Exalpha Biologicals, Inc.

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Exalpha Biologicals, Inc. is now a US distributor for Nordic-Mubio products

Nordic-MUbio develops and manufactures high quality antibody reagents for use in R&D. All our products are manufactured according to strict ISO 9001 quality guidelines, and our focus is on developing antibodies targetting Cell Adhesion, Nuclear and Cytoskeletal Proteins.

Nordic-MUbio is one of the leading antibody companies developing antibodies for zebrafish research – we currently have over 50 antibodies validated for immunofluorescence in zebrafish.

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Akazawa, Y., et al. "Endoplasmic Reticulum Stress Contributes to Helicobacter Pylori VacA-Induced Apoptosis" PLoS ONE 8(12): e82322

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Homa, N.J., et al. "Epstein-Barr Virus Induces Global Changes in Cellular mRNA Isoform Usage That Are Important for the Maintenance of Latency" J. Virol., 2013, 87, 12291-12301

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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

Synonyms

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

Host/Source

Rabbit

Isotype

N/A

Product Type

Polyclonal Antibody

Reactivity

Human

Applications

Western Blot, ELISA

Purification

Ammonium Sulfate Precipitation

Size

100 µg

Price (USD)

$355

Background

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).

Immunogen

Synthetic peptide derived from human acid sphingomyelinase protein.

Formulation

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

69851

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:

SwissProtP17405Human

References

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).