>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Theoretical MW
70 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
70-85 kDa, reducing conditions
Publications
Read Publication using 5298-SK in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -70 °C as supplied.
3 months, -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl, Glycerol and DTT.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Sphingosine Kinase 2/SPHK2 Protein, CF
EC 2.7.1.91
SK 2
SK2
sphingosine kinase 2
sphingosine kinase type 2 isoform
SPHK2
SPK 2
SPK2
Background
Sphingosine kinases catalyze the phosphorylation of sphingosine to sphingosine-1-phosphate, a lipid messenger molecule involved in the regulation of processes such as growth, differentiation, and cellular migration (1). Two types of sphingosine kinases, SPHK1 and SPHK2, are known to be expressed in human cells. The two enzymes share considerable amino acid sequence similarity, but differ in their N-terminal and central regions (2). The two proteins also differ in tissue distribution and some kinetic properties (2). Sphingosine kinases can be either cytosolic or membrane-associated. Differences in the distribution of SPHK1 and SPHK2 within cells may be the cause of differences that have been observed in the function of the two enzymes, particularly their roles in apoptosis (3).
Spiegel, S. (1999) J. Leukocyte Biol. 65:341.
Liu, H. et al. (2000) J. Biol. Chem. 275:19513.
Maceyka, M. et al. (2005) J. Biol. Chem. 280:37118.
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