UBE2G2抗体—艾普蒂

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-3: Jurkat cell, Mouse testis tissue and 231 cell lysates, Primary antibody: P02340(UBE2G2 Antibody) at dilution 1/250, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 2 minutes    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P02340(UBE2G2 Antibody) at dilution 1/45. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P02340(UBE2G2 Antibody) at dilution 1/45. (Original magnification: ×200)    

  
  

The UBE2G2 antibody is a tool used to detect and study the ubiquitin-conjugating enzyme E2 G2 (UBE2G2), a key component of the ubiquitin-proteasome system (UPS). UBE2G2. part of the E2 enzyme family, facilitates the transfer of ubiquitin to substrate proteins in conjunction with E3 ligases, marking them for proteasomal degradation or functional modulation. This enzyme is involved in endoplasmic reticulum-associated degradation (ERAD), helping to eliminate misfolded proteins by tagging them with K48-linked polyubiquitin chains. Dysregulation of UBE2G2 has been linked to diseases such as cancer, neurodegenerative disorders, and metabolic syndromes, where protein homeostasis is disrupted.

UBE2G2 antibodies are widely used in research to investigate protein ubiquitination dynamics, enzyme-substrate interactions, and UPS-related pathways. They enable detection of UBE2G2 expression levels via techniques like Western blotting, immunohistochemistry, and immunofluorescence. These antibodies also aid in studying UBE2G2’s role in cellular stress responses, apoptosis, and cancer progression, where its overexpression or inhibition may influence tumor growth or drug resistance. Additionally, they are critical in validating CRISPR/Cas9 knockout models or siRNA-mediated silencing in functional studies. High specificity and validation for cross-reactivity are essential for reliable data, making UBE2G2 antibodies vital for advancing understanding of ubiquitination mechanisms and therapeutic targeting.