Ac-Trp-OHCAS# 1218-34-4 |
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Quality Control & MSDS
Number of papers citing our products
Chemical structure
3D structure
| Cas No. | 1218-34-4 | SDF | Download SDF |
| PubChem ID | 700653 | Appearance | Powder |
| Formula | C13H14N2O3 | M.Wt | 246.3 |
| Type of Compound | N/A | Storage | Desiccate at -20°C |
| Synonyms | N-Acetyl-L-tryptophan;Acetyl-L-tryptophan;acetyltryptophan | ||
| Solubility | Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc. | ||
| Chemical Name | (2S)-2-acetamido-3-(1H-indol-3-yl)propanoic acid | ||
| SMILES | CC(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)O | ||
| Standard InChIKey | DZTHIGRZJZPRDV-LBPRGKRZSA-N | ||
| Standard InChI | InChI=1S/C13H14N2O3/c1-8(16)15-12(13(17)18)6-9-7-14-11-5-3-2-4-10(9)11/h2-5,7,12,14H,6H2,1H3,(H,15,16)(H,17,18)/t12-/m0/s1 | ||
| General tips | For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months. We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months. Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it. |
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| About Packaging | 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial. 2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial. 3. Try to avoid loss or contamination during the experiment. |
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| Shipping Condition | Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request. | ||
Ac-Trp-OH Dilution Calculator
Ac-Trp-OH Molarity Calculator
| 1 mg | 5 mg | 10 mg | 20 mg | 25 mg | |
| 1 mM | 4.0601 mL | 20.3004 mL | 40.6009 mL | 81.2018 mL | 101.5022 mL |
| 5 mM | 0.812 mL | 4.0601 mL | 8.1202 mL | 16.2404 mL | 20.3004 mL |
| 10 mM | 0.406 mL | 2.03 mL | 4.0601 mL | 8.1202 mL | 10.1502 mL |
| 50 mM | 0.0812 mL | 0.406 mL | 0.812 mL | 1.624 mL | 2.03 mL |
| 100 mM | 0.0406 mL | 0.203 mL | 0.406 mL | 0.812 mL | 1.015 mL |
| * Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations. | |||||
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Kinetics of enzyme attack on substrates covalently attached to solid surfaces: influence of spacer chain length, immobilized substrate surface concentration and surface charge.[Pubmed:18817422]
Langmuir. 2008 Oct 21;24(20):11762-9.
The use of alpha-chymotrypsin to cleave covalently bound N-acetyl- l-tryptophan (Ac-Trp-OH) from the surfaces of aminopropylated controlled pore glass (CPG) and the polymer PEGA 1,900 was investigated. Oligoglycine spacer chains were used to present the covalently attached Ac-Trp-OH substrate to the aqueous enzyme. In the absence of the oligoglycine spacer chain, the rate of release was relatively slow, especially from the PEGA 1,900. These slow rates reflect the position of the amino group to which Ac-Trp-OH is covalently attached. On the glass there was a clear optimum with a chain of four glycine residues. For PEGA 1,900 there is no real apparent change beyond two glycine residues. The decline in rate beyond these optima are a possible result of changes in oligoglycine structure. Comparing different surface loadings of bound substrate the rate of release of Ac-Trp-OH from CPG with a pore diameter of 1,200 A was optimal when using 83% of the maximum that can be coupled, then fell again at higher loading. The rate of Ac-Trp-OH release from CPG was the same for surface coverages of 0.4 and 1.0. The introduction of permanent surface charges on CPG 1,200 exhibits a distinct influence on enzymatic cleavage with an increase in the rate of biocatalysis at the surface. Optimal presentation of covalently immobilized substrate on different supports by use of appropriate linkers leads to favorable biocatalysis from the support.
