Technical Data
Heat Shock Protein 70 (HSP70)
Heat shock proteins are produced by prokaryotic and eukaryotic cells, and are among the most conserved molecules in phylogeny. Eukaryotic cells contain an HSP70 multigene that differ in their intracellular location and regulation. Members of the HSP70 family play a major role in the folding, unfolding and translocation of polypeptides as well as in the assembly and disassembly of oligomeric protein complexes, as well as in the immune response. HSP72 was found to increase dramatically in the brains of Alzheimer?s disease patients, and was localized exclusively in neuritic plaques and neurofibrillary tangles. HSP70 concentrates in nuclei during heat shock and returns to the cytoplasm when the shock is removed.

Suitable for use in Immunofluorescence, ELISA, Western Blot and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Immunofluorescence: Immunofluorescent staining demonstrates a rapid and reversible accumulation of HSP70 within the nucleus of heat-stressed (42C, 1 hour) human fibroblasts.
Western Blot: 1:5000
Immunohistochemistry: Frozen
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20CBlue IceBovineMouse
Not Determined
Full length native purified Heat Shock Protein 70 from bovine brain. Cellular Localization: Cytoplasmic and nuclear
Supplied as a liquid, 15mM sodium azide.
Recognizes bovine Heat Shock Protein 70 (HSP70) from brain and other tissues. In Western Blot, localizes both the constitutive (HSP73) and inducible (HSP72) forms of HSP70. Species Crossreactivity: rat, chicken, human, Drosophila melanogaster, guinea pig, hamster, plants, rabbit, C. elegans.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
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