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Anti-B-Raf (S446) [C-Raf (S338)/A-Raf (S299)], Phosphospecific Antibody
![- Anti-B-Raf (S446) [C-Raf (S338)/A-Raf (S299)], Phosphospecific Antibody AN1932](/assets/uploads/products/202310/Braf_Nterm_S446_86e7698a-66a8-46fc-b0ce-b527419bb452_1600x.jpg)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P15056 |
|---|---|
| Reactivity | Bovine |
| Host | Rabbit |
| Clonality | Rabbit Polyclonal |
| Isotype | IgG |
| Calculated MW | 84437 Da |
| Gene ID | 673 |
|---|---|
| Storage | Maintain 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. |
| Precautions | Anti-B-Raf (S446) [C-Raf (S338)/A-Raf (S299)], Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
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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