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HSP40, Hdj1 Antibody
HSP40, Hdj1 Antibody, Clone 3B9.E6
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, ICC, IP, E |
|---|---|
| Primary Accession | P25685 |
| Other Accession | NP_006136.1 |
| Host | Mouse |
| Isotype | IgG1 |
| Reactivity | Human, Mouse, Rat |
| Clonality | Monoclonal |
| Description | Mouse Anti-Human HSP40, Hdj1 Monoclonal IgG1 |
| Target/Specificity | Detects ~40kDa. Does not cross-react with HDJ2 or YDJ1. |
| Other Names | DNAJ1 Antibody, NDAJB1 Antibody, HDJ1 Antibody, HSP40 Antibody, HSPF1 Antibody, DnaJ homolog subfamily B member 1 Antibody, Dna J protein homolog 1 Antibody, Heat shock 40 kDa protein 1 Antibody, HSP40 Antibody, heat shock protein 40 Antibody, Human DnaJ protein 1 Antibody, hDj-1 Antibody |
| Clone Names | 3B9.E6 |
| Immunogen | Recombinant Protein HSP40 (Hdj1) |
| Purification | Protein G Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.2, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 0.5 µg/ml of SMC-145 was sufficient for detection of HSP40 (HDJ1) in 15 µg of HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody. |
| Cellular Localization | Cytoplasm | Nucleus |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Human HSP40/DnaJ proteins comprise a large protein family, members of which feature the J domain (named after the bacterial DnaJ protein) (1). The J-domain spans the first 75 N-terminal amino acids and is separated from the C-terminal by a glycine/phenylalanine-rich domain (2). Members of the HSP40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. In particular, Hdj1, the first human HSP40/DnaJ protein identified, plays an important role in protein translation and folding, as well as in the regulation of HSP70 function (3). HSP40 stimulates the ATPase activity of HSP70 which in turn causes conformational changes of the unfolded proteins (4, 5). The HSP40-HSP70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 which leads to protein folding, or components of protein degradation machinery CHIP and BAG-1 (6). Some studies have shown that the difference between HDJ1 and type 1 DNAJ proteins including HDJ2 and yeast YdjI is the result of the possession of a zinc finger domain by the latter, which helps in the function of protein folding. (7, 8).
References
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. Sohn S.Y., Kim S.B., Kim J., and Ahn B.Y. (2006) J Gen Virol. 87(7): 1883-91.
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.
7. Terda K., et al. (1997) J Cell Biol. 139: 1089-1095.
8. Lu Z. and Cyr D.M. (1998) J Biol Chem. 273: 27824-27830.
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