DNAJB11 Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9UBS4 |
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Clone Names | 100324022 |
Gene ID | 51726 |
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Other Names | DnaJ homolog subfamily B member 11, APOBEC1-binding protein 2, ABBP-2, DnaJ protein homolog 9, ER-associated DNAJ, ER-associated Hsp40 co-chaperone, Endoplasmic reticulum DNA J domain-containing protein 3, ER-resident protein ERdj3, ERdj3, ERj3p, HEDJ, Human DnaJ protein 9, hDj-9, PWP1-interacting protein 4, DNAJB11, EDJ, ERJ3, HDJ9 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | DNAJB11 |
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Synonyms | EDJ, ERJ3, HDJ9 |
Function | 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). |
Cellular Location | Endoplasmic reticulum lumen Note=Associated with the ER membrane in a C-terminally epitope-tagged construct |
Tissue Location | Widely expressed. |
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Provided below are standard protocols that you may find useful for product applications.
Background
DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40family of proteins, which regulate molecular chaperone activity bystimulating ATPase activity. DNAJ proteins may have up to 3distinct domains: a conserved 70-amino acid J domain, usually atthe N terminus; a glycine/phenylalanine (G/F)-rich region; and aC-terminal cysteine-rich region (Ohtsuka and Hata, 2000 [PubMed11147971]).
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Wen, K.W., et al. Oncogene 29(24):3532-3544(2010)Bernal-Bayard, J., et al. J. Biol. Chem. 285(21):16360-16368(2010)Vembar, S.S., et al. J. Biol. Chem. 284(47):32462-32471(2009)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
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