He at shock protein 70 human has been used as a control for checking antibody reactivity.
HSPA8 (he at shock 70kDa protein 8) is a human cytoplasmic chaperone which is involved in protein folding, protein aggregation prevention and protein transport. During nutrient stress, it participates in antigen transport to regulate MHC (major histocompatibility) class II presentation. It is upregulated in cancer cells and is involved in protein homeostasis, leading to cancer cell growth and survival.
HSP70 antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Recommended dilution range for Western blot is 1:500 ~ 1:2,000 and immunohistochemistry analysis is 1:100~200. Recommended start
Human;Mouse;Rat;Monkey;Bovine
Anti-human HSP70 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSP70 amino acids 1-641 purified from E. coli.
HSP70 is a human heat shock protein. HSP-70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the HSP70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc...).
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[4] Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.
