SGTA抗体—艾普蒂

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-2: LNCAP and A172 cell lysates, Primary antibody: P10370(SGTA Antibody) at dilution 1/1150, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 2 minutes    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P10370(SGTA Antibody) at dilution 1/75. (Original magnification: ×200)    

  
  

SGTA (Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha) is a cytosolic co-chaperone involved in protein quality control, particularly in regulating the folding, sorting, and trafficking of nascent or misfolded proteins. It interacts with HSP70/HSP90 chaperones and components of the ubiquitin-proteasome system, playing a role in substrate triage decisions—either facilitating proper folding or targeting proteins for degradation. SGTA’s tetratricopeptide repeat (TPR) domains mediate protein-protein interactions, while its glutamine-rich region may contribute to solubility and binding specificity.

Research links SGTA to diverse cellular processes, including hormone signaling, viral infection (e.g., HIV-1), and stress responses. Dysregulation of SGTA has been implicated in neurodegenerative diseases (e.g., ALS) and cancers, where altered protein homeostasis is a hallmark. Its role in androgen receptor maturation also ties it to prostate cancer progression.

SGTA antibodies are essential tools for studying these functions. They are used in techniques like Western blotting, immunofluorescence, and co-immunoprecipitation to detect SGTA expression, localization, and interaction partners. Commercial antibodies are typically raised against epitopes in its N-terminal or C-terminal regions, with validation including knockout cell lines to confirm specificity. Researchers prioritize antibodies with high affinity and minimal cross-reactivity to homologous proteins (e.g., BAG family chaperones). Recent studies also employ SGTA antibodies to explore its therapeutic potential, such as modulating proteostasis in protein aggregation disorders or targeting chaperone networks in cancer.