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CAS No. : | 159766-56-0 | MDL No. : | MFCD00077409 |
Formula : | C23H26N2O5 | Boiling Point : | - |
Linear Structure Formula : | - | InChI Key : | HQLBYVWJOXITAM-NRFANRHFSA-N |
M.W : | 410.46 | Pubchem ID : | 7018846 |
Synonyms : |
|
Num. heavy atoms : | 30 |
Num. arom. heavy atoms : | 12 |
Fraction Csp3 : | 0.35 |
Num. rotatable bonds : | 12 |
Num. H-bond acceptors : | 5.0 |
Num. H-bond donors : | 3.0 |
Molar Refractivity : | 112.21 |
TPSA : | 104.73 Ų |
GI absorption : | High |
BBB permeant : | No |
P-gp substrate : | Yes |
CYP1A2 inhibitor : | No |
CYP2C19 inhibitor : | No |
CYP2C9 inhibitor : | Yes |
CYP2D6 inhibitor : | No |
CYP3A4 inhibitor : | Yes |
Log Kp (skin permeation) : | -6.62 cm/s |
Log Po/w (iLOGP) : | 2.39 |
Log Po/w (XLOGP3) : | 3.07 |
Log Po/w (WLOGP) : | 3.28 |
Log Po/w (MLOGP) : | 2.15 |
Log Po/w (SILICOS-IT) : | 3.33 |
Consensus Log Po/w : | 2.85 |
Lipinski : | 0.0 |
Ghose : | None |
Veber : | 1.0 |
Egan : | 0.0 |
Muegge : | 0.0 |
Bioavailability Score : | 0.55 |
Log S (ESOL) : | -3.82 |
Solubility : | 0.0617 mg/ml ; 0.00015 mol/l |
Class : | Soluble |
Log S (Ali) : | -4.94 |
Solubility : | 0.00475 mg/ml ; 0.0000116 mol/l |
Class : | Moderately soluble |
Log S (SILICOS-IT) : | -6.44 |
Solubility : | 0.000148 mg/ml ; 0.000000361 mol/l |
Class : | Poorly soluble |
PAINS : | 0.0 alert |
Brenk : | 0.0 alert |
Leadlikeness : | 2.0 |
Synthetic accessibility : | 4.08 |
Signal Word: | Warning | Class: | N/A |
Precautionary Statements: | P261-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 |
---|---|---|
General procedure: The C-terminal fragmentof SAHH (amino acid 396-432 with 396 replaced by Cys, CAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY) with or without acetyl groups at Lys401 and Lys408 were synthesizedusing the standard Fmoc solid phase synthesis strategy on a PS3 peptide synthesizer from Protein Technologies (Tucson, AZ) on 0.1-0.2 mmol scale. Fmoc-protected amino acids were mixed with 4eq of the coupling reagent 1-(bis(dimethylamino)-methylene)-1H-1,2,3-triazolo[4,5-b]pyridinium 3-oxid hexafluorophosphate and double coupled to Wang resin (Novabiochem) containing the protected C-terminal amino acid. The Fmoc protecting group was removed by addition of 20% piperidine in dimethylformamide. A total of four peptides were produced including unacetylated, two singly acetylated, and the bi-acetylated forms. After completion, peptides were cleaved from the resin using reagent K (TFA/thioanisole/water/phenol/ethane dithiol (82.5:5:5:5:2.5, v/v)) for 3-4 h at room temperature. After precipitation with ice-cold diethyl ether, peptides were purified by reversed phase HPLC using a preparative C18 column and a gradient of increasing acetonitrile versus water, each containing 0.05% trifluoroacetic acid. Purefractions were pooled, concentrated by rotor vapor, lyophilized,and stored at -20 C. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: The C-terminal fragmentof SAHH (amino acid 396-432 with 396 replaced by Cys, CAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY) with or without acetyl groups at Lys401 and Lys408 were synthesizedusing the standard Fmoc solid phase synthesis strategy on a PS3 peptide synthesizer from Protein Technologies (Tucson, AZ) on 0.1-0.2 mmol scale. Fmoc-protected amino acids were mixed with 4eq of the coupling reagent 1-(bis(dimethylamino)-methylene)-1H-1,2,3-triazolo[4,5-b]pyridinium 3-oxid hexafluorophosphate and double coupled to Wang resin (Novabiochem) containing the protected C-terminal amino acid. The Fmoc protecting group was removed by addition of 20% piperidine in dimethylformamide. A total of four peptides were produced including unacetylated, two singly acetylated, and the bi-acetylated forms. After completion, peptides were cleaved from the resin using reagent K (TFA/thioanisole/water/phenol/ethane dithiol (82.5:5:5:5:2.5, v/v)) for 3-4 h at room temperature. After precipitation with ice-cold diethyl ether, peptides were purified by reversed phase HPLC using a preparative C18 column and a gradient of increasing acetonitrile versus water, each containing 0.05% trifluoroacetic acid. Purefractions were pooled, concentrated by rotor vapor, lyophilized,and stored at -20 C. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: The C-terminal fragmentof SAHH (amino acid 396-432 with 396 replaced by Cys, CAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY) with or without acetyl groups at Lys401 and Lys408 were synthesizedusing the standard Fmoc solid phase synthesis strategy on a PS3 peptide synthesizer from Protein Technologies (Tucson, AZ) on 0.1-0.2 mmol scale. Fmoc-protected amino acids were mixed with 4eq of the coupling reagent 1-(bis(dimethylamino)-methylene)-1H-1,2,3-triazolo[4,5-b]pyridinium 3-oxid hexafluorophosphate and double coupled to Wang resin (Novabiochem) containing the protected C-terminal amino acid. The Fmoc protecting group was removed by addition of 20% piperidine in dimethylformamide. A total of four peptides were produced including unacetylated, two singly acetylated, and the bi-acetylated forms. After completion, peptides were cleaved from the resin using reagent K (TFA/thioanisole/water/phenol/ethane dithiol (82.5:5:5:5:2.5, v/v)) for 3-4 h at room temperature. After precipitation with ice-cold diethyl ether, peptides were purified by reversed phase HPLC using a preparative C18 column and a gradient of increasing acetonitrile versus water, each containing 0.05% trifluoroacetic acid. Purefractions were pooled, concentrated by rotor vapor, lyophilized,and stored at -20 C. |
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 |
---|---|---|
75% | With sodium carbonate; In 1,4-dioxane; at 15℃; for 6h;pH 8 - 9;Large scale; | 4, 115kg fmoc-cl and 250L dioxane solution were slowly added to the 3 system. The pH of the sodium carbonate solid solution system was 8-9, and the reaction was carried out at 15 C for 6 hours. The reaction process was monitored by TLC. After the reaction was completed, the system was completed. It was washed 4 times with 800 L of a mixed solvent of ethyl acetate and petroleum ether, and then extracted with 1000 L of ethyl acetate, acidified with citric acid and washed with acid water 3 times, then washed with water, saturated with brine, dried, and then dissolved, dried. The product is 84.24 Kg, which is: Nalpha-[(9H-fluoren-9-ylmethoxy)carbonyl]-Nepsilon-acetyl-L-lysine. The product Nalpha-[(9H-fluoren9-ylmethoxy)carbonyl]-Nepsilon-acetyl-L-lysine was analyzed by HPLC, the purity of Nalpha-[(9H-fluoren9-ylmethoxy)carbonyl]-Nepsilon-acetyl-L-lysine is 97.29% as shown in Figure 2, the yield is 75%, the melting point is 161.5-163.2C. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
68% | With sodium carbonate; In acetone; at 15℃; for 6h;pH 8 - 9;Large scale; | 4, 92kg fmoc-osu and 200L acetone solution were slowly added to the 3 system. The pH of the sodium carbonate solid solution system was 8-9, and the reaction was carried out at 15 C for 6 hours. The reaction process was monitored by TLC. After the reaction was completed, the system was treated with 800L. The mixed solvent of ethyl acetate and petroleum ether was washed 4 times, then extracted with 1000 L of ethyl acetate, acidified with citric acid and washed with acid water 3 times, then washed with water, saturated with brine, dried and desolved to obtain a dry product of 76.38 Kg. That is: Nalpha-[(9H-fluoren-9-ylmethoxy)carbonyl]-Nepsilon-acetyl-L-lysine. TLC system and Rf value: 98:8::2 Rf=0..4. The product Nalpha-[(9H-fluoren-9-ylmethoxy)carbonyl]-Nepsilon-acetyl-L-lysine was analyzed by HPLC ,the purity of Nalpha-[(9H-fluoren-9-ylmethoxy)carbonyl]-Nepsilon-acetyl-L-lysine is 99.67%, as shown in Figure 1, the yield is 68%, the melting point is 164.3-164.9C. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
2.A Loading of Fmoc-Lys(Ac)-OH on Rink Amide Resin (0433) In a 100 ml reactor equipped with a sintered glass at the bottom, 6 g of Novabiochem or ChemImpex Rink amide AM resin (Low Loading 0.47 mmol/g) was swelled in 40 ml of DMF. The solvent was drained and 30 ml of 20% piperidine in DMF solution were added. After 15 min shaking, the solvent was drained. This was repeated twice to ensure complete Fmoc protecting group removal. The resin was washed with 5×30 ml DMF. (0434) In a separate flask a solution containing Fmoc-Lys(Ac)-OH (3.5 g, 8 mmol, 3 eq.) HOBT.H2O (1.3 g 8.5 mmol) in 30 ml DMF was prepared. Diisopropylcarbodiimide (DIC) (1 g, 8.5 mmol) was added to this solution and after 5 min the resulting mixture was added to the resin. The suspension was shaken on a stirring plate for 4 h or until completion of the reaction as judged by Kaiser Test (Ninhidrin test) on an aliquot part of the resin. (0435) The solvent was then drained and the resin washed 3 times with 30 ml DMF. Fmoc-Lys(Ac)-NH2 loaded resin was used immediately for subsequent steps or stored wet at 4 C. until needed. (0436) 2.B. Synthesis of Peptide Having the SEQ ID NO: 3 (0437) The following synthesis was performed using 5 times an amount of resin obtained at step 2.A. corresponding to 0.2 mmol of Fmoc-Lys(Ac)-NH2 each. The syntheses were performed separately on each individual batches using a CEM Liberty Blue microwave peptide synthesizer to assemble the second and third residue of the peptide sequence (starting from the C-terminus). (0438) Peptide synthesis was performed by using DIC 0.5M/Oxyma 1M in DMF. (0439) All amino acids were introduced with double couplings using standard heating protocol. (0440) The resin was removed from the synthesizer and Fmoc-alpha-methyl-lysine(Boc)-OH (3 eq.) was coupled manually using 3 eq. Oxyma and 3 eq. DIC with microwave heating (75 C. 15 sec. and 90 C. 110 sec). The completion of the reaction was controlled by Kaiser test. If positive, DIC 3 eq. was added followed by microwave heating as above. When coupling of Fmoc-alpha-methyl-lysine(Boc)-OH was complete the rest of the peptide sequence was assembled using a CEM Liberty Blue microwave peptide synthesizer. (0442) All amino acids were introduced with double couplings at 90 C. as above, with the exception of amino-isobutyric acid at position 21 and serine at position 29 for which a triple coupling at 90 for 2 minutes was performed. Fmoc-Lys(Dde)-OH was used at position 25. (0443) At the end of the 5 syntheses, the 5 batches of resin were combined and transferred into a 50 mL polypropylene syringe and the peptide was acetylated at N-terminus with acetic anhydride (944 10 mmol) in DMF (30 mL) for 20 minutes, repeating the cycle twice. (0444) Then, Dde protecting group on Lysine 25 side chain was removed by percolating 50 mL of a solution of hydrazine 5% w/v in DMF, followed by DMF washes (5×20 ml). The reaction was monitored by Kaiser Test and cleavage of an aliquot part of resin and UPLC/MS analysis. (0445) Three TTDS spacer units were introduced by single coupling by performing three times the following procedure: To the resin a solution of Fmoc-TTDS-OH (1.62 g, 3 mmol) in 30 mL of DMF were added followed by HOAt (5 ml of a 0.6 ml solution in DMF, 3 mmol) and DIC (1 ml, 6 mmol). The syringe was agitated on an orbital table for 18 h. The reaction was monitored by Kaiser Test. The resin was washed with DMF (2×30 mL). Then to the resin, 30 mL of 20% v/v of piperidine in DMF was added. The syringe was agitated on an orbital table for 20 min. This deprotection procedure was repeated a second time and the resin was washed with DMF (2×30 mL) and dichloromethane (3×30 mL). (0446) The three gamma-glutamic acids spacers were introduced by performing a double coupling of each Fmoc-Glu-OtBu. Thus the following procedure was applied three times: To the resin a solution (4S)-5-tert-butoxy-4-(9H-fluoren-9-yl methoxy carbonylamino)-5-oxo-pentanoic acid (Fmoc-Glu-OtBu) (1.275 g, 3 mmol) in of 30 mL of DMF were added followed by HOAt (5 ml of a 0.6 ml solution in DMF 3 mmol) and DIC (1 ml, 6 mmol). The syringe was agitated on an orbital table for 4 h. The resin was washed with DMF (2×20 mL) and the coupling was repeated a second time. The reaction was monitored by Kaiser Test. The resin was washed with DMF (2×30 mL). Then to the resin, 30 mL of 20% v/v of piperidine in DMF was added. The syringe was agitated on an orbital table for 20 min. This deprotection procedure was repeated a second time and the resin was washed with DMF (3×30 mL) and dichloromethane (3×30 mL). (0448) Finally, the peptide was acylated with palmitic acid (768 mg, 3 mmol), HOAt (5 ml of a 0.6 M solution in DMF, 3 mmol) and DIC (1 ml, 6 mmol) activation in DMF (30 mL) for 2.5 h. The resin was washed with DMF (2×30 mL) and dichloromethane (3×30mL) and dried under vacuum. (0449) The cleavage of the peptide from the resin was performed using a solution phenol (6.25 g), water (6.25 mL) and TIPS (3 mL) ... |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
2.A Loading of Fmoc-Lys(Ac)-OH on Rink Amide Resin (0433) In a 100 ml reactor equipped with a sintered glass at the bottom, 6 g of Novabiochem or ChemImpex Rink amide AM resin (Low Loading 0.47 mmol/g) was swelled in 40 ml of DMF. The solvent was drained and 30 ml of 20% piperidine in DMF solution were added. After 15 min shaking, the solvent was drained. This was repeated twice to ensure complete Fmoc protecting group removal. The resin was washed with 5×30 ml DMF. (0434) In a separate flask a solution containing Fmoc-Lys(Ac)-OH (3.5 g, 8 mmol, 3 eq.) HOBT.H2O (1.3 g 8.5 mmol) in 30 ml DMF was prepared. Diisopropylcarbodiimide (DIC) (1 g, 8.5 mmol) was added to this solution and after 5 min the resulting mixture was added to the resin. The suspension was shaken on a stirring plate for 4 h or until completion of the reaction as judged by Kaiser Test (Ninhidrin test) on an aliquot part of the resin. (0435) The solvent was then drained and the resin washed 3 times with 30 ml DMF. Fmoc-Lys(Ac)-NH2 loaded resin was used immediately for subsequent steps or stored wet at 4 C. until needed. (0436) 2.D. Synthesis of Peptide Having the SEQ ID NO: 6 A batch of resin obtained in 2.A. corresponding to 0.1 mmol of Fmoc-Lys(Ac)-NH2 was placed in the reactor of a CEM Liberty Blue microwave peptide synthesizer. Peptide synthesis was performed by using DIC 0.5M/Oxyma 1M in DMF. (0468) All amino acids were introduced with double couplings at 90 C. as above, with the exception of amino-isobutyric acid at position 21 and serine at position 29 for which a triple coupling at 90 for 2 minutes was performed. <strong>[204777-78-6]Fmoc-Lys(ivDde)-OH</strong> was used at position 25. (0469) At the end of peptide assembly, the resin was transferred to a 20 ml polypropylene syringe and peptide was acetylated at N-terminus with of acetic anhydride (95 muL, 1 mmol) and DIPEA (174 muL, 1 mmol) in DMF (10 mL) for 20 minutes, repeating the cycle twice. (0470) Then, ivDde protecting group on lysine 25 side chain was removed by stirring with 10 mL of a solution of hydrazine 5% w/v in DMF for 20 min as many times as necessary until no starting material could be detected after cleavage of an aliquot part of resin and UPLC/MS analysis. When deprotection was judged complete, resin was washed with DMF (5×10 ml). (0471) Two TTDS spacer units were introduced by single coupling by performing twice the following procedure: To the resin a solution of Fmoc-TTDS-OH (163 mg, 0.3 mmol) HOAt (42 mg, 0.3 mmol) and DIC (77 muL, 0.5 mmol) 7 mL of DMF was added. The syringe was agitated on an orbital table for 18 h. The reaction was monitored by Kaiser Test. When needed, a double coupling was performed. The resin was washed with DMF (2×10 mL). Then to the resin, 10 mL of 20% v/v of piperidine in DMF was added. The syringe was agitated on an orbital table for 20 min. This deprotection procedure was repeated a second time and the resin was washed with DMF (2×10 mL) and dichloromethane (3×10 mL). (0472) The three gamma-glutamic acids spacers were introduced by performing a double coupling of each Fmoc-Glu-OtBu. Thus the following procedure was applied three times: (0473) To the resin a solution (4S)-5-tert-butoxy-4-(9H-fluoren-9-yl methoxy carbonylamino)-5-oxo-pentanoic acid (Fmoc-Glu-OtBu) (127 mg, 0.3 mmol), HOAt (42 mg, 0.3 mmol) and DIC (77 muL, 0.5 mmol) in 7 mL of DMF. The syringe was agitated on an orbital table for 18 h. The reaction was monitored by Kaiser Test. The resin was washed with DMF (2×10 mL). Then to the resin, 10 mL of 20% v/v of piperidine in DMF was added. The syringe was agitated on an orbital table for 20 min. This deprotection procedure was repeated a second time and the resin was washed with DMF (3×10 mL) and dichloromethane (3×30 mL). Finally, the peptide was acylated with Stearoyl chloride (62 mg, 0.2 mmol) and DIPEA (54 muL, 0.3 mmol) in 5 ml DCM for 2.5 h. The resin was washed with DMF (2×30 mL) and dichloromethane (3×30mL) and dried under vacuum. (0475) The cleavage of the peptide from the resin was performed using a solution phenol (0.5 g), water (0.5 mL) and TIPS (0.2 mL) in TFA (QSP 10 mL) for 2.5 hours at room temperature. The resin was filtered off, and washed with 2×4 mL TFA. The combined filtrates were transferred to a 100 mL round bottom flask and partially concentrated under vacuum at T<30 C. and the peptide was precipitated by the addition of 50 mL ice-cold MTBE and centrifuged at 3600 rpm for 30 minutes. (0476) The centrifuged pellet was then washed with ice-cold diethyl ether and centrifuged. This process was repeated three times. 240 g of crude peptide were obtained. Purification was performed using purification system B and fractions containing pure desired peptide were lyophilized. The peptide as trifluoroacetate salt was obtained as a white solid. (0477) m=38 mg (8%) (0478) UPLC/MS: (0479) RT: 5.40 min. (Analytical condition A), purity 97% (UV) (0480) Observed mass m/z (ion type): 1376.1 (M+3H); 1032.0 (M+4H); 826.0 (M+5H). |
Precautionary Statements-General | |
Code | Phrase |
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P103 | Read label before use |
Prevention | |
Code | Phrase |
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Response | |
Code | Phrase |
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P304 | IF INHALED: |
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P321 | |
P322 | |
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P378 | |
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P301 + P312 | IF SWALLOWED: call a POISON CENTER or doctor/physician IF you feel unwell. |
P301 + P330 + P331 | IF SWALLOWED: Rinse mouth. Do NOT induce vomiting. |
P302 + P334 | IF ON SKIN: Immerse in cool water/wrap in wet bandages. |
P302 + P350 | IF ON SKIN: Gently wash with plenty of soap and water. |
P303 + P361 + P353 | IF ON SKIN (or hair): Remove/Take off Immediately all contaminated clothing. Rinse SKIN with water/shower. |
P304 + P312 | IF INHALED: Call a POISON CENTER or doctor/physician if you feel unwell. |
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P304 + P341 | IF INHALED: If breathing is difficult, remove victim to fresh air and keep at rest in a position comfortable for breathing. |
P305 + P351 + P338 | IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continue rinsing. |
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P370 + P380 | In case of fire: Evacuate area. |
P370 + P380 + P375 | In case of fire: Evacuate area. Fight fire remotely due to the risk of explosion. |
P371 + P380 + P375 | In case of major fire and large quantities: Evacuate area. Fight fire remotely due to the risk of explosion. |
Storage | |
Code | Phrase |
P401 | |
P402 | Store in a dry place. |
P403 | Store in a well-ventilated place. |
P404 | Store in a closed container. |
P405 | Store locked up. |
P406 | Store in corrosive resistant/ container with a resistant inner liner. |
P407 | Maintain air gap between stacks/pallets. |
P410 | Protect from sunlight. |
P411 | |
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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