HSP70 (D69) Antibody

Product Pathways - Protein Folding

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HSP70 (D69) Antibody #4876

Applications	Reactivity	Sensitivity	MW (kDa)	Source
W IHC-P IHC-F IF-IC F	H M R Mk	Endogenous	70	Rabbit

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)  IHC-F=Immunohistochemistry (Frozen)  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
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.

Protocols

4876:

Flow , IHC / Frozen , IHC / Paraffin , Immunofluorescence , Western Blotting

Specificity / Sensitivity

HSP70 (D69) Antibody detects endogenous levels of total HSP70 protein. This antibody does not cross-react with other HSPs.  

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.

Background

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).

1. Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
2. Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
3. Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
4. Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.

Application References

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

Companion Products

• 4872 HSP70 Antibody
• 4873 HSP70 (6B3) Rat mAb
• 4874 HSP90 Antibody
• 4875 HSP90 (E289) Antibody
• 4871 HSP40 (C64B4) Rabbit mAb
• 7071 Phototope^® -HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
• 7074 Anti-rabbit IgG, HRP-linked Antibody
• 7720 Prestained Protein Marker, Broad Range (Premixed Format)
• 7727 Biotinylated Protein Ladder Detection Pack
• 7003 20X LumiGLO^® Reagent and 20X Peroxide
• 8112 SignalStain^® Antibody Diluent

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For Research Use Only. Not For Use In Diagnostic Procedures.