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L-Glutamic acid, 5-(1,1-dimethylethyl) 1-methyl ester is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

53838-27-0

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53838-27-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 53838-27-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,3,8,3 and 8 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 53838-27:
(7*5)+(6*3)+(5*8)+(4*3)+(3*8)+(2*2)+(1*7)=140
140 % 10 = 0
So 53838-27-0 is a valid CAS Registry Number.

53838-27-0SDS

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 5-O-tert-butyl 1-O-methyl (2S)-2-aminopentanedioate

1.2 Other means of identification

Product number -
Other names AmbotzHAA6700

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:53838-27-0 SDS

53838-27-0Relevant articles and documents

Method for synthesizing glutamic acid-1-methyl ester-5-tert-butyl ester

-

, (2019/04/13)

The invention discloses a method for synthesizing glutamic acid-1-methyl ester-5-tert-butyl ester. The method comprises the following steps: generating dimethyl glutamate by using glutamic acid as aninitial raw material in methyl alcohol under the effect of thionyl chloride; reacting the dimethyl glutamate with triphenylchloromethane to generate dimethyl glutamate with triphenylmethyl protected amino; taking off methyl ester on the 5 position of the dimethyl glutamate with triphenylmethyl protected amino under the effect of sodium hydroxide to generate triphenylmethyl-glutamic acid-1-methyl ester; reacting the triphenylmethyl-glutamic acid-1-methyl ester-5-tert-butyl ester with trichloroacetic imine tert-butyl ester to generate triphenylmethyl-glutamic acid-1-methyl ester-5-tert-butyl ester, adding a small amount of triisopropylsilane into the triphenylmethyl-glutamic acid-1-methyl ester-5-tert-butyl ester in a low-concentration dichloromethane trifluoroacetate solution to take off triphenylmethyl to generate the glutamic acid-1-methyl ester-5-tert-butyl ester. The method is simple in operation, has few byproduct which can be extremely easy to treat and high product yield, and cansolve the problem of large operation difficulty in an existing synthesizing method.

Simple and efficient Fmoc removal in ionic liquid

Di Gioia,Costanzo,De Nino,Maiuolo,Nardi,Olivito,Procopio

, p. 36482 - 36491 (2017/08/02)

A mild method for an efficient removal of the fluorenylmethoxycarbonyl (Fmoc) group in ionic liquid was developed. The combination of a weak base such as triethylamine and [Bmim][BF4] makes the entire system more efficient for the cleavage at room temperature of various amines and amino acid methyl esters in short reaction times. The procedure works well even in the case of N-Fmoc amino acids bearing acid-sensitive protecting groups and of N-alkylated amino acid methyl esters. The solvent-free condition provides a complementary method for Fmoc deprotection in solution phase peptide synthesis and modern organic synthesis.

Synthesis and immunomodulating activity of new glycopeptides of glycyrrhizic acid containing residues of L-glutamic acid

Kondratenko,Baltina Jr.,Baltina,Baschenko,Tolstikov

, p. 595 - 601 (2008/02/08)

New glycopeptides of glycyrrhizic acid (GA) containing Glu residues and their α-methyl esters, γ-methyl esters, and α,γ-dimethyl esters were synthesized using N,N′-dicyclohexylcarbodiimide in the presence of N-hydroxybenzotriazole or N-hydroxysuccinimide.

Compounds which inhibit leukocyte adhesion mediated by VLA-4

-

, (2008/06/13)

Disclosed as compounds which bind VLA-4. Certain of these compounds also inhibit leukocyte adhesion and, in particular, leukocyte adhesion mediated by VLA-4. Such compounds are useful in the treatment of inflammatory diseases in a mammalian patient, e.g., human, such as asthma, Alzheimer's disease, atherosclerosis, AIDS dementia, diabetes, inflammatory bowel disease, rheumatoid arthritis, tissue transplantation, tumor metastasis and myocardial ischemia. The compounds can also be administered for the treatment of inflammatory brain diseases such as multiple sclerosis.

TBAT-mediated nitrone formation of ω-mesyloxy-O-tert-butyldiphenylsilyloximes: Facile synthesis of cyclic nitrones from hemiacetals

Tamura, Osamu,Toyao, Atsushi,Ishibashi, Hiroyuki

, p. 1344 - 1346 (2007/10/03)

Chiral and cyclic nitrones were synthesized by TBAT-mediated desilylative cyclization of ω-mesyloxy-O-tert-butyl-diphenylsilyloximes, readily prepared from sugar derivatives by a consecutive treatment with O-tert-butyldiphenylsilylhydroxylamine and with m

A New Acidic Amino Acid from a Basidiomycetes, Lactarius piperatus

Fushiya, Shinji,Watari, Fumie,Tashiro, Takashi,Kusano, Genjiro,Nozoe, Shigeo

, p. 1366 - 1370 (2007/10/02)

A new acidic amino acid was isolated from a Basidiomycetes, Lactarius piperatus (Fr.) S.F.GRAY.The structure of this compound has been determined as 2(S),3'(S)-1-(3-amino-3-carboxypropyl)-5-oxo-2-pyrrolidinecarboxylic acid (1) on the basis of nuclear magn

Methotrexate Analogues. 14. Synthesis of New γ-Substituted Derivatives as Dihydrofolate Reductase Inhibitors and Potential Anticancer Agents

Rosowsky, Andre,Forsch, Ronald,Uren, Jack,Wick, Michael

, p. 1450 - 1455 (2007/10/02)

The γ-tert-butyl ester (1), γ-hydrazide (2), γ-n-butylamide (3), and γ-benzylamide (4) derivatives of methotrexate (MTX) were synthesized from 4-amino-4-deoxy-N10-methylpteroic acid (APA) and the appropriate blocked L-glutamic acid precursors with the aid of the peptide bond forming reagent diethyl phosphorocyanidate.The affinity of these side chain modified products for dihydrofolate reductase (DHFR) from Lactobacillus casei and L1210 mouse leukemic cells was determined spectrophotometrically or by competitive radioligand binding assay, and their cytotoxicity was evaluated against L1210 leukemic cells in culture.The results provide continuing support for the view that the "γ-terminal region" of the MTX side chain is an attractive site for molecular modification of this anticancer agent.

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