Recombinant Mouse ACY1 / Aminoacylase-1 Protein (His tag)

Recombinant Mouse ACY1 / Aminoacylase-1 Protein (His tag)

PKSM040921

Regular price $732.00 $593.00 You Pay

Supplier: Elabscience Product Name: Recombinant Mouse ACY1 / Aminoacylase-1 Protein (His tag) Catalog No. PKSM040921 Product Type: recombinant protein Size: 50 ug Activity: Measured by its ability to cleave N-acetyl-L-Methione (Ac-Met). The specific activity is >4,000 pmoles/min/?g. Protein Construction: A DNA sequence encoding the mouse ACY1 (Q99JW2) (Met 1-Ser 408) was expressed with a C-terminal polyhistidine tag. Sequence: Met 1-Ser 408 Fusion Tag: C-His Accession: Q99JW2 Species: Mouse Expressed Host: HEK293 Cells Shipping Conditions: In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Purity: > 95 % as determined by SDS-PAGE Endotoxin: < 1.0 EU per ?g of the protein as determined by the LAL method Stability: Samples are stable for up to twelve months from date of receipt at -70?.Store it under sterile conditions at -20? to -80?. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. Molecular Weight: 45 kDa Applied MM: 45 kDa Formulation: Lyophilized from sterile PBS, pH 7.4 Reconstitution: Please refer to the printed manual for detailed information. Background: 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.