FKBP8抗体

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: Mouse liver tissue, Primary antibody: P08340(FKBP8 Antibody) at dilution 1/1150, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 1 minute    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colon cancer tissue using P08340(FKBP8 Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P08340(FKBP8 Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

**Background of FKBP8 Antibody**

FKBP8 (FK506-binding protein 8), also known as FKBP38. is a member of the immunophilin protein family, characterized by its peptidyl-prolyl isomerase (PPIase) activity and interaction with immunosuppressive drugs like FK506. Unlike other FKBPs, FKBP8 lacks a canonical PPIase domain and is anchored to mitochondrial and endoplasmic reticulum membranes via a C-terminal transmembrane region. It plays critical roles in regulating apoptosis, autophagy, and mitochondrial function by interacting with Bcl-2 family proteins (e.g., Bcl-2 and Bcl-XL) and modulating mitochondrial outer membrane permeabilization.

FKBP8 antibodies are essential tools for studying its expression, localization, and functional mechanisms. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to detect FKBP8 in various tissues and cell lines. These antibodies often target specific epitopes, such as the N-terminal region or unique domains, to ensure specificity. Research links FKBP8 to cancer (e.g., influencing chemoresistance in glioblastoma) and neurodegenerative diseases (e.g., Parkinson’s via mitophagy regulation). However, its dual role as a pro- or anti-apoptotic factor, depending on cellular context, complicates interpretation. Challenges in detection arise from low endogenous expression or isoform-specific variants. Validated FKBP8 antibodies are crucial for elucidating its physiological and pathological roles, offering insights into therapeutic targeting of apoptosis-related disorders.