Rabbit Polyclonal PE2(phospho-Thr526) Antibody

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     Western blot analysis of PE2 (phospho-Thr526) expression in HEK293, MCF7, mouse lung, rat lung whole cell lysates.    

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     Immunofluorescent analysis of PE2 (phospho-Thr526) staining in HeLa cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PBS and incubated overnight at 4 C in a hidified chamber. Cells were washed with PBST and incubated with a DyLight 594-conjugated secondary antibody (red) in PBS at room temperature in the dark.    

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     Immunohistochemical analysis of PE2 (phospho-Thr526) staining in human ovarian cancer formalin fixed paraffin embedded tissue section. The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.    

**Background of the PE2 (phospho-Thr526) Antibody**

The PE2 (phospho-Thr526) antibody is a specialized tool designed to detect the phosphorylated form of a protein at threonine residue 526. Phosphorylation at Thr526 is often associated with the activation or functional modulation of signaling proteins involved in DNA damage response, cell cycle regulation, or stress signaling pathways. For instance, this modification may occur in kinases or adaptor proteins (e.g., members of the ATM/ATR or MAPK cascades) that relay signals to maintain genomic stability or coordinate cellular adaptation to stress.

This antibody is commonly used in research to study phosphorylation-dependent protein interactions, signaling dynamics, or dysregulation in diseases like cancer, where aberrant phosphorylation can drive proliferation or survival. It is validated for techniques such as Western blotting, immunofluorescence, or immunoprecipitation, often in human, mouse, or rat models. Specificity is confirmed using knockout controls or phosphatase-treated samples.

Understanding Thr526 phosphorylation provides insights into mechanisms of cellular responses to DNA damage, therapeutic resistance, or targeted drug development. Studies leveraging this antibody may explore how post-translational modifications at this site influence protein stability, localization, or enzymatic activity in physiological and pathological contexts.