Cell Signaling Technology

Product Pathways - Protein Folding

HSP40 (C64B4) Rabbit mAb #4871

Applications Reactivity Sensitivity MW (kDa) Isotype
W IHC-P H M R Mk Endogenous 40 Rabbit IgG

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)
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

Specificity / Sensitivity

HSP40 (C64B4) Rabbit mAb detects endogenous levels of total HSP40 protein. This antibody does not cross-react with other HSPs.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to Glu223 of human HSP40/Hdj1.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, C2C12, C6 and COS cells using HSP40 (C64B4) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma using HSP40 (C64B4) Rabbit mAb.

Background

HSP40 and HSP40-like proteins represent a large family of chaperone proteins that are homologous to E. coli DnaJ protein (1). These proteins are classified into three subtypes based on their structures. The common feature of the family is a conserved J domain, which is usually located at the amino terminus of proteins and responsible for their association with HSP70 (1,2). Human HSP40, also known as Hdj1, belongs to subtype II that contain a unique Gly/Phe-rich region (2). HSP40 family proteins bind unfolded proteins, prevent their aggregation, and then deliver them to HSP70 (2,3). Another major function of HSP40 is to stimulate ATPase activity of HSP70, which causes conformational change of the unfolded proteins (4,5). The HSP40-HSP70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 or components of the protein degradation machinery such as CHIP and BAG-1, which either leads to protein folding or degradation, respectively (6).

  1. Cheetham, M.E. and Caplan, A.J. (1998) Cell Stress Chaperones 3, 28-36.
  2. Fan, C.Y. et al. (2003) Cell Stress Chaperones 8, 309-316.
  3. Langer, T. et al. (1992) Nature 356, 683-689.
  4. Liberek, K. et al. (1991) Proc. Natl. Acad. Sci. USA 88, 2874-2878.
  5. Cyr, D.M. et al. (1992) J. Biol. Chem. 267, 20927-20931.
  6. Höhfeld, J. et al. (2001) EMBO Rep. 2, 885-890.

Application References

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Companion Products

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

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