HSPA8 (HSC70) is a 70-72 kDa heat shock protein that facilitates protein folding, prevents aggregation, and regulates autophagy during bacterial infection or cellular stress . Key roles include:
Autophagy Regulation: Promotes autophagosome formation and bacterial clearance by stabilizing BECN1 and RHOB, critical factors in LC3 lipidation .
Protein Homeostasis: Maintains cellular protein balance by interacting with co-chaperones (e.g., HSP90) and client proteins .
Stress Response: Upregulated during heat shock, oxidative stress, or DNA damage to protect cellular integrity .
HSPA8 antibodies are typically monoclonal or polyclonal reagents validated for specificity across human, mouse, and rat models. Key structural and functional features include:
Format: Recombinant monoclonal or affinity-purified polyclonal antibodies .
Epitope: Targets synthesized peptides or full-length HSPA8, often validated via Western blot (WB), immunohistochemistry (IHC), and immunocytochemistry (ICC) .
Autophagy Induction: HSPA8 stabilizes BECN1 and RHOB, reducing their K48-linked ubiquitination and proteasomal degradation. This enhances LC3-II formation and intracellular pathogen clearance .
Chaperone Complexes: Interacts with RHOB (residues 1–42/89–118) and BECN1 (residues 244–337) via distinct domains, forming a ternary complex critical for autophagy .
DNA Binding Regulation: In plants, homologs like MdHSFA8a bind HSE cis-elements in promoters of flavonoid synthesis genes (e.g., MdMYB12, MdANS), though this mechanism is HSP90-dependent .
Specificity: No cross-reactivity with HSP70 isoforms (e.g., HSPA1A) confirmed via WB .
Storage: Stable at -20°C for 12 months; post-reconstitution, usable for 1 month at 4°C or 6 months at -20°C .
HSPA8 antibodies are indispensable for studying stress responses, infection biology, and protein quality control. Recent studies highlight their utility in: