CCT8L2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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     Western blot analysis using GSTM1 mouse mAb against Cos7 (1), MCF-7 (2), Jurkat (3), Hela (4), HL7702 (5) and HepG2 (6) cell lysate.    

  
  

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     Flow cytometric analysis of Jurkat cells using GSTM1 mouse mAb (green) and negative control (red).    

  
  

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     Immunohistochemical analysis of paraffin-embedded human rectum cancer tissues using GSTM1 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human liver cancer tissues using GSTM1 mouse mAb with DAB staining.    

  
  

The CCT8L2 antibody targets the chaperonin-containing TCP-1 subunit 8-like 2 (CCT8L2) protein, a putative paralog of the CCT8 subunit within the chaperonin complex CCT/TRiC. This evolutionarily conserved complex assists in ATP-dependent folding of nascent polypeptides, including actin, tubulin, and cell cycle regulators. While CCT8 is a well-characterized subunit critical for substrate binding and structural integrity, CCT8L2 is considered a pseudogene or a low-expression variant in humans, with unclear functional divergence. Its gene locus on chromosome 11 and sequence homology to CCT8 suggest possible redundancy or regulatory roles.

Antibodies against CCT8L2 are primarily used in research to distinguish it from CCT8 and explore its expression patterns, particularly in cancers or neurological disorders where chaperonin dysregulation is implicated. However, due to high sequence similarity, cross-reactivity remains a challenge, requiring rigorous validation via knockout controls. Studies using CCT8L2 antibodies have detected weak or tissue-specific signals, hinting at restricted expression in certain cell types or developmental stages. Current efforts focus on clarifying whether CCT8L2 retains chaperone activity, acts as a dominant-negative regulator, or serves non-canonical roles in stress responses. Further characterization may uncover its relevance to proteostasis-related diseases.