
Katalognummer: 665 - STJ91363
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 200 µl
A02159S646
Boster Bio Anti-Phospho-Rad17 (S646) Antibody catalog # A02159S646. Tested in ELISA, WB applications. This antibody reacts with Human, Mouse, Rat.
A02159S645
Boster Bio Anti-Phospho-Rad17 (S645) Antibody catalog # A02159S645. Tested in ELISA, WB applications. This antibody reacts with Human, Mouse.
ET1612-75
Several serine/threonine protein kinases have been implicated as intermediates in signal transduction pathways. These include ERK/MAP kinases, ribosomal S6 kinase (Rsk)and Raf-1. Raf-1 is a cytoplasmic protein with intrinsic serine/threonine activity. It is broadly expressed in nearly all cell lines tested to date and is the cellular homolog of v-Raf, the product of the transforming gene of the 3611 strain of murine sarcoma virus. The unregulated kinase activity of the v-Raf protein has been associated with transformation and mitogenesis while the activity of Raf-1 is normally suppressed by a regulatory N-terminal domain. Raf-1 is activated in response to activation of a variety of tyrosine kinase receptors as well as in response to pp60v-Src expression. There is accumulating evidence that Ras p21 may play a role in activation of Raf-1 and may play the role of the messenger from membrane tyrosine kinases to Raf-1.
ET1612-87
Raf-1 is a ubiquitously expressed cytoplasmic protein with intrinsic serine/threonine kinase activity. Raf-1, or c-Raf, is the cellular homolog of v-Raf, the product of the transforming gene of the 3611 strain of murine sarcoma virus. The unregulated kinase activity of the v-Raf protein is associated with cellular transformation and mitogenesis. Raf-1 is normally suppressed by its regulatory N-terminal domain. Raf-1 is activated in response to a variety of tyrosine kinase receptors as well as in response to pp60v-Src expression. Specifically, Raf-1 is phosphorylated in the catalytic domain at Ser 338 and, to a lesser extent, Ser 339. This phosphorylation requires the co-activation of PI 3-kinase and the Ras signaling pathway. Raf-1 is also phosphorylated on Tyr 340 and 341, which induces the phosphorylation of MEK. Phosphorylation of Ser 621 is essential for the catalytic activity of Raf-1 and downregulation by c-AMP-dependent protein kinase A (PKA). PKA also phosphorylates Raf-1 on Ser 43 and Ser 259. PKA phosphorylation of Ser 259 inhibits Raf-1 and decreases the phosphorylation necessary for Raf-1 activation at Ser 338.
ET1701-3
Raf-1 is a ubiquitously expressed cytoplasmic protein with intrinsic serine/threonine kinase activity. Raf-1, or c-Raf, is the cellular homolog of v-Raf, the product of the transforming gene of the 3611 strain of murine sarcoma virus. The unregulated kinase activity of the v-Raf protein is associated with cellular transformation and mitogenesis. Raf-1 is normally suppressed by its regulatory N-terminal domain. Raf-1 is activated in response to a variety of tyrosine kinase receptors as well as in response to pp60v-Src expression. Specifically, Raf-1 is phosphorylated in the catalytic domain at Ser 338 and, to a lesser extent, Ser 339. This phosphorylation requires the co-activation of PI 3-kinase and the Ras signaling pathway. Raf-1 is also phosphorylated on Tyr 340 and 341, which induces the phosphorylation of MEK. Phosphorylation of Ser 621 is essential for the catalytic activity of Raf-1 and downregulation by c-AMP-dependent protein kinase A (PKA). PKA also phosphorylates Raf-1 on Ser 43 and Ser 259. PKA phosphorylation of Ser 259 inhibits Raf-1 and decreases the phosphorylation necessary for Raf-1 activation at Ser 338.

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