INSR抗体;INSR Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P12760(INSR Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

The insulin receptor (INSR) is a transmembrane tyrosine kinase receptor critical for regulating glucose homeostasis, cell growth, and metabolism. Composed of two extracellular α-subunits and two transmembrane β-subunits, INSR binds insulin to activate downstream signaling pathways, including PI3K-AKT and MAPK. Dysregulation of INSR signaling is linked to metabolic disorders (e.g., diabetes, insulin resistance) and cancers.

INSR antibodies are tools used in research and diagnostics to detect receptor expression, localization, and activation states. Polyclonal antibodies target multiple epitopes, while monoclonal antibodies offer specificity to particular domains (e.g., ligand-binding sites, phosphorylated tyrosine residues). These antibodies enable techniques like Western blotting, immunohistochemistry, and flow cytometry to study INSR expression in tissues or cell lines.

In clinical contexts, autoantibodies against INSR are associated with rare conditions like type B insulin resistance syndrome, where they disrupt insulin signaling, causing hyperglycemia or hypoglycemia. Therapeutic anti-INSR antibodies are also explored for modulating receptor activity—antagonistic antibodies may inhibit oncogenic signaling in cancers, whereas agonist antibodies could mimic insulin effects in diabetes.

Overall, INSR antibodies serve as vital reagents for unraveling insulin-related pathophysiology and developing targeted therapies. Their applications span basic research, diagnostic profiling, and therapeutic innovation.