SCAP抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P08742(SCAP Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P08742(SCAP Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

SCAP (SREBP Cleavage-Activating Protein) is a key regulatory protein in cholesterol and lipid metabolism. It functions as a sterol sensor and chaperone for sterol regulatory element-binding proteins (SREBPs), transcription factors that control genes involved in cholesterol synthesis and uptake. Under low cellular cholesterol conditions, SCAP escorts SREBPs from the endoplasmic reticulum (ER) to the Golgi apparatus, where SREBPs undergo proteolytic activation. Activated SREBPs then migrate to the nucleus to upregulate lipid biosynthesis genes. When cholesterol levels are sufficient, SCAP retains SREBPs in the ER by binding to insulin-induced gene (Insig) proteins, inhibiting further lipid production.

SCAP antibodies are essential tools for studying cholesterol homeostasis, metabolic disorders, and related diseases like atherosclerosis or obesity. They enable detection of SCAP expression, localization, and protein interactions via techniques such as Western blotting, immunofluorescence, or co-immunoprecipitation. Research using these antibodies has elucidated SCAP’s conformational changes during sterol sensing and its role in pathologies linked to dysregulated lipid metabolism. Additionally, SCAP-targeting therapeutic strategies, including small-molecule inhibitors, are being explored to modulate cholesterol levels, highlighting the protein’s clinical relevance. Understanding SCAP dynamics through antibody-based assays continues to advance insights into metabolic regulation and potential treatments for cardiovascular and metabolic diseases.