HSP70/HSC70 Antibody, Clone BB70: APC

HSP70 proteins are a highly conserved family of 70-kDa molecular chaperones essential for maintaining protein homeostasis across all domains of life. In eukaryotes, HSP70 genes form a multigene family, with isoforms localized to the cytosol, nucleus, mitochondria, endoplasmic reticulum, and chloroplasts. These chaperones are either constitutively expressed (HSC70) or stress-inducible (HSP70), and share over 50% sequence identity across species. Functionally, HSP70s bind ATP with high affinity and exhibit ATPase activity that is stimulated by interaction with unfolded or misfolded proteins. The N-terminal domain mediates ATP binding, while the C-terminal domain is responsible for substrate recognition. This ATP-driven cycle enables HSP70s to bind and release hydrophobic regions of nascent or damaged proteins, preventing aggregation and facilitating proper folding, transport, and assembly. In neuroscience, HSP70 and HSC70 are critical for neuronal survival under proteotoxic stress—conditions commonly associated with neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s disease. These chaperones stabilize misfolded proteins, support autophagic clearance, and modulate apoptotic signaling pathways. Their ability to interact with co-chaperones and degradation machinery further enhances their role in maintaining neuronal proteostasis. Given their central role in stress response and protein quality control, HSP70/HSC70 are promising therapeutic targets and biomarkers in neurodegeneration research.

HSPA1A, HSPA1B, HSPA1, HSPA8, HSP70, HSP70-1, HSP70.1, HSP70-2, HSP72, HSP73, HSC70, HSX70, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1B, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein

1 µg/ml of SMC-106 was sufficient for detection of HSP70 and HSC70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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1. Zho J. (1998) Cell 94 : 471-480. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38 (1) : 1-17. 3. Rothman J. (1989) Cell 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Nat Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al, (1993) Mol. Cell. Biol. 13 (2) : 869-876. 8. Prapapanich V., et al. (1996) Mol. Cell. Biol. 16 (11) :6200-6207. 9. Fernandez-Funez et al., (2000) Nature 408 (6808) : 101-106.

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