Recombinant Human EDJ protein (His tag N-Terminus)
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Recombinant Human EDJ protein (His tag N-Terminus) is a Human Full Length protein, in the 23 to 358 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
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EDJ, ERJ3, HDJ9, PSEC0121, UNQ537/PRO1080, DNAJB11, DnaJ homolog subfamily B member 11, APOBEC1-binding protein 2, DnaJ protein homolog 9, ER-associated DNAJ, ER-associated Hsp40 co-chaperone, Endoplasmic reticulum DNA J domain-containing protein 3, HEDJ, Human DnaJ protein 9, PWP1-interacting protein 4, ABBP-2, ER-resident protein ERdj3, ERdj3, ERj3p, hDj-9
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human EDJ protein (His tag N-Terminus) (AB105636)
15% SDS-PAGE analysis of ab105636 (3ug)
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This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
EDJ facilitates protein folding by stabilizing unfolded protein states and preventing protein aggregation. It acts as part of a larger multiprotein complex which is essential for maintaining cellular homeostasis. The chaperone activity of EDJ enables cells to cope with stress conditions such as those caused by ER stress or the accumulation of unfolded proteins. This involvement highlights its participation in the unfolded protein response (UPR) mechanism which restores normal cellular function in stressed cells.
Pathways
EDJ plays a significant role in the unfolded protein response and the heat shock response pathways. In these pathways EDJ interacts with proteins like BiP/GRP78 contributing to the regulatory mechanisms that maintain protein equilibrium within the ER. The protein helps manage these pathways by modulating the activity of stress sensors that initiate adaptive responses when proteins lose their proper folding within the ER.
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기능
As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins (PubMed : 10827079, PubMed : 15525676, PubMed : 29706351). Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed (PubMed : 15525676). May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (PubMed : 10827079). It is necessary for maturation and correct trafficking of PKD1 (PubMed : 29706351).
Post-translational modifications
Contains high-mannose Endo H-sensitive carbohydrates.. Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular disulfide bonds. The preferential partner for each Cys is not known.. Thr-188 was reported to be phosphorylated upon DNA damage by ATM or ATR; however as this position has been shown to be in the ER lumen, the in vivo relevance is not proven.
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