Fmoc-Glu-OAllCAS# 144120-54-7 |
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Quality Control & MSDS
Number of papers citing our products
Chemical structure
3D structure
| Cas No. | 144120-54-7 | SDF | Download SDF |
| PubChem ID | 7020606 | Appearance | Powder |
| Formula | C23H23NO6 | M.Wt | 409.4 |
| Type of Compound | N/A | Storage | Desiccate at -20°C |
| Solubility | Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc. | ||
| Chemical Name | (4S)-4-(9H-fluoren-9-ylmethoxycarbonylamino)-5-oxo-5-prop-2-enoxypentanoic acid | ||
| SMILES | C=CCOC(=O)C(CCC(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13 | ||
| Standard InChIKey | ORKKMGRINLTBPC-FQEVSTJZSA-N | ||
| Standard InChI | InChI=1S/C23H23NO6/c1-2-13-29-22(27)20(11-12-21(25)26)24-23(28)30-14-19-17-9-5-3-7-15(17)16-8-4-6-10-18(16)19/h2-10,19-20H,1,11-14H2,(H,24,28)(H,25,26)/t20-/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. | ||
Fmoc-Glu-OAll Dilution Calculator
Fmoc-Glu-OAll Molarity Calculator
| 1 mg | 5 mg | 10 mg | 20 mg | 25 mg | |
| 1 mM | 2.4426 mL | 12.213 mL | 24.426 mL | 48.852 mL | 61.065 mL |
| 5 mM | 0.4885 mL | 2.4426 mL | 4.8852 mL | 9.7704 mL | 12.213 mL |
| 10 mM | 0.2443 mL | 1.2213 mL | 2.4426 mL | 4.8852 mL | 6.1065 mL |
| 50 mM | 0.0489 mL | 0.2443 mL | 0.4885 mL | 0.977 mL | 1.2213 mL |
| 100 mM | 0.0244 mL | 0.1221 mL | 0.2443 mL | 0.4885 mL | 0.6106 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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Solid-phase synthesis of peptide-4-nitroanilides.[Pubmed:8956082]
Int J Pept Protein Res. 1996 Nov;48(5):486-94.
A wide variety of Glu/Asp and Gln containing peptide-4-nitroanilides and other chromogenic peptidyl-arylamides could be quickly synthesized by a Fmoc-based solid-phase synthesis strategy employing the side-chain carboxyl groups for transient anchoring to the resin. Suitable synthons for this method, Fmoc-Glu-NH-Np and Fmoc-Asp-NH-Np, were prepared using a diphenylphosphinic chloride-mediated coupling reaction. Peptides of the common structure Suc-Ala-Phe-Pro-Xaa-NH-Np (Xaa = Glu/Asp, Gln) were synthesized and were shown to be substrates for the protease subtilisin Carlsberg (E.C.3.4.21.14a) and for peptidyl-prolyl cis/trans-isomerases (PPIases E.C. 5.2.1.8.). The method was extended to amino acids possessing a side chain missing an anchor for binding to the matrix. We synthesized Suc-Ala-Phe-Pro-Gln-Phe-NH-Np anchoring the dipeptide derivative Fmoc-Glu-Phe-NH-Np with the carboxyl group to Rink amide resin using standard SPPS procedures. Additionally this procedure allowed us the preparation of peptidyl-arylamides, utilizing the commercial available Fmoc-Glu-OAll as building block. A mixture of pentapeptide-4-nitroanilides with the general sequence Ala-Ala-Xaa-Pro-Gln-NH-Np was synthesized. Electrospray ionization mass spectrometry (ESI-MS) was used to evaluate the hydrolysis of the peptide mixture by the protease subtilisin Carlsberg. It could be shown that peptides with the hydrophobic amino acids Phe, Tyr, Leu and Val in the varied P3-position were most rapidly cleaved under the chosen conditions. Hydrolysis of the Gln-NH-Np bond in Ala-Ala-Pro-Pro-Gln-NH-Np has not been observed.
