9012-37-7[HH].[HH].[HH]ULGJWNIHLSLQPZ-UHFFFAOYSA-N9012-37-7Safety information is for reference only and does not replace the supplier’s Safety Data Sheet (SDS), applicable regulations, or professional assessment.
Danger
H315 (88.9%): Causes skin irritation [Warning Skin corrosion/irritation]
P233, P260, P261, P264, P264+P265, P271, P280, P284, P302+P352, P304+P340, P305+P351+P338, P319, P321, P332+P317, P337+P317, P342+P316, P362+P364, P403, P403+P233, P405, and P501 (click each P-code to see the statement)
Aggregated GHS information provided per 45 reports by companies from 4 notifications to the ECHA C&L Inventory. Each notification may be associated with multiple companies.
XU - indicates a substance exempt from reporting under the Chemical Data Reporting Rule, (40 CFR 711).
Aminoacylase: Does not have an individual approval but may be used under an appropriate group standard
DescriptionAminoacylase-1 (EC 3.5.1.14) is a homodimeric zinc-binding metalloenzyme. A cytosolic enzyme with a wide range of tissue expression, it cleaves acylated L-amino acids (except L-aspartate) into L-amino acids and an acyl group. L-aspartate derivatives are cleaved by aminoacylase-2 (aspartoacylase). Aminoacylase-1 is the most abundant of the aminoacylases, a class of enzymes involved in hydrolysis of N-acetylated proteins.
UsesAcylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues . Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids .
General DescriptionAcylase I belongs to the aminoacylase family of enzymes.
No reaction records under the current filter.
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