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HSP40, YDJ1 Antibody, Clone 2A7.H6: HRP
Mouse Anti-Yeast HSP40, YDJ1 Monoclonal IgG1 Kappa
Artikelnummer
STRSMC-166D-HRP
Verpackungseinheit
100 µg
Hersteller
Stressmarq Biosciences
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Target: HSP40
Conjugate: HRP
Product Type: Monoclonal
Clone Number: 2A7.H6
Immunogen: Yeast Full length protein HSP40 (YDJ1)
Swiss-Prot: P25491
Purification: Protein G Purified
Storage Buffer: 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Detects ~40kDa. Yeast specific. Does not cross react with Human, Mouse or Rat.
Cellular Localization: Cytoplasm,Nucleus
Scientific 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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
Conjugate: HRP
Product Type: Monoclonal
Clone Number: 2A7.H6
Immunogen: Yeast Full length protein HSP40 (YDJ1)
Swiss-Prot: P25491
Purification: Protein G Purified
Storage Buffer: 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Detects ~40kDa. Yeast specific. Does not cross react with Human, Mouse or Rat.
Cellular Localization: Cytoplasm,Nucleus
Scientific 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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
| Artikelnummer | STRSMC-166D-HRP |
|---|---|
| Hersteller | Stressmarq Biosciences |
| Hersteller Artikelnummer | SMC-166D-HRP |
| Green Labware | Nein |
| Verpackungseinheit | 100 µg |
| Mengeneinheit | STK |
| Reaktivität | Yeast |
| Klonalität | Monoclonal |
| Methode | Immunoprecipitation, Western Blotting, ELISA |
| Isotyp | IgG1 kappa |
| Human Gene ID | 855661 |
| Wirt | Mouse |
| Produktinformation (PDF) | Download |
| MSDS (PDF) | Download |
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