Active • Host: Insect cells • AA: 22-395 • Tag: N-terminal His • MW: 44 kDa
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Acid Ceramidase (human, recombinant)

Item No. 31491

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • AC
  • ACDase
  • N-Acylethanolamine Hydrolase ASAH1
  • N-Acylsphingosine Amidohydrolase
  • Acylsphingosine Deacylase
  • ASAH1
  • PHP32
  • Putative 32 kDa Heart Protein
Purity
≥65% estimated by SDS-PAGE
Source
Active recombinant human N-terminal His-tagged AC expressed in insect cells
Amino Acids
22-395
MW
30kDa β-subunit, 13 kDa α-subunit
Formulation (Request formulation change)
1x PBS, pH 7.2, 0.02% Triton X-100, 20% glycerol
Host
Insect cells
UniProt Accession №
Q13510
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $605

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    Product Description

    Acid ceramidase (AC) is a hydrolase and member of the N-terminal nucleophile superfamily of hydrolases.1,2 It is initially expressed as a proenzyme, which undergoes autocleavage at the peptide bond between threonine 142 and cysteine 143 to produce the active enzyme.3 AC is composed of an α-subunit domain and a β-subunit domain linked by a disulfide bond.1,3 It is ubiquitously expressed and located in the lysosome.3 AC is involved in sphingolipid degradation and hydrolyzes ceramides into sphingolipids and free fatty acids.4 Mutations in ASAH1, the gene encoding AC, are found in patients with Farber disease or spinal muscular atrophy with progressive myoclonic epilepsy (SMA-PME).2,5 Cayman's Acid Ceramidase (human, recombinant) protein can be used for enzyme activity assay, ELISA, and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Gebai, A., Gorelik, A., Li, Z., et al. Structural basis for the activation of acid ceramidase. Nat. Commun. 9(1), 1621 (2018).

    2. Momoi, T., Ben-Yoseph, Y., and Nadler, H.L. Substrate-specificities of acid and alkaline ceramidases in fibroblasts from patients with Farber disease and controls. Biochem. J. 205(2), 419-425 (1982).

    3. Ferlinz, K., Kopal, G., Bernardo, K., et al. Human acid ceramidase. Processing, glycosylation, and lysosomal targeting. The Journal of Biological Chemisty 276(38), 35352-35360 (2001).

    4. Zeidan, Y.H., Jenkins, R.W., Korman, J.B., et al. Molecular targeting of acid ceramidase: Implications to cancer therapy. Curr. Drug Targets 9(8), 653-661 (2008).

    5. Yu, F.P.S., Amintas, S., Levade, T., et al. Acid ceramidase deficiency: Farber disease and SMA-PME. Orphanet J. Rare Dis. 13(1), 121 (2018).

    Product Citations

    Nobumoto, W., Naganuma, T., Nozaka, N., et al. Acid ceramidase ASAH1 is a key regulator of epidermal ceramide levels and composition. The Journal of Biological Chemisty 302(3), 111178 (2026).