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Anti-B-Raf (N-terminus) Antibody

     
  • 1 - Anti-B-Raf (N-terminus) Antibody AN1931
    Western blot of human Jurkat cells treated with calyculin A (100 nM) for 30 min. The blots were untreated (lanes 1 & 3) or treated (lanes 2 & 4) with lambda phosphatase and probed with anti-B-Raf (N-terminus) (lanes 1 & 2) or anti-B-Raf (Ser-446) (lanes 3 & 4).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P15056
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 84437 Da
Additional Information
Gene ID 673
Other Names Serine/threonine-protein kinase B-raf, 2.7.11.1, Proto-oncogene B-Raf, p94, v-Raf murine sarcoma viral oncogene homolog B1, BRAF (HGNC:1097), BRAF1, RAFB1
Dilution WB~~1:1000
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-B-Raf (N-terminus) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

The Ras-Raf-MAP kinase signaling pathway is involved in control of cell proliferation and differentiation. The Raf kinase family includes A-Raf, B-Raf, and C-Raf. Each family member has three highly conserved regions (CR1-3). The N-terminal CR1 contains the Ras-GTP-binding domain. The CR2 contains a negative regulatory serine residue (C-Raf (S259)/B-Raf(S365)) that may bind 14-3-3 proteins. The CR3 is the catalytic domain that contains phosphorylation sites for Raf-regulating enzymes within two segments, the N-region and the activation segment. Activation of C-Raf involves phosphorylation at many sites including Ser-338, Tyr-341, and multiple catalytic domain sites. In B-Raf, multiple phosphorylation sites have been identified, but their specific roles are uncertain. Phosphorylation of Ser-446 may prime B-Raf for activation, and Ser-446 and/or Ser-447 phosphorylation may be critical for B-Raf biological activity during PC12 differentiation. Ser-579 is required for growth factor activation and kinase activity. Thus, multiple sites of phosphorylation within Rafs may be important for regulation of their activity.

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