Dna J

  • Official Full Name

  • Overview

    DnaJ, Heat shock protein, functions in association with DnaK(Hsp70) molecular chaperone to facilitate protein folding. p70 chaperone. DnaJ plays a key role in the chaperone reaction by stimulating the ATPase activity and activating the substrate binding of Hsp70.. DnaJ consists of four domains that are N-terminal 76 amino acid J-domain, G/F domain, zinc-binding cystein rich CR-domain, C-terminal CTD-domain and they are conserved to various degrees among the homologues.
  • Synonyms

    Dna J (1-376);Dna J;Co-chaperone with DnaK (1-376);DnaJ Chaperone Hsp40;dnaJ;dnaJ chaperone Hsp40;co-chaperone with DnaK;ECK0015;groP;grpC;JW0014;chaperone with DnaK;heat shock protein;Hsp40 (heat shock protein 40 kD)
Cat.# Product name Source (Host) Species Tag Protein Length Price

    Involved Pathway

    Dna J involved in several pathways and played different roles in them. We selected most pathways Dna J participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with Dna J were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    Protein Function

    Dna J has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by Dna J itself. We selected most functions Dna J had, and list some proteins which have the same functions with Dna J. You can find most of the proteins on our site.

    Function Related Protein

    Interacting Protein

    Dna J has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with Dna J here. Most of them are supplied by our site. Hope this information will be useful for your research of Dna J.

    dnaK;malT;uspG;malE;ileS;glyQ;rpsF;dnaA;kdsB;recD;pdxB

    Resources

    References

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