Sphingosine Kinase 2 (N-terminal region) Blocking Peptide
€155.00
In stock
SKU
ECM-SX4625
Background:
Sphingolipids are metabolized into bioactive products that include ceramide, sphingosine, and sphingosine-1-phosphate (S1P). Sphingosine Kinase (SK) catalyzes the phosphorylation of the lipid sphingosine, creating S1P. S1P subsequently signals through cell surface G protein-coupled receptors, as well as intracellularly, to modulate cell proliferation, survival, motility and differentiation. Two isoforms of SK have been identified, SK1 and SK2. The mRNA for both of these isoforms is widely expressed with SK1 expression highest in brain, heart, kidney, thymus, spleen and lung, while SK2 is highest in kidney and liver. SKs can be activated through growth factor, G protein-coupled, and immunoglobulin receptor signalling. Regulation of SK1 and SK2 activity may occur through phosphorylation. SK1 is phosphorylated at Ser-225 by ERK leading to increased activity and translocation to the plasma membrane. SK2 is phosphorylated in response to EGF, PKC activators, and phorbol esters. ERK1 can phosphorylate both Ser-351 and Thr-578, and non-phosphorylatable mutants of these sites suppress ERK1-mediated chemotaxis.
Sequence: SK2 (N-terminal region) synthetic peptide corresponding to amino acid residues in the N-terminal region of human SK2. This peptide sequence is highly conserved in rat and mouse SK2 proteins, and has no homology to SK1.
Specificity: The peptide is specifically recognized by anti-SK2 (N-terminal region) antibody (SP4621) in ELISA, and has been shown to block the reactivity of SP4621 during Western blot. In addition, the peptide is recommended for use in blocking SP4621 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Sphingolipids are metabolized into bioactive products that include ceramide, sphingosine, and sphingosine-1-phosphate (S1P). Sphingosine Kinase (SK) catalyzes the phosphorylation of the lipid sphingosine, creating S1P. S1P subsequently signals through cell surface G protein-coupled receptors, as well as intracellularly, to modulate cell proliferation, survival, motility and differentiation. Two isoforms of SK have been identified, SK1 and SK2. The mRNA for both of these isoforms is widely expressed with SK1 expression highest in brain, heart, kidney, thymus, spleen and lung, while SK2 is highest in kidney and liver. SKs can be activated through growth factor, G protein-coupled, and immunoglobulin receptor signalling. Regulation of SK1 and SK2 activity may occur through phosphorylation. SK1 is phosphorylated at Ser-225 by ERK leading to increased activity and translocation to the plasma membrane. SK2 is phosphorylated in response to EGF, PKC activators, and phorbol esters. ERK1 can phosphorylate both Ser-351 and Thr-578, and non-phosphorylatable mutants of these sites suppress ERK1-mediated chemotaxis.
Sequence: SK2 (N-terminal region) synthetic peptide corresponding to amino acid residues in the N-terminal region of human SK2. This peptide sequence is highly conserved in rat and mouse SK2 proteins, and has no homology to SK1.
Specificity: The peptide is specifically recognized by anti-SK2 (N-terminal region) antibody (SP4621) in ELISA, and has been shown to block the reactivity of SP4621 during Western blot. In addition, the peptide is recommended for use in blocking SP4621 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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