HSP70 Antibody, Clone 1H11: APC

HSP70 proteins are a highly conserved family of 70-kDa molecular chaperones encoded by a multigene family in most eukaryotes and prokaryotes. Found in nearly all cellular compartments—including the cytosol, nucleus, mitochondria, endoplasmic reticulum, and chloroplasts—HSP70s are constitutively expressed and strongly upregulated in response to cellular stress. These chaperones play a vital role in protein homeostasis by binding to nascent polypeptides and partially folded or misfolded proteins, preventing aggregation and facilitating proper folding. HSP70s exhibit high-affinity ATP binding and weak ATPase activity, which is stimulated upon interaction with unfolded substrates. ATP hydrolysis triggers conformational changes that regulate substrate binding and release, enabling dynamic cycles of protein folding and refolding. Structurally, the N-terminal domain of HSP70 is responsible for ATP binding, while the C-terminal domain mediates substrate interaction. This modular design allows HSP70s to coordinate with co-chaperones such as HSP40, HIP, HOP, and BAG-1, integrating folding with degradation and transport pathways. In neurodegenerative disease research, HSP70 is of particular interest due to its ability to counteract protein misfolding and aggregation—hallmarks of disorders like Alzheimer’s, Parkinson’s, and Huntington’s disease. By stabilizing toxic intermediates and promoting their clearance, HSP70 enhances neuronal survival and resilience under proteotoxic stress.

Conformation-specific antibody for membrane-bound HSP70. Binds to cell surface HSP70 without permeabilization of cell membrane in tumor cell lines. Does not bind to intracellular HSP70 at low concentrations. Cross-reacts with HSC70. Detects a ~70 kDa band in Western Blot.

A 1:250 dilution of SMC-249 was sufficient for detection of cell surface HSP70 in HCT116 cells using Fluorescence-activated cell sorting, applied in flow cytometry, with FITC as the fluorescent probe.

1. Gribaldo, S. et al. (1999) J. Bacteriol. 181, 434-443. 2. Sharma, D. & Masison, D.C. (2009) Protein Pept. Lett. 16, 571-581. 3. Sharma, D. et al. (2009) PLoS. ONE.4, e6644. 4. Kampinga, H.H. & Craig, E.A. (2010) Nat. Rev. Mol. Cell Biol. 11, 579-592. 5. Nickel, W. & Seedorf, M. (2008) Annu. Rev. Cell Dev. Biol. 24, 287-308. 6. Multhoff, G. & Hightower, L.E. (1996) Cell Stress. Chaperones. 1, 167-176. 7. De Maio, A. (2011) Cell Stress. Chaperones. 16, 235-249. 8. Horvath, I. & Vigh, L. (2010) Nature. 463, 436-438. 9. Horvath, I., Multhoff, G., Sonnleitner, A., & Vigh, L. (2008) Biochim. Biophys. Acta 1778, 1653-1664.

Conformation-specific antibody for membrane-bound HSP70. Binds to cell surface HSP70 without permeabilization of cell membrane in tumor cell lines. Does not bind to intracellular HSP70 at low concentrations. Cross-reacts with HSC70. Detects a ~70 kDa band in Western Blot.

1. Gribaldo, S. et al. (1999) J. Bacteriol. 181, 434-443. 2. Sharma, D. & Masison, D.C. (2009) Protein Pept. Lett. 16, 571-581. 3. Sharma, D. et al. (2009) PLoS. ONE.4, e6644. 4. Kampinga, H.H. & Craig, E.A. (2010) Nat. Rev. Mol. Cell Biol. 11, 579-592. 5. Nickel, W. & Seedorf, M. (2008) Annu. Rev. Cell Dev. Biol. 24, 287-308. 6. Multhoff, G. & Hightower, L.E. (1996) Cell Stress. Chaperones. 1, 167-176. 7. De Maio, A. (2011) Cell Stress. Chaperones. 16, 235-249. 8. Horvath, I. & Vigh, L. (2010) Nature. 463, 436-438. 9. Horvath, I., Multhoff, G., Sonnleitner, A., & Vigh, L. (2008) Biochim. Biophys. Acta 1778, 1653-1664.