Product Name :
Rabbit anti Drosophila Sphingomyelin synthase-related protein 1
Description :
| Isotype IgG | Product Type Polyclonal Antibody | Units 100 µg | Host Rabbit | Species Reactivity Drosophila | Application Western Blotting
Background :
Immunogen: Recombinant SMSr derived from Drosophila .
Source :
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 <
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
Specificity :
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 our company accepts no liability for any inaccuracies or omissions in this information.
References :
1: Dickson, R. C. (1998) Annu. Rev. Biochem. 67, 27–482: Pewzner-Jung, Y., Ben-Dor, S., and Futerman, A. H. (2006) J. Biol. Chem. 281, 25001–250053: Mandon, E. C., Ehses, I., Rother, J., van Echten, G., and Sandhoff, K. (1992) J. Biol. Chem. 267, 11144–111484: Jeckel, D., Karrenbauer, A., Burger, K. N., van Meer, G., and Wieland, F. (1992) J. Cell Biol. 117, 259–2675: Futerman, A. H., Stieger, B., Hubbard, A. L., and Pagano, R. E. (1990) J. Biol. Chem. 265, 8650–86576: Huitema, K., van den Dikkenberg, J., Brouwers, J. F., and Holthuis, J. C. (2004) EMBO J. 23, 33–447: Yamaoka, S., Miyaji, M., Kitano, T., Umehara, H., and Okazaki, T. (2004) J. Biol. Chem. 279, 18688–186938: Ullman, M. D., and Radin, N. S. (1974) J. Biol. Chem. 249, 1506–15129: Voelker, D. R., and Kennedy, E. P. (1982) Biochemistry 21, 2753–275910: van Helvoort, A., van’t Hof, W., Ritsema, T., Sandra, A., and van Meer, G. (1994) J. Biol. Chem. 269, 1763–176911: Muehlenberg, B. A., Sribney, M., and Duffe, M. K. (1972) Can J. Biochem. 50, 166–17312: Hannun, Y. A., and Obeid, L. M. (2002) J. Biol. Chem. 277, 25847–2585013: 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, 397–40714: Ogretmen, B., and Hannun, Y. A. (2004) Nat. Rev. Cancer 4, 604–61615: Holthuis, J. C., Pomorski, T., Raggers, R. J., Sprong, H., and Van Meer, G. (2001) Physiol. Rev. 81, 1689–1723
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