Sphingosine Kinase 2 (N Terminal HIS Tag) - Active Enzyme


Catalog number


Full name

Sphingosine Kinase 2 (N Terminal HIS Tag) - Active Enzyme


10 μg


426.00 €

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Proteins & Peptides

Long description

Sphingosine Kinase 2 (Sphk2) catalyzes the phosphorylation of sphingosine to sphingosine 1-phosphate (S1P), an important signaling molecule with intra- and extracellular functions. Inside the cell S1P acts as a signaling molecule like other sphingolipid metabolites like ceramide and sphingosine. S1P has been implicated in regulating cell differentiation, calcium mobilization from intracellular stores, and apoptosis. The cell surface receptors for S1P are the EDG family of G protein-coupled receptors (S1P Receptors). These receptors couple to multiple G proteins (e.g. S1P1 couples to Gi whereas S1P2 and S1P3 couple to Gq, G13 in addition to Gi) and regulate a extremely wide raange of cellular events including cell motility, survival, apoptosis, migration and cell-cell interaction. Important roles for S1P have also been reported in regulation of cardiogenesis, vascular maturation, oocyte survival, immune cell trafficking, cells of the neuronal system and bone cells. S1P levels are regulated by the activity of Sphk (Sphk1 and Sphk2).

Antibody come from

Hybridoma produced by the fusion of splenocytes from mice immunized with a keratin isolated from the human breast carcinoma cell line MCF-7 and mouse myeloma cells.

Other description

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


not specified

Antigen-antibody binding interaction

Sphingosine Kinase 2 (N Terminal HIS Tag) - Active Enzyme

Antibody is raised in

Sf9 cells

Antibody's reacts with


Antibody's reacts with these species

This antibody doesn't cross react with other species

Antibody's specificity

No Data Available


Study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Antibody's suited for

Antibody can be used for immunoblotting (1:100-1:1000), immunocytochemistry, immunohistochemistry on frozen tissue sections (1:100-1:200) and flow cytometry. Optimal concentration should be evaluated by serial dilutions.



Relevant references

1. Van Muijen, G. N., et al. (1987). Coexpression of intermediate filament polypeptides in human fetal and adult tissues, Lab Invest 57, 359-69._x000B_2. Van Muijen, G. N., et al. (1987). Differentiation-related changes of cytokeratin expression in cultured keratinocytes and in fetal, newborn, and adult epidermis, Exp Cell Res 171, 331-45._x000B_3. Schaafsma, H. E., et al. (1989). Distribution of cytokeratin polypeptides in epithelia of the adult human urinary tract, Histochemistry 91, 151-9._x000B_4. Smedts, F., et al. (1990). Changing patterns of keratin expression during progression of cervical intraepithelial neoplasia, Am J Pathol 136, 657-68._x000B_5. Ramaekers, F., et al. (1990). Use of monoclonal antibodies to keratin 7 in the differential diagnosis of adenocarcinomas, Am J Pathol 136, 641-55._x000B_6. Schaafsma, H. E., et al. (1990). Distribution of cytokeratin polypeptides in human transitional cell carcinomas, with special emphasis on changing expression patterns during tumor progression, Am J Pathol 136, 329-43._x000B_7. Ivanyi, D., et al. (1990). Keratin subtypes in carcinomas of the uterine cervix: implications for histogenesis and differential diagnosis, Cancer Res 50, 5143-52._x000B_8. Wetzels, R. H., et al. (1991). Basal cell-specific and hyperproliferation-related keratins in human breast cancer, Am J Pathol 138, 751-63._x000B_9. Ku, N. O., et al. (2001). Keratin 8 mutations in patients with cryptogenic liver disease, N Engl J Med 344, 1580-7._x000B_10. Waseem, A., Karsten, U., Leigh, I.M., Purkis, P., Waseem, H. and Lane, B. (2004). Conformational changes in the rod domain of human keratin 8 following heterotypic association with keratin 18 and its implication for filament stability. Biochemistry 43, 1283-95.

Protein number

see ncbi


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. This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.


Enzymes are cleaving the substrate. If the substrate is DNA they are called restriction enzymes. Activating enzymes will cut off the domain that is biological active to become functional.