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145038-52-4

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145038-52-4 Usage

General Description

FMOC-ASP-OME, also known as Fmoc-L-aspartic acid 4-methyl ester, is a chemical compound commonly used in peptide synthesis and organic chemistry research. It is a derivative of aspartic acid with an FMOC (9-fluorenylmethoxycarbonyl) protecting group on the amine group and an OME (methoxycarbonyl) protecting group on the carboxyl group. FMOC-ASP-OME is often used as a building block for the synthesis of aspartic acid-containing peptides and can be incorporated into complex peptide structures. FMOC-ASP-OME is soluble in organic solvents and is commercially available for research and laboratory use.

Check Digit Verification of cas no

The CAS Registry Mumber 145038-52-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,5,0,3 and 8 respectively; the second part has 2 digits, 5 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 145038-52:
(8*1)+(7*4)+(6*5)+(5*0)+(4*3)+(3*8)+(2*5)+(1*2)=114
114 % 10 = 4
So 145038-52-4 is a valid CAS Registry Number.
InChI:InChI=1/C20H19NO6/c1-26-18(22)10-17(19(23)24)21-20(25)27-11-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,16-17H,10-11H2,1H3,(H,21,25)(H,23,24)/t17-/m0/s1

145038-52-4SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name (S)-3-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-4-methoxy-4-oxobutanoic acid

1.2 Other means of identification

Product number -
Other names (3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methoxy-4-oxobutanoic acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:145038-52-4 SDS

145038-52-4Downstream Products

145038-52-4Relevant articles and documents

Synthesis of chlorophyll-amino acid conjugates as models for modification of proteins with chromo/fluorophores

Tamiaki, Hitoshi,Isoda, Yasuaki,Tanaka, Takuya,Machida, Shinnosuke

, p. 1421 - 1428 (2014)

A chlorophyll-a derivative bonded directly with epoxide at the peripheral position of the chlorin π-system was reacted with N-urethane and C-ester protected amino acids bearing an alcoholic or phenolic hydroxy group as well as a carboxy group at the residue to give chlorophyll-amino acid conjugates. The carboxy residues of N,C-protected aspartic and glutamic acids were esterified with the epoxide in high yields. The synthetic conjugates in dichloromethane had absorption bands throughout the visible region including intense red-side Qy and blue-side Soret bands. By their excitation at the visible bands, strong and efficient fluorescence emission was observed up to the near-infrared region. The chromo/fluorophores are promising for preparation of functional peptides and modification of proteins.

Hydantoin and thiohydantoin derivatives as antiviral drugs

-

Paragraph 0280-0281, (2013/12/03)

The present invention relates to a compound of the following formula (I), or a salt, solvate, tautomer, enantiomer, diastereoisomer or racemic mixture thereof: as well as its use as a drug, notably in the treatment of hepatitis C, its preparation process, and the pharmaceutical compositions containing such a compound.

Design and preparation of serine-threonine protein phosphatase inhibitors based upon the nodularin and microcystin toxin structures. Part 3

Webster,Maude,O'Donnell,Mehrotra,Gani

, p. 1673 - 1695 (2007/10/03)

Nodularin and microcystins are complex natural cyclic isopeptidic hepatotoxins that serve as subnanomolar inhibitors of the eukaryotic serine-threonine protein phosphatases PP1 and PP2A, enzymes that are intimately involved in controlling cellular metabolism. Previously we described a solution-phase synthesis of stripped-down nodularin analogues; cyclo[-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)-Asp-α-OMe- β-(S)-Phe-] 3 and cyclo[-(3R)-3-hydroxymethyl-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)- Asp-α-OMe-β-(S)-Phe-] 5. The synthetic strategy was designed to allow post-macrocyclisation elaboration. Here we examine alternative methods for introducing diversity and achieving macrolactamisation and compare the relative efficiency of solution- vs. solid-phase peptide syntheses of the macrocycles. Syntheses and the biological activities of the macrocycles cyclo{-[(2R)-α-4-benzylpiperidinylamido-Asp]-β-[(R)-Glu]-γ- Sar-[(R)-Asp]-β-(S)-Phe-} 29 and cyclo{-(2S)-Phe-[(2R)-α-4-benzylpiperidinylamido-Asp]-(R)-Glu-γ- (S)-Pro-β-(R)-Asp-} 65 are compared. Both compounds contain sufficient side-chain functionality to interact with a hydrophobic groove at the enzyme active site. The proline containing analogues 30, 31 (R3 = CH3) where sarcosine is replaced in macrocycles 3 and 4, were also synthesised in order to correlate conformational properties with biological activity. In accord with predictions macrocycles 29 and 65 were found to be weak inhibitors of PP1 with IC50 2.9 and 2.7 mM respectively.

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