Render Target: STATIC
Render Timestamp: 2024-12-02T11:11:00.829Z
Commit: cd2fae6ca3f811b1ddb1df24ac291ed56d5d501b
XML generation date: 2024-07-11 16:01:08.088
Product last modified at: 2024-11-14T13:15:31.068Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

B-Raf (V600E Mutant) (IHC600) Mouse mAb #29002

Filter:
  • IHC

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Mouse IgG2b kappa
    Application Key:
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    IHC Leica Bond 1:50 - 1:200
    Immunohistochemistry (Paraffin) 1:50 - 1:200

    Storage

    Supplied in a Tris-based buffer with 1% BSA and less than 0.1% sodium azide. Stable for 24 months when stored at 4°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    B-Raf (V600E Mutant) (IHC600) Mouse mAb recognizes the V600E mutant of B-Raf protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a peptide covering the V600E mutation.

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