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Manufactured by BioVendor

Aminoacylase-1 Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:ACY-1, N-acyl-L-amino-acid amidohydrolase, ACY1
  • Species:Human
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Cat. No. Size Price

RD172406100 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 416 AA. MW: 47.0 kDa (calculated). UniProtKB Q03154 (Met1-Ser408). C-terminal His-tag (8 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence



E. coli


Purity as determined by densitometric image analysis: > 95%


14 % SDS-PAGE separation of Human Aminoacylase-1:
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and boiled sample, 2.5 μg/lane
3. non-reduced and non-boiled sample, 2.5 μg/lane


< 1.0 EU/ug


Filtered (0.4 μm) and lyophilized in phosphate buffered saline, pH 7.5.


Add 200 µl of deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.


Western blotting, ELISA


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic

Cardiovascular disease, Neural tissue markers, Renal disease, Reproduction, Transplantation


Aminoacylase-1 (ACY-1, N-acyl-L-amino-acid amidohydrolase) belongs to the M20 family of metalloproteases. It is a 408-amino-acid protein with a molecular weight of 45.8 KDa which catalyzes the hydrolysis of N-acetylated amino acids into the free amino acid and acetic acid. ACY-1 plays a general role in the cytosolic breakdown of acetylated amino acids generated during intracellular protein degradation. The gene encoding ACY-1 is evolutionarily conserved in fish, frog, mouse, rat and human.The expression of ACY-1 is highest in the kidney and brain. Aminoacylase-1 is a potential biomarker of long-term outcome after kidney transplantation. Significant differences in serum ACY-1 levels were apparent between delayed, slow and immediate graft function. ACY-1 was not detected in the majority of patients before transplantation and remained low in recipients of live-donor kidneys. Serum ACY-1 levels were increased significantly in the majority of patients with delayed graft function (DGF), but rose in only a minority of patients with immediate function. These analyses provide novel insights into the potential clinical utility of serum ACY-1 levels immediately post kidney transplation, enabling subdivision of patients with delayed graft function in terms of long-term outcome. Serum ACY-1 concentration was high in patients with tubular cell damage due to ischemia-reperfusion injury (IRI) and/ or acute tubular necrosis. ACY-1 also interacts with sphingosine kinase type 1, which is involved in promoting cell growth and inhibiting apoptosis of tumor cells. ACY-1 plays a role in regulating responses of the cell to oxidative stress. ACY-1 serves as a putative suppressor in renal cell carcinoma and small cell lung cancer. ACY-1 expression is also significantly correlated with serum alpha fetoprotein level and tumor invasiveness. It was also demonstrated that ACY-1 acts as a tumor suppresor in hepatocellular carcinoma. An enzymatic deficiency in ACY-1 may result in defects of brain metabolism and function, such as encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features (e.g. fever). Epileptic seizures are a frequent feature in these patients. ACY-1 deficiency has also been described as an inborn error of metabolism. This disorder was identified in children who have increased urinary excretion of N-acetylamino acids.

Summary References (9)

References to Aminoacylase-1

  • Ali S, Sheerin NS. Biomarkers of acute injury: predicting the long-term outcome after transplantation. Kidney Int. 2013 Dec;84 (6):1072-4
  • Baumeier C, Kaiser D, Heeren J, Scheja L, John C, Weise C, Eravci M, Lagerpusch M, Schulze G, Joost HG, Schwenk RW, Schurmann A. Caloric restriction and intermittent fasting alter hepatic lipid droplet proteome and diacylglycerol species and prevent diabetes in NZO mice. Biochim Biophys Acta. 2015 May;1851 (5):566-76
  • Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Menard R. Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family. J Biol Chem. 2003 Nov 7;278 (45):44496-504
  • Lindner HA, Tafler-Naumann M, Rohm KH. N-acetylamino acid utilization by kidney aminoacylase-1. Biochimie. 2008 May;90 (5):773-80
  • Long PM, Stradecki HM, Minturn JE, Wesley UV, Jaworski DM. Differential aminoacylase expression in neuroblastoma. Int J Cancer. 2011 Sep 15;129 (6):1322-30
  • Maceyka M, Nava VE, Milstien S, Spiegel S. Aminoacylase 1 is a sphingosine kinase 1-interacting protein. FEBS Lett. 2004 Jun 18;568 (1-3):30-4
  • Sommer A, Christensen E, Schwenger S, Seul R, Haas D, Olbrich H, Omran H, Sass JO. The molecular basis of aminoacylase 1 deficiency. Biochim Biophys Acta. 2011 Jun;1812 (6):685-90
  • Wei X, Li J, Xie H, Ling Q, Wang J, Lu D, Zhou L, Xu X, Zheng S. Proteomics-based identification of the tumor suppressor role of aminoacylase 1 in hepatocellular carcinoma. Cancer Lett. 2014 Aug 28;351 (1):117-25
  • Welberry Smith MP, Zougman A, Cairns DA, Wilson M, Wind T, Wood SL, Thompson D, Messenger MP, Mooney A, Selby PJ, Lewington AJ, Banks RE. Serum aminoacylase-1 is a novel biomarker with potential prognostic utility for long-term outcome in patients with delayed graft function following renal transplantation. Kidney Int. 2013 Dec;84 (6):1214-25
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