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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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     Western blot analysis using OTUB2 mouse mAb against HepG2 (1), A549 (2),HT-29 (3), MCF-7 (4), Jurkat (5), Hela (6), and Hek293 (7) cell lysate.    

  
  

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     Flow cytometric analysis of Hela cells using OTUB2 mouse mAb (green) and negative control (red).    

  
  

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     Flow cytometric analysis of HepG2 cells using OTUB2 mouse mAb (green) and negative control (red).    

  
  

OTUB2 antibody is a research tool designed to detect and study the OTUB2 protein, a member of the ovarian tumor (OTU) deubiquitinase family. OTUB2. encoded by the OTUB2 gene in humans, is a cysteine protease that specifically cleaves ubiquitin chains, regulating protein stability, localization, and signaling pathways. Unlike its well-characterized homolog OTUB1. OTUB2 exhibits distinct substrate preferences and cellular roles. It is implicated in modulating DNA damage response, immune regulation, and cell cycle progression. Studies suggest OTUB2 may act as both a canonical deubiquitinase and a non-catalytic signaling modulator, particularly through interactions with E2 ubiquitin-conjugating enzymes.

Antibodies targeting OTUB2 are typically developed in rabbits or mice using immunogenic peptide sequences or recombinant protein fragments. These antibodies enable researchers to investigate OTUB2's expression patterns, subcellular localization (predominantly nuclear), and protein interactions via techniques like Western blotting, immunofluorescence, and immunoprecipitation. Recent research highlights OTUB2's potential oncogenic role in cancers, where its overexpression correlates with tumor progression and therapy resistance by stabilizing oncoproteins. However, its exact mechanistic contributions remain under active investigation. Validated OTUB2 antibodies are crucial for elucidating its dual enzymatic and scaffolding functions in cellular homeostasis and disease pathogenesis.