epitope corresponding to amino acids 25-65 mapping near the N-terminus of Acid Ceramidase of human origin
Modification Notes
Acid ceramidase catalyzes the degradation of ceramide in normal tissues, and deficiency leads to accumulation of ceramide in tissues, a hallmark of Farber disease. Effected individuals experience early onset joint problems and neurological problems, owing to mutations in the acid ceramidase gene. Bioinformatic analysis of gene expression also reveals acid ceramidase to be among the 5 most important genes associated with melanoma. In addition to ceramide hydrolysis, purified acid ceramidase also exhibits the ability to catalyze ceramide synthesis, utilizing [14C]lauric acid and sphingosine as substrates. Interestingly, pH regulates which reaction is favored; for hydrolysis the pH optimum is 4.5, whereas for the reverse reaction favors a pH of 5.5, further supporting a complex and central role for acid ceramidase in sphingolipid metabolism.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Acid Ceramidase of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including bovine and porcine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 25-65 mapping near the N-terminus of Acid Ceramidase of human origin
Tissue Specificity
epitope corresponding to amino acids 25-65 mapping near the N-terminus of Acid Ceramidase of human origin
Western blot analysis of Acid Ceramidase expression in HeLa whole cell lysate.
Application Notes
recommended for detection of Acid Ceramidase of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including bovine and porcine:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.