-(7-Aza-1H-benzotriazole-1-yl)-1,1,3,3- tetramethyluroniumhexafluorophosphate (HATU, 4 equiv)/1-Hydroxy-7- azabenzotriazole (HOAt, 3.8 equiv) asactivator, N,N-Diisopropylethylamine (DIEA, 8 equiv) as activator base, DMF as solvent for1hour. After coupling all amino acids, the crude peptides were cleaved from resin byTFA/TIS/H2O (88%/6%/6%, v/v/v) for 2 hours, purified by RP-HPLC and identified by ESI-MS.The purification was measured on Shimadzu LC-6AD with preparative C18 column (YMC, Japan,5mum, 20×250 mm), solution A (80% MeCN/H2O with 0.06% TFA) and solution B (100% H2Owith 0.06% TFA). The analysis was measured on Shimadzu LC-2010A with analytic C18 column(YMC, Japan, 5mum, 4.6×150 mm), solution A (80% MeCN/H2O with 0.06% TFA) and solution B(100% H2O with 0.06% TFA). The ESI-MS was measured on Thermo Scientific UltiMate 3000.After RP-HPLC purification, the peptide was obtained by lyophilization. The lyophilizedglycopeptides were redissolved in MeOH/MeONa solution with pH 9.5 to deprotect the acetylgroup on carbohydrate. The glycopeptide was obtained by further RP-HPLC purification andlyophilization. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: Sufficient quantity (50-100 mg) of Fmoc-PAL-PEG-PS resin or Fmoc-Rink amide MB HA resin, loading: 0.5-0.6 mmol/g was swelled in DMF (1-10 ml /100 mg of resin) for 2-10 minutes. The Fmoc-group on resin was removed by incubation of resin with 10-30 % piperidine in DMF (10- 30 ml / 100 mg of resin), for 10-30 minutes. Deprotected resin was filtered and washed excess of DMF, DCM and ether (50 ml X 4). Washed resin was incubated in freshly distilled DMF (1 ml / 100 mg of resin), under nitrogen atmosphere for 5 minutes. A 0.5 M solution of first Fmoc- protected amino acid (1-3 eq.), pre-activated with HOBt (1-3 eq.) and DIPCDI (1-2 eq.) in DMF was added to the resin, and the resin was then shaken for 1-3 hrs, under nitrogen atmosphere. Coupling completion was monitored using a qualitative ninhydrin test. After the coupling of first amino acid, the resin was washed with DMF, DCM and Diethyl ether (50 ml X 4). For the coupling of next amino acid, firstly, the Fmoc-protection on first amino acid, coupled with resin was deprotected, using a 10-20% piperidine solution, followed by the coupling the Fmoc- protected second amino acid, using a suitable coupling agents, and as described above. The repeated cycles of deprotection, washing, coupling and washing were performed until the desired peptide chain was assembled on resin, as per general (Scheme 1) above. Finally, the Fmoc- protected peptidyl-resin prepared above was deprotected by 20% piperidine treatment as described above and the peptidyl-resins were washed with DMF, DCM and Diethyl ether. Resin containing desired peptide was dried under nitrogen pressure for 10-15 minutes and subjected for cleavage/ deprotection. Using above protocol and suitable variations thereof which are within the scope of a person skilled in the art, the short chain peptides designed in the present invention were prepared, using Fmoc-SPPS approach. Furthermore, resin bound short chain peptides were cleaved and deprotected, purified and characterized using following protocol. CLEAVAGE AND DEPROTECTION: The desired short chain peptides were cleaved and deprotected from their respective peptidyl- resins by treatment with TFA cleavage mixture as follows. A solution of TFA / Water / Triisopropylsilane (95: 2.5: 2.5) (10 ml / 100 mg of peptidyl-resin) was added to peptidyl-resins and the mixture was kept at room temperature with occasional starring. The resin was filtered, washed with a cleavage mixture and the combined filtrate was evaporated to dryness. Residue obtained was dissolved in 10 ml of water and the aqueous layer was extracted 3 times with ether and finally the aqueous layer was freeze-dried. Crude peptide obtained after freeze-drying was purified by preparative HPLC as follows: PREPARATIVE HPLC PURIFICATION OF THE CRUDE SHORT CHAIN PEPTIDES: Preparative HPLC was carried out on a Shimadzu LC-8A liquid chromatography. A solution of crude peptide dissolved in DMF or water was injected into a semi-Prep column (Luna 10mu; C18; 100 A0), dimension 250 X 50 mm and eluted with a linear gradient of ACN in water, both buffered with 0.1 % TFA, using a flow rate of 15 -50 ml / min, with effluent monitoring by PDA detector at 220 nm. A typical gradient of 20 % to 70 % of water- ACN mixture, buffered with 0.1 % TFA was used, over a period of 50 minutes, with 1% gradient change per minute. The desired product eluted were collected in a single 10-20 ml fraction and pure short chain peptides were obtained as amorphous white powders by lyophilisation of respective HPLC fractions. HPLC ANALYSIS OF THE PURIFIED SHORT-CHAIN PEPTIDES After purification by preparative HPLC as described above, each peptide was analyzed by analytical RP-HPLC on a Shimadzu LC-10AD analytical HPLC system. For analytical HPLC analysis of short chain peptides, Luna 5mu; C18; 100 A , dimension 250 X 4.6 mm column was used, with a linear gradient of 0.1 % TFA and ACN buffer and the acquisition of chromatogram was carried out at 220 nm, using a PDA detector. CHARACTERIZATION BY MASS SPECTROMETRY Each peptide was characterized by electrospray ionisation mass spectrometry (ESI-MS), either in flow injection or LC/MS mode. Triple quadrupole mass spectrometers (API-3000 (MDS-SCIES, Canada) was used in all analyses in positive and negative ion electrospray mode. Full scan data was acquired over the mass range of quadrupole, operated at unit resolution. In all cases, the experimentally measured molecular weight was within 0.5 Daltons of the calculated monoisotopic molecular weight. Quantification of the mass chromatogram was done using Analyst 1.4.1 software. Following table l(i) is the list of short chain peptides synthesized using the SPPS approach as described above. Mentioned Seq. ID. No 1 in the list was taken as a reference from WO 2011027257. |
Tags: 71989-16-7 synthesis path| 71989-16-7 SDS| 71989-16-7 COA| 71989-16-7 purity| 71989-16-7 application| 71989-16-7 NMR| 71989-16-7 COA| 71989-16-7 structure
A1116731[ 157355-73-2 ]
3-Carbamoyl-2-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)propanoic acid
Reason: Racemic-enantiomer
[ 201473-83-8 ]
(S)-2,4-Bis((((9H-fluoren-9-yl)methoxy)carbonyl)amino)butanoic acid
Similarity: 0.96
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P412 | Do not expose to temperatures exceeding 50 oC/ 122 oF. |
P413 | |
P420 | Store away from other materials. |
P422 | |
P402 + P404 | Store in a dry place. Store in a closed container. |
P403 + P233 | Store in a well-ventilated place. Keep container tightly closed. |
P403 + P235 | Store in a well-ventilated place. Keep cool. |
P410 + P403 | Protect from sunlight. Store in a well-ventilated place. |
P410 + P412 | Protect from sunlight. Do not expose to temperatures exceeding 50 oC/122oF. |
P411 + P235 | Keep cool. |
Disposal | |
Code | Phrase |
P501 | Dispose of contents/container to ... |
P502 | Refer to manufacturer/supplier for information on recovery/recycling |
Physical hazards | |
Code | Phrase |
H200 | Unstable explosive |
H201 | Explosive; mass explosion hazard |
H202 | Explosive; severe projection hazard |
H203 | Explosive; fire, blast or projection hazard |
H204 | Fire or projection hazard |
H205 | May mass explode in fire |
H220 | Extremely flammable gas |
H221 | Flammable gas |
H222 | Extremely flammable aerosol |
H223 | Flammable aerosol |
H224 | Extremely flammable liquid and vapour |
H225 | Highly flammable liquid and vapour |
H226 | Flammable liquid and vapour |
H227 | Combustible liquid |
H228 | Flammable solid |
H229 | Pressurized container: may burst if heated |
H230 | May react explosively even in the absence of air |
H231 | May react explosively even in the absence of air at elevated pressure and/or temperature |
H240 | Heating may cause an explosion |
H241 | Heating may cause a fire or explosion |
H242 | Heating may cause a fire |
H250 | Catches fire spontaneously if exposed to air |
H251 | Self-heating; may catch fire |
H252 | Self-heating in large quantities; may catch fire |
H260 | In contact with water releases flammable gases which may ignite spontaneously |
H261 | In contact with water releases flammable gas |
H270 | May cause or intensify fire; oxidizer |
H271 | May cause fire or explosion; strong oxidizer |
H272 | May intensify fire; oxidizer |
H280 | Contains gas under pressure; may explode if heated |
H281 | Contains refrigerated gas; may cause cryogenic burns or injury |
H290 | May be corrosive to metals |
Health hazards | |
Code | Phrase |
H300 | Fatal if swallowed |
H301 | Toxic if swallowed |
H302 | Harmful if swallowed |
H303 | May be harmful if swallowed |
H304 | May be fatal if swallowed and enters airways |
H305 | May be harmful if swallowed and enters airways |
H310 | Fatal in contact with skin |
H311 | Toxic in contact with skin |
H312 | Harmful in contact with skin |
H313 | May be harmful in contact with skin |
H314 | Causes severe skin burns and eye damage |
H315 | Causes skin irritation |
H316 | Causes mild skin irritation |
H317 | May cause an allergic skin reaction |
H318 | Causes serious eye damage |
H319 | Causes serious eye irritation |
H320 | Causes eye irritation |
H330 | Fatal if inhaled |
H331 | Toxic if inhaled |
H332 | Harmful if inhaled |
H333 | May be harmful if inhaled |
H334 | May cause allergy or asthma symptoms or breathing difficulties if inhaled |
H335 | May cause respiratory irritation |
H336 | May cause drowsiness or dizziness |
H340 | May cause genetic defects |
H341 | Suspected of causing genetic defects |
H350 | May cause cancer |
H351 | Suspected of causing cancer |
H360 | May damage fertility or the unborn child |
H361 | Suspected of damaging fertility or the unborn child |
H361d | Suspected of damaging the unborn child |
H362 | May cause harm to breast-fed children |
H370 | Causes damage to organs |
H371 | May cause damage to organs |
H372 | Causes damage to organs through prolonged or repeated exposure |
H373 | May cause damage to organs through prolonged or repeated exposure |
Environmental hazards | |
Code | Phrase |
H400 | Very toxic to aquatic life |
H401 | Toxic to aquatic life |
H402 | Harmful to aquatic life |
H410 | Very toxic to aquatic life with long-lasting effects |
H411 | Toxic to aquatic life with long-lasting effects |
H412 | Harmful to aquatic life with long-lasting effects |
H413 | May cause long-lasting harmful effects to aquatic life |
H420 | Harms public health and the environment by destroying ozone in the upper atmosphere |
Sorry,this product has been discontinued.
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