USP32抗体—艾普蒂

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     Black line: Control Antigen (100 ng); Purple line: Antigen(10ng); Blue line: Antigen (50 ng); Red line: Antigen (100 ng);    

  
  

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     Immunohistochemical analysis of paraffin-embedded human muscle tissues using VIL1 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human stomach cancer tissues using VIL1 mouse mAb with DAB staining.    

  
  

The USP32 (Ubiquitin-Specific Protease 32) antibody is a research tool targeting a deubiquitinating enzyme (DUB) belonging to the ubiquitin-specific protease family. USP32 regulates protein stability and function by cleaving ubiquitin moieties from substrate proteins, thereby counteracting ubiquitin-mediated degradation. This enzyme contains conserved catalytic domains characteristic of USPs, including the cysteine protease domain critical for its enzymatic activity. USP32 is implicated in diverse cellular processes, such as cell cycle regulation, DNA damage repair, and endosomal trafficking. Dysregulation of USP32 has been linked to cancer progression, with studies suggesting its overexpression in certain tumors may promote oncogenic signaling or chemoresistance.

Antibodies against USP32 are primarily used to study its expression, localization, and interactions in various biological contexts. They enable detection via techniques like Western blotting, immunofluorescence, and immunoprecipitation. Polyclonal antibodies often recognize multiple epitopes, while monoclonal antibodies offer higher specificity. Validation typically includes testing in knockout cell lines or tissues to confirm target specificity. Research utilizing USP32 antibodies contributes to understanding its role in ubiquitin-dependent pathways, disease mechanisms, and potential therapeutic targeting. However, commercial availability and functional validation data remain limited compared to well-characterized DUBs, necessitating careful experimental controls.