Product Details
Alternative Name: | HSP40, Heat shock protein 40, Heat shock protein J |
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Host: | Rabbit |
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Immunogen: | E. coli DnaJ. |
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UniProt ID: | P08622 |
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Source: | Purified from rabbit serum. |
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Species reactivity: | E. coli
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Applications: | IP, WB
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Recommended Dilutions/Conditions: | Immunoprecipitation (1:200) Western Blot (1:1,000, ECL) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
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Application Notes: | Detects a band of ~41kDa by Western blot. |
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Purity Detail: | Protein A affinity purified. |
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Formulation: | Liquid. In PBS containing 50% glycerol and 0.09% sodium azide. |
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Handling: | Avoid freeze/thaw cycles. |
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Shipping: | Blue Ice |
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Long Term Storage: | -20°C |
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Scientific Background: | DnaJ is a basic 41 kDa E. coli Heat shock protein which belongs to the molecular chaperone class of proteins. Bacterial DnaJ protein acts synergistically with the bacterial chaperone DnaK (Hsp70 homologue) and the other co-chaperone GrpE in suppressing eukaryotic and prokaryotic polypeptide aggregation, facilitating protein translocation through intracellular compartments or protein secretion, reactivating some partially aggregated enzymes, and activating pre-priming complex during initiation of DNA replication. |
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Regulatory Status: | RUO - Research Use Only |
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Western blot analysis: Lane 1: DnaJ Recombinant E. coli Protein.
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Product Literature References
Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli: T. Yura, et al. ; J. Biol. Chem.
276, 14393 (2001),
Application(s): WB using bacteria (E. coli) samples,
Abstract;
Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils: F.U. Hartl, et al. ; PNAS
97, 7841 (2000),
Application(s): WB using bacteria (E. coli) samples,
Abstract;