HSC70 (HSP73) Antibody, Clone 1F2-H5

The HSP70 family comprises highly conserved, heat-inducible 70-kDa proteins that play a pivotal role in maintaining cellular proteostasis, particularly under stress conditions. Encoded by a multigene family in most eukaryotes, HSP70 proteins are ubiquitously distributed across cellular compartments—including the cytosol, nucleus, mitochondria, endoplasmic reticulum, and chloroplasts—and are also present in prokaryotes. Their evolutionary conservation, with over 50% sequence identity, underscores their essential biological functions. HSP70 proteins exhibit high-affinity ATP binding and possess ATPase activity, which is enhanced upon interaction with unfolded proteins and synthetic peptides. Structurally, the N-terminal domain mediates ATP binding, while the C-terminal domain governs substrate interaction. This dual-domain architecture enables HSP70s to act as molecular chaperones, facilitating protein folding, preventing aggregation, and promoting recovery from proteotoxic stress. In the context of neurodegenerative diseases, inducible HSP70 (HSP72) and its constitutively expressed counterpart HSC70 are of particular interest. Following cellular stress, such as heat shock, HSP72 is rapidly upregulated and forms ATP-dependent complexes with HSC70. This interaction is critical for restoring centrosomal integrity and function—processes often disrupted in neurodegenerative pathologies like Alzheimer’s and Parkinson’s disease. Given their central role in protein quality control and cellular resilience, HSP70 proteins are emerging as promising therapeutic targets in neuroscience and neurodegeneration research.

1 µg/ml of SMC-151 was sufficient for detection of HSC70 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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1. Brown C.L. et al. (1993) J.Cell Biol., 120 (5) : 1101-1112. 2. Boorstein W.R., Ziegelhoffer T., and 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., and Valencia A. (1992) Proc. Nut1Acad. Sci. USA 89: 7290-7294. 6. Brown C.L. et al. (1996) J. Biol. Chem. 271 (2) : 833-840.