EPHA7 Antibody

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Description

Introduction to EPHA7 Antibody

EPHA7 Antibody is a research reagent designed to detect the EphA7 receptor, a member of the Ephrin receptor family (EphA subclass), which plays a critical role in cell signaling, tumor suppression, and developmental processes . The antibody is widely used in molecular biology techniques such as Western blotting (WB), immunoprecipitation (IP), and immunohistochemistry (IHC) to study EphA7 expression, phosphorylation, and functional mechanisms in cancer, neural development, and angiogenesis .

Key Applications of EPHA7 Antibody

2.1. Tumor Research
EPHA7 Antibody has been instrumental in identifying EphA7 as a tumor suppressor in prostate cancer (PCa), follicular lymphoma (FL), and glioblastoma multiforme (GBM) . For example, studies using this antibody demonstrated that EphA7 downregulation correlates with adverse outcomes in GBM patients and is a target of 6q deletions in FL .

2.2. Signaling Pathway Analysis
The antibody has been used to study ligand-dependent EphA7 phosphorylation, particularly at tyrosine residue Y791, which inhibits tumor cell migration and invasion via PI3K/Akt pathway modulation .

2.3. Neural Development Studies
In developmental biology, EPHA7 Antibody has been employed to investigate EphA7’s role in neural tube closure and progenitor cell apoptosis .

Research Findings Highlighted by EPHA7 Antibody

4.1. Tumor Suppression Mechanisms

  • Prostate Cancer: Ligand-dependent EphA7 signaling inhibits tumor growth by inducing apoptosis and blocking PI3K/Akt signaling .

  • Follicular Lymphoma: EPHA7 acts as a soluble tumor suppressor, blocking oncogenic EphA2 signaling, with therapeutic potential when fused to anti-CD20 antibodies .

  • Glioblastoma: Overexpression of EphA7 correlates with high microvessel density (MVD) and poor survival outcomes .

4.2. Phosphorylation and Signaling

  • Tyrosine 791 phosphorylation is critical for EphA7’s antitumor activity, as shown in PC-3 and DU145 cell models .

  • Soluble EphA7 TR variants function as decoy receptors, disrupting EphA2 signaling in lymphoma cells .

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