Antibodies - Heat Shock Proteins, Oxydative Stress, Apoptosis, Cell Signaling

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Product Name: Hsp40 (YDJ1) Antibody
Catalog #: SMC-150C
Package size: 25ug
Price: $155.00 USD

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Alternate Product Sizes: SMC-150D
Type: Monoclonal
Conjugate: N/A
Datasheet: SMC 150 Heat Shock Protein 40 (Hsp40) (YDJ1)
Description: Anti-Hsp40 (YDJ1)
Research Area: Chaperones, Heat Shock, Trafficking
Alternative Names: DNAJA2, CPR3, HIRIP4, DNAJ, DNJ3, DJ3, RDJ2, HIRa interatcting protein4
Clone Number: 1G10.H8
Host Species: Mouse
Isotype: IgG1 Kappa
Immunogen: Full length protein yeast Hsp40 (YDJ1)
Applications: WB, IP, ELISA, Other applications not yet tested.
Species Reactivity: Yeast. Does not cross react with human, mouse or rat.
Accession Number: NP_014335.1
Gene ID: 855661
SwissProt: P25491
Background Info: Detects ~40kDa.
Recommended Dilutions: 1:2000 (WB)
Form: Protein G Purified
Storage Buffer: 50% glycerol, 0.09% sodium azide
Concentration: 1mg/mL
Certificate of Analysis: 0.5 μg/mL of SMC-150 was sufficient for detection of 50ng YDJ1 by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Storage Temp: -20°C
Shipping Temp: Blue Ice or 4°C

Western blot analysis of Hsp40 YDJ1 in a human cell line mix using a 1:1000 dilution of SMC-150.

Research 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). There are two main types of Hsp40; type 1 DNAJ proteins including HDJ2 and yeast YdjI; type II includes yeast Sis1 and human Hdj1. Whereas type I possesses a zinc finger domain which helps in the function of protein folding. (3, 4), type II does not. Members of the Hsp40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. Hsp40 stimulates the ATPase activity of Hsp70 which in turn causes conformational changes of the unfolded proteins (5, 6). 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 (7).
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. Terda K., et al. (1997) J Cell Biol. 139: 1089-1095.
4. Lu Z. and Cyr D.M. (1998) J Biol Chem. 273: 27824- 27830.
5. Liberek K. et al. (1991) Proc. Natl. Acad. Sci. USA 88: 2874–2878.
6. Cyr D.M., et al. (1992) J Biol Chem. 267: 20927– 20931.
7. Höhfeld J., et al. (2001) EMBO Rep. 2: 885–890.

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