|Recombinant Human ACY1 / Aminoacylase-1 protein (Catalog#10549-H08B)|
|0.2 μm filtered solution in PBS with 5% trehalose|
|This antibody was obtained from a rabbit immunized with purified, recombinant Human ACY1 / Aminoacylase-1 (rh ACY1 / Aminoacylase-1; Catalog#10549-H08B; NP_000657.1; Met1-Ser408).|
|Human ACY1 / Aminoacylase-1|
|ICC/IF, IF, FCM|
FCM: 0.5-2 μg/Test
ICC/IF: 10-25 μg/mL
|This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.|
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Aminoacylase 1 (ACY1), a metalloenzyme that removes amide-linked ACY1 groups from amino acids and may play a role in regulating responses to oxidative stress. Both the C-terminal fragment found in the two-hybrid screen and full-length ACY1 co-immunoprecipitate with SphK1. Though both C-terminal and full-length proteins slightly reduce SphK1 activity measured in vitro, the C-terminal fragment inhibits while full-length ACY1 potentiates the effects of SphK1 on proliferation and apoptosis. It suggested that ACY1 physically interacts with SphK1 and may influence its physiological functions. As a homodimeric zinc-binding enzyme, Aminoacylase 1 catalyzes the hydrolysis of N alpha-acylated amino acids. Deficiency of Aminoacylase 1 due to mutations in the Aminoacylase 1 (ACY1) gene follows an autosomal-recessive trait of inheritance and is characterized by accumulation of N-acetyl amino acids in the urine.