|Application ||WB, IHC-P, IF, E|
|Other Accession||EAW63795, 427|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||44660 Da|
|Application Notes||ASAH1 antibody can be used for detection of ASAH1 by Western blot at 1 and 2 μg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 μg/mL. For immunofluorescence start at 20 μg/mL.|
|Target/Specificity||ASAH1 antibody was raised against a 16 amino acid synthetic peptide near the carboxy terminus of the human ASAH1.|
The immunogen is located within amino acids 240 - 290 of ASAH1.
|Reconstitution & Storage||ASAH1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||ASAH1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.|
|Tissue Location||Broadly expressed with highest expression in heart|
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Provided below are standard protocols that you may find useful for product applications.
ASAH1 Antibody: Sphingolipids are hydrolyzed by ceramidases to yield sphingosine and fatty acids. These ceramidases are classified according to the pH range that supports their optimal activity. ASAH1 is an acid ceramidase and key regulator of ceramide metabolism. Mutations in this gene results in Farber Lipogranulomatosis, a fatal human genetic disorder that results in the painful swelling of the joints and tendons and pulminary insufficiency, while a complete knockout of its expression is lethal in mice. Recent studies have shown elevated levels of ASAH1 in Alzheimer's disease (AD) patients correlating with a reduction in sphingomyelin and elevation of ceramide. Pretreatment of cultured neurons with recombinant AHAH1 prevented the cells from undergoing A-beta (Ab)-induced apoptosis.
Nilsson A and Duan RD. Alkaline sphingomyelinases and ceramidases of the gastrointestinal tract. Chem. Phys. Lipids 1999; 102:97-105.
Koch J, Gartner S, Li CM, et al. Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification of the first molecular lesion causing Farber’s disease. J. Biol. Chem. 1996; 271:33110-5.
Li CM, Park JH, Simonaro CM, et al. Insertional mutagenesis of the mouse acid ceramidase gene leads to early embryonic lethality in homozygotes and progressive lipid storage disease in heterozygotes. Genomics 2002; 79:218-24.
He X, Huang Y, Li B, et al. Deregulation of sphingolipid metabolism in Alzheimer’s disease. Neurobiol. Aging 2010; 31:398-408.
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