Product Pathways - Protein Folding
HSP70 (D69) Antibody #4876
|W IHC-P IHC-F IF-IC F||H M R Mk||Endogenous||70||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
HSP70 (D69) Antibody detects endogenous levels of total HSP70 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide surrounding Asp69 of human HSP70. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from HeLa, NIH/3T3 and C6 cells, using HSP70 (D69) Antibody.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using HSP70 (D69) Antibody.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using HSP70 (D69) Antibody in the presence of control peptide (left) or antigen speicific peptide (right).
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using HSP70 (D69) Antibody.
Immunohistochemical analysis of paraffin-embedded human prostate carcinoma, using HSP70 (D69) Antibody.
Flow cytometric analysis of HeLa cells, using HSP70 (D69) Antibody (blue) compared to a nonspecific negative control antibody (red).
HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).
- Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
- Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
- Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
- Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.
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For Research Use Only. Not For Use In Diagnostic Procedures.