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Commit: 461ca8d8fe5b1efd4c01fc87e5b5eb592e2d154a
XML generation date: 2025-03-07 13:15:59.098
Product last modified at: 2025-03-27T14:15:10.559Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

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

Filter:
  • IHC
Immunohistochemistry Image 1: B-Raf (V600E Mutant) (IHC600) Mouse mAb
Immunohistochemical analysis of paraffin-embedded human thyroid carcinoma using B-Raf (V600E Mutant) (IHC600) Mouse mAb performed on the Leica® BOND™ Rx. Mutational status was confirmed by genomic sequencing.

To Purchase # 29002

Cat. # Size Qty. Price
29002S 100 µl
$411

Supporting Data

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

Product Information

Product Usage Information

Application Dilution
IHC Leica Bond 1:100 - 1:400
Immunohistochemistry (Paraffin) 1:100 - 1:400

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).

Pathways

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