Anti-Aminoacylase 1 Antibody (Rabbit Monoclonal antibody) General Information
Anti-Aminoacylase 1 Antibody
Reacts with: Human
Human Aminoacylase 1
Recombinant Human ACY1 / Aminoacylase-1 protein (Catalog#10549-H08B)
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).
Monoclonal Rabbit IgG Clone #006
0.2 μm filtered solution in PBS
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
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. Avoid repeated freeze-thaw cycles.
Immunofluorescence staining of Human ACY1 in Hela or SKBR3 cells. Cells were fixed with 4% PFA, permeabilzed with 1% Triton X-100 in PBS, blocked with 10% serum, and incubated with Rabbit anti-Human ACY1 monoclonal antibody (1:60). Then cells were stained with the Alexa Fluor® 488-conjugated Goat Anti-rabbit IgG secondary antibody (left panel, captured by laser confocal scanning microscope; right panel, captured by fluorescence microscope), countstained with DAPI (blue). Positive staining was localized to cytoplasm.
Flow cytometric analysis of Human ACY1 expression on HepG2 cells. The cells were treated according to manufacturer’s manual (BD Pharmingen™ Cat. No. 554714), stained with purified anti-Human ACY1, then a FITC-conjugated second step antibody. The fluorescence histograms were derived from gated events with the forward and side light-scatter characteristics of intact cells.
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.
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