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HSP40/Hdj2 polyclonal antibody

 
ADI-SPA-405-050 50 µg 140.00 USD
 
ADI-SPA-405-200 200 µg 345.00 USD
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Product Specification

Alternative Name:Heat shock protein 40
 
Host:Rabbit
 
Immunogen:Recombinant human HSP40/Hdj2.
 
UniProt ID:P31689
 
Species reactivity:Human, Mouse, Rat
Hamster
 
Specificity:Has high specificity for the constitutively expressed Hdj2 compared to Hdj1 using recombinant controls.
 
Applications:WB
 
Recommended Dilutions/Conditions:Western Blot (1:1,000, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Application Notes:Detects a band of ~45kDa by Western blot.
 
Purity Detail:Protein A-affinity purified.
 
Formulation:Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background:Hdj2 is an approximately 40kDa member of the heat shock protein (Hsp40) family, a eukaryotic homolog of the E. coli DnaJ protein.  Eukaryotic DnaJ-like proteins share structural domain conservation with DnaJ  namely: 1) an N-terminal ~70 amino acid J domain, 2) a glycine- and phenylalanine-rich domain, 3) a cysteine-rich zinc finger domain, and 4) a poorly conserved C-terminal domain. The human constitutive Hdj2 protein shares full domain conservation with DnaJ, as opposed to the human inducible Hdj1 which lacks the zinc-finger domain. The Hsp40 J domain regulates its interaction with Hsp70 (E. coli DnaK), increasing Hsp70 ATPase activity and in turn enhancing substrate binding by the Hsp70 chaperone. Hsp40 co-chaperones are involved in nearly all aspects of protein synthesis and secretion because of their importance in Hsp70 function, and they are also thought to have an intrinsic ability to bind and fold some misfolded proteins. Hdj2 has been specifically shown to interact with Hsc70, the constitutive form of Hsp70, in the biogenesis of the cystic fibrosis transmembrane conductance regulator (CFTR), mutations of which are known to cause inherited cystic fibrosis.
 
SPA-405 WB
Western Blot Analysis of HSP40/Hdj2, pAb: Lane 1: MWM, Lane 2: Hsp40/Hdj2 Recombinant Human Protein (Prod. No. ADI-SPP-405), Lane 3: HeLa Cell Lysate (Prod. No. ADI-LYC-HL100), Lane 4: HeLa Cell Lysate, Heat Shocked (Prod. No. ADI-LYC-HL101), Lane 5: PC-12 Cell Lysate (Prod. No. ADI-LYC-PC100), Lane 6: PC-12 Cell Lysate, Heat Shocked (Prod. No. ADI-LYC-PC101), Lane 7: 3T3 Cell Lysate (Prod. No. ADI-LYC-3T100), Lane 8: 3T3 Cell Lysate, Heat Shocked (Prod. No. ADI-LYC-3T101), Lane 9: CHO-K1 Cell Lysate, Lane 10: CHO-K1 Cell Lysate, Heat Shocked.
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SPA-405 WB

Product Literature References

Basal and stress-induced Hsp70 are modulated by ataxin-3: C.P. Reina, et al.; Cell Stress Chaperones 17, 729 (2012), Application(s): WB using mouse cell lysate, Abstract; Full Text
Methylglyoxal alters the function and stability of critical components of the protein quality control: C. F. Bento, et al.; PLoS One 5, e13007 (2010), Application(s): WB using human cell lysates, Abstract; Full Text

General Literature References

Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway: N.S. Cintron & D. Toft; J. Biol. Chem. 281, 26235 (2006), Abstract;
A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase: J.M. Younger, et al.; J. Cell Biol. 167, 1075 (2004), Abstract;
Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70: K. Terada & M. Mori; J. Biol. Chem. 275, 24728 (2000), Abstract;
Role of the J-domain in the cooperation of Hsp40 with Hsp70: M.K. Greene, et al.; PNAS USA 95, 6108 (1998), Abstract;
Conformational characterization of DnaK and its complexes by small-angle X-ray scattering: L. Shi, et al.; Biochemistry 35, 3297 (1996), Abstract;
Molecular chaperones in cellular protein folding: F.U. Hartl; Nature 381, 571 (1996), Abstract;
Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication: A. Buchberger, et al.; J. Biol. Chem. 270, 16903 (1995), Abstract;

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