Catalogue

Background
Sphingomyelin synthases are enzymes that mediate the biosynthesis of sphingolipid headgroups. Sphingomyelin synthase 1 and 2 (SMS1 and SMS2) mediate the biosynthesis of sphingomyelin, a central sphingolipid in mammalian cells. In addition to SMS1 and SMS2, a third SMS-related protein, SMSr, is known, however its function remains largely unknown. SMSr also occurs in organisms which lack sphingomyelin, such as the fruit fly Drosophila melanogaster. Its function appears to be biosynthesis of ethanolamine phosphorylceramide (EPC), a sphingolipid structurally related to sphingomyelin. SMSr has also been found in mammals as well.

Synonyms: SMSr

Source

Immunogen: Recombinant SMSr derived from Drosophila .

Product

Product Form: Unconjugated

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

Purification Method: Ammonium Sulfate Precipitation

Concentration: See vial for concentration

Applications
Optimal concentration should be evaluated by serial dilutions.

Functional Analysis: Western Blotting

Positive Control: Recombinant sphingomelin synthase protein

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

Product Stability: See expiration date on vial

Shipping Conditions: Ship at ambient temperature, freeze upon arrival

Caution
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. It may contain hazardous ingredients. Please refer to the Safety Data Sheets (SDS) for additional information and proper handling procedures. Dispose product remainders according to local regulations.This datasheet is as accurate as reasonably achievable, but Nordic-MUbio​ accepts no liability for any inaccuracies or omissions in this information.

References
1: Dickson, R. C. (1998) Annu. Rev. Biochem. 67, 27–48 2: Pewzner-Jung, Y., Ben-Dor, S., and Futerman, A. H. (2006) J. Biol. Chem. 281, 25001–25005 3: Mandon, E. C., Ehses, I., Rother, J., van Echten, G., and Sandhoff, K. (1992) J. Biol. Chem. 267, 11144–11148 4: Jeckel, D., Karrenbauer, A., Burger, K. N., van Meer, G., and Wieland, F. (1992) J. Cell Biol. 117, 259–267 5: Futerman, A. H., Stieger, B., Hubbard, A. L., and Pagano, R. E. (1990) J. Biol. Chem. 265, 8650–8657 6: Huitema, K., van den Dikkenberg, J., Brouwers, J. F., and Holthuis, J. C. (2004) EMBO J. 23, 33–44 7: Yamaoka, S., Miyaji, M., Kitano, T., Umehara, H., and Okazaki, T. (2004) J. Biol. Chem. 279, 18688–18693 8: Ullman, M. D., and Radin, N. S. (1974) J. Biol. Chem. 249, 1506–1512 9: Voelker, D. R., and Kennedy, E. P. (1982) Biochemistry 21, 2753–2759 10: van Helvoort, A., van't Hof, W., Ritsema, T., Sandra, A., and van Meer, G. (1994) J. Biol. Chem. 269, 1763–1769 11: Muehlenberg, B. A., Sribney, M., and Duffe, M. K. (1972) Can J. Biochem. 50, 166–173 12: Hannun, Y. A., and Obeid, L. M. (2002) J. Biol. Chem. 277, 25847–25850 13: Wiegmann, K., Schutze, S., Machleidt, T., Witte, D., and Kronke, M. (1994) Cell 78, Spiegel, S., and Milstien, S. (2003) Nat. Rev. Mol. Cell Biol. 4, 397–407 14: Ogretmen, B., and Hannun, Y. A. (2004) Nat. Rev. Cancer 4, 604–616 15: Holthuis, J. C., Pomorski, T., Raggers, R. J., Sprong, H., and Van Meer, G. (2001) Physiol. Rev. 81, 1689–1723

Protein Reference(s)

Database Name: UniProt

Accession Number: Q9VS60

Species Accession: Human

Safety Datasheet(s) for this product: