Target: HSP70
Conjugate: FITC
Product Type: Monoclonal
Clone Number: 1H11
Immunogen: Human native HSP70 protein
Swiss-Prot: P0DMV8/P0DMV9
Purification: Protein G Purified
Storage Buffer: PBS pH 7.4, 50% glycerol, 0.09% Sodium azide *Storage buffer may change when conjugated
Concentration: 0.5 mg/ml
Specificity: 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.
Cellular Localization: Cell membrane
Tissue Specificity: Induced by heat shock.
Scientific Background: HSP70 is a highly conserved protein that is ubiquitously expressed. It can be found in chloroplasts, eukaryotic cytosol, endoplasmic reticulum, and mitochondria, but also embedded in the cell membrane and in the extracellular space (1,2,3,4). Even though HSP70 is one of the most studied heat shock proteins, the export mechanism and method of membrane insertion are not fully understood. The majority of the proteins in the heat shock family lack a consensus signal for secretion via the ER-Golgi pathway (5). Researchers have found that HSP70 may be released from cells via exosomes or secretory vesicles (6).Although HSP70 is ubiquitously expressed, there is not much information about its presence on cell surface. The finding that HSP70 is localized on the cell surface of cancer cells but not normal cells suggests a conformational change of HSP70 in the lower pH environment characteristic of cancer cells (7). The presence of cell membrane embedded HSP70 has been found to increase the stability of cancer cells, thereby protecting tumors from environmental stress (8, 9).Anti-HSP70 antibody, clone 1H11 (Catalog No. SMC-249) is unique from other commercially available antibodies in that it can bind to the extracellular region of the cell membrane embedded HSP70 protein, allowing researchers to differentiate between membrane bound and intracellular HSP70 across cancer cells types.
References: 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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
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