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BRAF [F-7]

Product group: Primary
Monoclonal/ Polyclonal: Monoclonal
Clone: F-7
Host: Mouse
Isotype: IgG2a
Application: ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB)
Application notes: 50-250
Conjugation Type: Unconjugated
Reactivity: Human, Mouse, Rat
General notes: Localization: cytoplasm.
Buffer: citrate pH6.0 or EDTA pH8.0
UNSPSC code: 12352203

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-A, a second member of the Raf gene family of serine/threonine protein kinases, exhibits substantial homology to Raf-1 within the kinase domain of the two molecules, but less homology elsewhere. Expression of Raf-B is highly restricted with highest levels in the cerebrum and testis (Shipping Cost: €200.00)

BRAF [F-7]

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-A, a second member of the Raf gene family of serine/threonine protein kinases, exhibits substantial homology to Raf-1 within the kinase domain of the two molecules, but less homology elsewhere. Expression of Raf-B is highly restricted with highest levels in the cerebrum and testis