Rabbit anti Drosophila Sphingomyelin synthase-related protein 1
CAT:
579-X1861P
Size:
100 µg
Price:
Ask
- Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
- Dry Ice Shipment: No

Rabbit anti Drosophila Sphingomyelin synthase-related protein 1
- 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
- UniProt: Q9VS60
- Host: Rabbit
- Isotype: IgG
- Conjugation: Unconjugated
- Type: Polyclonal Antibody
- Applications: WB
- Field of Research: Lipid Mediators
- Purification Method: Ammonium Sulfate Precipitation
- Assay Principle: Optimal concentration should be evaluated by serial dilutions.
- Stability: See expiration date on vial
- Concentration: See vial for Concentration
- Form: Provided as solution in phosphate buffered saline with 0,08% sodium azide
- Precautions: 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.
- References & Citations: 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
- Shipping Conditions: Ambient Temperature, freeze upon arrival
- Storage Conditions: Product should be stored at -20ºC; Aliquot to avoid freeze/thaw cycles
- Functional Analysis: WB