KSR1抗体;KSR1 Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P11892(KSR1 Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P11892(KSR1 Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

The Kinase Suppressor of Ras 1 (KSR1) is a scaffold protein critical for regulating the RAS-MAPK (mitogen-activated protein kinase) signaling pathway, which controls cell proliferation, differentiation, and survival. Initially identified in genetic screens as a positive modulator of Ras signaling in *Drosophila* and *C. elegans*, KSR1 facilitates the assembly and activation of the RAF-MEK-ERK kinase cascade by bridging components like RAF, MEK, and ERK. Its scaffolding role enhances signal fidelity and amplification, making it essential for both physiological and oncogenic RAS-MAPK signaling. Dysregulation of KSR1 is implicated in cancers, inflammatory diseases, and developmental disorders.

KSR1 antibodies are widely used to study the expression, localization, and molecular interactions of KSR1 in cellular and disease models. These antibodies enable techniques such as Western blotting, immunoprecipitation, immunofluorescence, and immunohistochemistry. Due to KSR1’s dynamic conformational changes and low abundance in some tissues, antibody specificity and affinity are critical. Many commercially available KSR1 antibodies target conserved regions (e.g., the CA1 domain or C-terminal epitopes) and are validated across species (human, mouse, rat). However, cross-reactivity with KSR2 or other scaffold proteins remains a potential concern, necessitating careful validation via knockout controls.

Research on KSR1 antibodies also supports therapeutic exploration, as disrupting KSR1-mediated signaling is a strategy to inhibit RAS-driven cancers. Challenges persist in targeting KSR1’s scaffolding function pharmacologically, underscoring the continued importance of reliable antibodies for mechanistic studies.