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DnaJ (E. coli), (recombinant) (His-tag)

 
ADI-SPP-640-D 50 µg 201.00 USD
 
ADI-SPP-640-F 200 µg 494.00 USD
 
ADI-SPP-640-J 1 mg 1,949.00 USD
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Product Specification

Alternative Name:DNAJB2, DnaJ HSJ1, HSPF3, HSP40
 
Recommended Dilutions/Conditions:Western Blot (100ng, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
MW:~43kDa
 
Source:Produced in E. coli. E. coli DnaJ is fused at the N-terminus to a His-tag.
 
UniProt ID:P08622
 
Formulation:Liquid. In 25mM HEPES, pH 7.5, containing 200mM potassium chloride, 10% glycerol, and 5mM DTT.
 
Purity:≥90% (SDS-PAGE; Western blot)
 
Purity Detail:Purified by multi-step chromatography.
 
Applications:WB
Protein refolding assay
 
Application Notes:Western blot control.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:Escherichia coli heat shock protein DnaJ belongs to the molecular chaperone class of proteins. Located in an operon with dnaK, theE. coli dnaJ gene shares sequence identity with eukaryotic cytosolic and endoplasmic reticulum DnaJ homologs (Hsp40) involved in protein folding, membrane translocation of newly synthesized proteins, and initiation of translation. The N-terminal, highly-conserved "J" domain of the DnaJ protein supports interaction with the DnaK protein and represents the signature sequence of DnaJ family members. Bacterial DnaJ protein acts synergistically with bacterial chaperones DnaK (Hsp70 homolog) and GrpE in various functions, including suppressing eukaryotic and prokaryotic polypeptide aggregation to promote protein folding, facilitating protein translocation through intracellular compartments or protein secretion , and repairing and reactivating partially aggregated enzymes such asE. coli RNAP and luciferase. In these reactions, DnaJ protein facilitates the binding of DnaK to its substrate by accelerating DnaK-catalyzed ATP hydrolysis to produce a DnaK-ADP form with a higher affinity for certain protein substrates. Some eukaryotic homologues of DnaJ also display an ability to stimulate the ATPase activity of Hsp70 proteins, including DnaJ homologue S. cerevisiae YDJ1 which interacts with DnaK homologue Ssal to stimulate its ATPase activity. Data suggests that DnaJ protein acting alone possesses chaperone activity, demonstrating an ability to bind tightly to denatured proteins such as rhodanese or luciferase to prevent their aggregation or misfolding.
 
SPP-640 SDS-PAGE
SDS-PAGE analysis: Lane 1: MWM, Lane 2: 0.5µg, Lane 3: 1µg, Lane 4: 2µg, Lane 5: 5µg DnaJ Recombinant Protein.
SPP-640 WB
Western Blot Analysis: Lane 1: MWM, Lane 2: 100 ng of DnaJ probed with DnaJ pAb.
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SPP-640 SDS-PAGE SPP-640 WB

Product Literature References

Improvement of H2O2 stability of manganese peroxidase by combinatorial mutagenesis and high-throughput screening using in vitro expression with protein disulfide isomerase: H. Takahashi, et al. ; Protein Eng. 16, 423 (2003), Application(s): In Vitro Assay , Abstract;
Assembly of Tim9 and Tim10 into a functional chaperone: K. Tokatlidis, et al. ; J. Biol. Chem. 277, 36100 (2002), Abstract;
The DnaK chaperone system facilitates 30S ribosomal subunit assembly: G.M. Culver, et al. ; Mol. Cell 10, 129 (2002), Abstract;
Protein disulfide isomerase-mediated cell-free assembly of recombinant interleukin-12 p40 homodimers: K. Vandenbroeck, et al. ; Eur. J. Biochem. 267, 6679 (2000), Application(s): In Vitro Assay , Abstract;
Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomes: B. Hardesty, et al. ; J. Biol. Chem. 271, 31160 (1996), Application(s): In Vitro Assay , Abstract;

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