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AB189399

Anti-ACY-1 antibody

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(2 Publications)

Rabbit Polyclonal ACY-1 antibody. Suitable for WB, IHC-P, ICC/IF and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human Aminoacylase-1 aa 50-350.

View Alternative Names

Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, ACY1

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ACY-1 antibody (AB189399)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-ACY-1 antibody (AB189399)

Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human kidney tissue, labeling ACY-1 using ab189399 at 10 μg/ml.

Immunocytochemistry/ Immunofluorescence - Anti-ACY-1 antibody (AB189399)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-ACY-1 antibody (AB189399)

Immunofluorescence analysis of paraformaldehyde-fixed A431 cells labeling ACY-1 using ab189399 at a 1/200 dilution (upper panel) and merged with DNA probe (lower panel)

Western blot - Anti-ACY-1 antibody (AB189399)
  • WB

Supplier Data

Western blot - Anti-ACY-1 antibody (AB189399)

All lanes:

Western blot - Anti-ACY-1 antibody (ab189399) at 1/1000 dilution

All lanes:

H1299 whole cell lysate at 30 µg

Predicted band size: 46 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF, IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human Aminoacylase-1 aa 50-350. The exact immunogen used to generate this antibody is proprietary information.

Q03154

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/3000", "WB-species-notes": "<p></p>", "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "10 µg/mL", "IHCP-species-notes": "<p></p>", "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/100 - 1/200", "ICCIF-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 10% Glycerol (glycerin, glycerine), 1.79% Tris glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein ACY-1 also known as aminoacylase 1 or ACY plays a significant role in the deacetylation process of N-acyl amino acids. ACY-1 is a zinc-binding enzyme and has a molecular weight of approximately 45 kDa. This enzyme is expressed in various tissues including the liver and kidney. ACY-1 is essential for amino acid metabolism by catalyzing the hydrolysis of N-acyl-L-amino acids into L-amino acids and free fatty acids.
Biological function summary

The aminoacylase 1 enzyme functions in detoxification and metabolic regulation. It is not typically part of large protein complexes but acts independently to regulate amino acid and acetyl-CoA pathways. The activity facilitates the recycling of acyl groups and amino acids which is important for maintaining cellular homeostasis.

Pathways

Aminoacylase 1 is involved in amino acid catabolism and lipid metabolism pathways. In these processes ACY-1 interacts with proteins such as acetyl-CoA synthetase in the conversion of excess acyl-CoAs into free fatty acids and CoA preventing the build-up of toxic metabolites. It also has an indirect relationship with the urea cycle by ensuring the availability of free amino acids for further metabolism.

Alterations in ACY-1 function relate to neurological disorders and metabolic syndromes. For instance defects in ACY-1 have been associated with Canavan disease a condition affecting the brain. The protein's activity imbalance might also link to metabolic disorders where its interaction with proteins like aspartoacylase comes into play further affecting the acetylation status and metabolic regulation.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalyzes the hydrolysis of N-acetylated amino acids to acetate and free amino acids.
See full target information Aminoacylase-1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

American journal of cancer research 15:363-374 PubMed39949934

2025

Overexpression of SHANK2 contributes malignant outcomes as a Hippo pathway regulator in gastric cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Hiroshi Arakawa,Shuhei Komatsu,Jun Kiuchi,Taisuke Imamura,Keiji Nishibeppu,Hajime Kamiya,Yusuke Takashima,Ryo Ishida,Satoshi Hamada,Masateru Yamauchi,Takuma Ohashi,Hiroki Shimizu,Tomohiro Arita,Hirotaka Konishi,Atsushi Shiozaki,Takeshi Kubota,Hitoshi Fujiwara,Hitoshi Tsuda,Eigo Otsuji

The Journal of clinical investigation 135: PubMed39808494

2025

Impaired hydrogen sulfide biosynthesis underlies eccentric contraction-induced force loss in dystrophin-deficient skeletal muscle.

Applications

Unspecified application

Species

Unspecified reactive species

W Michael Southern,Erynn E Johnson,Elizabeth K Fasbender,Katherine S Fallon,Courtney L Cavazos,Dawn A Lowe,George G Rodney,James M Ervasti
View all publications

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