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1949-51-5

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1949-51-5 Usage

General Description

ETHYL 3,5-DIAMINOBENZOATE, also known as ethyl-3,5-diaminobenzoate or ethyl 3,5-diaminobenzoate, is a chemical compound that is used in the production of hair dyes and other cosmetic products. It is a white crystalline solid that is soluble in water and has a faint odor. Ethyl 3,5-diaminobenzoate is a mild skin and eye irritant and should be handled with care. It is commonly used as a colorant in cosmetic products, but it can also be found in pharmaceuticals and other industrial applications. Due to its potential for skin irritation, it is important to use products containing ethyl 3,5-diaminobenzoate with caution and follow the recommended usage guidelines.

Check Digit Verification of cas no

The CAS Registry Mumber 1949-51-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,9,4 and 9 respectively; the second part has 2 digits, 5 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 1949-51:
(6*1)+(5*9)+(4*4)+(3*9)+(2*5)+(1*1)=105
105 % 10 = 5
So 1949-51-5 is a valid CAS Registry Number.
InChI:InChI=1/C9H12N2O2/c1-2-13-9(12)6-3-7(10)5-8(11)4-6/h3-5H,2,10-11H2,1H3

1949-51-5Relevant articles and documents

Factors influencing the activity of nanozymes in the cleavage of an RNA model substrate

Czescik, Joanna,Zamolo, Susanna,Darbre, Tamis,Mancin, Fabrizio,Scrimin, Paolo

supporting information, (2019/08/08)

A series of 2-nm gold nanoparticles passivated with different thiols all featuring at least one triazacyclonanone-Zn(II) complex and different flanking units (a second Zn(II) complex, a triethyleneoxymethyl derivative or a guanidinium of arginine of a peptide) were prepared and studied for their efficiency in the cleavage of the RNA-model substrate 2-hydroxypropyl-p-nitrophenyl phosphate. The source of catalysis for each of them was elucidated from the kinetic analysis (Michaelis–Menten profiles, pH dependence and kinetic isotope effect). The data indicated that two different mechanisms were operative: One involving two Zn(II) complexes and the other one involving a single Zn(II) complex and a flanking guanidinium cation. The mechanism based on a dinuclear catalytic site appeared more efficient than the one based on the cooperativity between a metal complex and a guanidinium.

Molecular design and synthesis of artificial ion channels based on cyclic peptides containing unnatural amino acids

Ishida,Qi,Sokabe,Donowaki,Inoue

, p. 2978 - 2989 (2007/10/03)

A series of novel cyclic peptides composed of 3 to 5 dipeptide units with alternating natural-unnatural amino acid units, have been designed and synthesized, employing 5-(N-alkanoylamino)-3-aminobenzoic acid with a long alkanoyl chain as the unnatural amino acid. All cyclic peptides with systematically varying pore size, shape, and lipophilicity are found to form ion channels with a conductance of ca. 9 pS in aqueous KCl (500 mM) upon examination by the voltage clamp method. These peptide channels are cation selective with the permeability ratio PCl-/PK+ of around 0.17. The ion channels formed by the neutral, cationic, and anionic cyclic peptides containing L-alanine, L-lysine, and L-aspartate, respectively, show the monovalent cation selectivity with the permeability ratio PNa+/PK+ of ca. 0.39. On the basis of structural information provided by voltage-dependent blockade of the single channel current of all the tested peptides by Ca2+, we inferred that each channel is formed from a dimer of the peptide with its peptide ring constructing the channel entrance and its alkanoyl chains lining across the membrane to build up the channel pore. The experimental results are consistent with an idea that the rate of ion conduction is determined by the nature of the hydrophobic alkanoyl chain region, which is common to all the channels.

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