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H-MET-ALA-OH FORMATE is a chemical compound that consists of the amino acids methionine (MET) and alanine (ALA) in a specific sequence, along with a formate group, which is a salt or ester of formic acid. H-MET-ALA-OH FORMATE plays a significant role in peptide synthesis and pharmaceutical research, serving as a building block for creating larger and more complex molecules. It is instrumental in studying protein structure and function, as well as in the development of new drug compounds.

3061-96-9

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3061-96-9 Usage

Uses

Used in Pharmaceutical Research:
H-MET-ALA-OH FORMATE is used as a building block in pharmaceutical research for the synthesis of larger and more complex molecules. Its incorporation into peptide structures aids in the development of new drug compounds, making it a valuable tool for researchers in the field of medicinal chemistry.
Used in Biochemical Research:
In the field of biochemistry, H-MET-ALA-OH FORMATE is utilized to study protein structure and function. Its role in peptide synthesis allows researchers to create and modify peptides for various applications, furthering the understanding of protein interactions and their implications in biological systems.

Check Digit Verification of cas no

The CAS Registry Mumber 3061-96-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,0,6 and 1 respectively; the second part has 2 digits, 9 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 3061-96:
(6*3)+(5*0)+(4*6)+(3*1)+(2*9)+(1*6)=69
69 % 10 = 9
So 3061-96-9 is a valid CAS Registry Number.

3061-96-9SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 13, 2017

Revision Date: Aug 13, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-[(2-amino-4-methylsulfanylbutanoyl)amino]propanoic acid

1.2 Other means of identification

Product number -
Other names L-Methionyl-L-alanin

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:3061-96-9 SDS

3061-96-9Downstream Products

3061-96-9Relevant academic research and scientific papers

Recombinant ribonuclease proteins

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, (2008/06/13)

PCT No. PCT/US97/02588 Sec. 371 Date Feb. 19, 1998 Sec. 102(e) Date Feb. 19, 1998 PCT Filed Feb. 19, 1997 PCT Pub. No. WO97/31116 PCT Pub. Date Aug. 28, 1997The invention relates to ribonucleases derived from a native ribonuclease found in the oocytes of Rana pipiens. Various humanized and recombinant forms of these molecules are described as well as uses for them.

ISOLATION AND CHARACTERIZATION OF AN L-AMINO ACID ACYLASE FROM Aspergillus oryzae

Malinka, M. K.,Stepanov, V. M.,Lobareva, L. S.

, p. 341 - 349 (2007/10/02)

A scheme of isolating a highly purified L-amino acylase from Aspergillus oryzae is described which excludes extraction of the enzyme from the preparation "Amilorizin", fractionation with ethanol, chromatography on DEAE-cellulose, and gel filtration through Sephadex G-200 and Bio-Gel P-300.The enzyme, as purified 1240-fold, has a molecular weight of 118,000, apparently consists of two subunits with a molecular weight of 60,000, is stable in the pH range of 7-10 and has an optimum pH of 8.9 and pI of 4.0.Its amino acid composition has been determined and its substrate specificity has been studied.The acylase is a metalloenzyme: Co2+ ions in concentrations of 10-4-5.10-5 M increase the rate of hydrolysis of N-acetyl-L-amino acids three- to fourfold.It shows differences in its molecular and functional properties from acylase I obtained from porcine kidney.

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