|Calculated MW||57580 Da|
|Other Names||DnaJ homolog subfamily C member 3, Endoplasmic reticulum DNA J domain-containing protein 6, ER-resident protein ERdj6, ERdj6, Interferon-induced, double-stranded RNA-activated protein kinase inhibitor, Protein kinase inhibitor of 58 kDa, Protein kinase inhibitor p58, DNAJC3, P58IPK, PRKRI|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human p58 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||p58 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity.|
|Cellular Location||Endoplasmic reticulum.|
|Tissue Location||Widely expressed with high level in the pancreas and testis. Also expressed in cell lines with different levels.|
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Provided below are standard protocols that you may find useful for product applications.
The 58-kDa inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a cellular protein that is activated during influenza virus infection to down-regulate the activity of PKR. The 58-kDa inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a cellular protein that is activated during influenza virus infection to down-regulate the activity of PKR (1). The P58 protein inhibits both the autophosphorylation of PKR and the phosphorylation of the PKR natural substrate, the alpha subunit of eukaryotic initiation factor eIF-2. Sequence analysis revealed that P58 is a member of the tetratricopeptide family of proteins (2). Also, like other J-domain proteins, P58 stimulated the ATPase activity of Hsc70. Taken together, data suggests that P58 is a co-chaperone, possibly directing hsp/Hsc70 to refold, and thus inhibit kinase function (3).
1. Korth MJ, et al. Gene 170(2):181-8, 1996.
2. Polyak SJ, et al. J Biol Chem. 271(3):1702-7, 1996.
3. Melville MW, et al. J Biol Chem. 274(6): 3797-803, 1999.
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