KLHL29抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P10548(KLHL29 Antibody) at dilution 1/100. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P10548(KLHL29 Antibody) at dilution 1/100. (Original magnification: ×200)    

  
  

The KLHL29 antibody targets the Kelch-like protein 29 (KLHL29), a member of the Kelch-like (KLHL) family characterized by conserved BTB/POZ, BACK, and Kelch-repeat domains. KLHL29 is implicated in protein ubiquitination pathways, likely acting as a substrate adaptor for Cullin 3 (CUL3)-based E3 ubiquitin ligase complexes. These complexes mediate substrate recognition and degradation via the ubiquitin-proteasome system, influencing cellular processes such as cytoskeletal organization, signal transduction, and stress responses. Though less studied than other KLHL family members, KLHL29 is hypothesized to play roles in neuronal development, cancer progression, or metabolic regulation, though its precise biological functions remain under investigation.

Antibodies against KLHL29 are essential tools for elucidating its expression patterns, subcellular localization, and interactions. They enable detection in techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding in tissue-specific expression profiling or disease-associated alterations. Commercial KLHL29 antibodies are limited, emphasizing the need for rigorous validation (e.g., knockout cell controls) to confirm specificity, as cross-reactivity with homologous KLHL proteins is a common challenge. Research utilizing KLHL29 antibodies could clarify its involvement in pathological conditions, such as tumorigenesis or neurological disorders, by linking its dysregulation to disease mechanisms. Current studies focus on identifying physiological substrates and signaling networks modulated by KLHL29. which may reveal therapeutic targets. Further development of high-affinity, well-validated KLHL29 antibodies remains critical to advancing this field.