Exalpha Biologicals, Inc.

Product Highlight

FIX&PERM Cell Fixation and Permeabilization Kit

Flow cytometric analyses with monoclonal antibodies were so far mainly restricted to cell surface molecules. Intracellular structures such as cytoplasmic or nuclear enzymes, oncoproteins, cytokines, immunoglobulins etc. were largely excluded from such studies. Also excluded from flow cytometric studies were cytoplasmic localizations of well-established membrane molecules like CD3 and CD22, which, in their cytoplasmic form, are the most reliable lineage markers in undifferentiated leukemia. With the FIX&PERM® Kit flow cytometric analysis of intracellular antigens has become as easy as surface antigen studies. The only prerequisite is the availability of suitable antibody conjugates. Most of the available monoclonal antibody conjugates can be used with the FIX&PERM® Kit, some determinants are sensitive, however, to the fixation step involved. This and the optimal fixation time have to be tested for each reagent.


Welcome, Peter Rutten

We are pleased to announce that Peter Rutten has now started in his role as Operations Director here at Exalpha Biologicals Inc. Peter has a Master’s of Science degree in Industrial and Organizational Psychology and this has lead him down a very business orientated career path. Peter is looking forward to working with the team at Exalpha. Peters primary focus is the customer experience and he will be working with the Laboratory team, the Quality Control team and the Order Processing team to ensure this focus is achieved. We all wish Peter well in his new role.

Exalpha Biologicals, Inc.

Acid Sphingomyelinase

  • Product Code: X1695P
  • Size: 100 µg
  • Availability: In Stock In Stock
  • Price (USD): $355

Cat #

X1695P		 Quantity:      

Data Sheet

Product Name

Acid Sphingomyelinase


Acid Sphingomyelinase, aSMase, SMPD1, ASM, Sphingomyelin phosphodiesterase, ASM-1





Product Type

Polyclonal Antibody




Western Blot, ELISA


Ammonium Sulfate Precipitation


100 µg

Price (USD)



Human acid sphingomyelinase (sphingomyelin phosphodiesterase, ASM) is the lysosomal enzyme responsible for the hydrolysis of sphingomyelin to ceramide and phosphocholine. Converts sphingomyelin to ceramide. aSM also has phospholipase C activities toward 1,2-diacylglycerol-phosphocholine and 1,2-diacylglycerol-phosphoglycerol. The enzyme is a membrane-associated glycoprotein with a pH optimum of about 4.5 and a subunit molecular mass of about 72 kDa. In addition AtoS M, two other sphingomyelinases have been identified in man, a Mg2+- dependent neutral sphingomyelinase found primarily in brain and a Zn2+-dependent acid sphingomyelinase found primarily in serum. Although it is likely that the acid and neutral sphingomyelinases are coded by different genes, the molecular genetic relationship of these three biochemically distinct sphingomyelinases has not been determined. Understanding the role of these sphingomyelinases in the hydrolysis of sphingomyelin to ceramide will be an important step in the understanding of ceramide as it is further hydrolyzed to sphingosine, a neutral phospholipid which has been implicated in the regulation of protein kinase C-mediated signal transduction. Inherited deficiencies of ASM have been reported in man, deficient ASM activity results in the two major subtypes of Niemann-Pick disease (NPD).


Synthetic peptide derived from human acid sphingomyelinase protein.


Provided as solution in phosphate buffered saline with 0.08% sodium azide

Customer Storage

Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight


Product Image

Image Legend

Western blot analysis using acid sphingomyelinase antibody on normal human brain lysate (7 µg/lane). Antibody used at 1 µg/ml (1) and 0.5 µg/ml (2) and detected using mouse anti-rabbit antibody (Cat. No. X1207M) at 1:75k dilution and visualized using Pierce West Femto substrate.

Database Links:



1. Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs.;
Schuchman E.H., Suchi M., Takahashi T., Sandhoff K., Desnick R.J.; J. Biol. Chem. 266:8531-8539(1991).

2. Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene.; Newrzella D., Stoffel W.; Biol. Chem. Hoppe-Seyler 373:1233-1238(1992).

3. Cloning of a human acid sphingomyelinase cDNA with a new mutation that renders the enzyme inactive.; Ida H., Rennert O.M., Eto Y., Chan W.Y.; J. Biochem. 114:15-20(1993).

4. Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts.; Quintern L.E., Schuchman E.H., Levran O., Suchi M., Ferlinz K., Reinke H., Sandhoff K., Desnick R.J.; EMBO J. 8:2469-2473(1989).

5. Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis.; Ferlinz K., Hurwitz R., Moczall H., Lansmann S., Schuchman E.H., Sandhoff K.; Eur. J. Biochem. 243:511-517(1997).

6. Human acid sphingomyelinase.; Lansmann S., Schuette C.G., Bartelsen O., Hoernschemeyer J., Linke T., Weisgerber J., Sandhoff K.;Eur. J. Biochem. 270:1076-1088(2003).