B-Raf (E3T5C) Mouse mAb (BSA and Azide Free) #60407
- WB
- IHC
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 86 |
| Source/Isotype | Mouse IgG2a kappa |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
B-Raf (E3T5C) Mouse mAb (BSA and Azide Free) recognizes endogenous levels of total B-Raf protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln356 of human B-Raf protein.
Background
A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites, including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events (11).
- Avruch, J. et al. (1994) Trends Biochem Sci 19, 279-83.
- Chong, H. et al. (2001) EMBO J 20, 3716-27.
- King, A.J. et al. (1998) Nature 396, 180-3.
- Fabian, J.R. et al. (1993) Mol Cell Biol 13, 7170-9.
- Mason, C.S. et al. (1999) EMBO J 18, 2137-48.
- Zimmermann, S. and Moelling, K. (1999) Science 286, 1741-4.
- Sprenkle, A.B. et al. (1997) FEBS Lett 403, 254-8.
- Marais, R. et al. (1997) J Biol Chem 272, 4378-83.
- Guan, K.L. et al. (2000) J Biol Chem 275, 27354-9.
- Davies, H. et al. (2002) Nature 417, 949-54.
- Dougherty, M.K. et al. (2005) Mol Cell 17, 215-24.
Limited Uses
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