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DNAJB12 Antibody(N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9NXW2 |
|---|---|
| Clone Names | 100406177 |
| Gene ID | 54788 |
|---|---|
| Other Names | DnaJ homolog subfamily B member 12, DNAJB12 |
| 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 | DNAJB12 {ECO:0000303|PubMed:21150129, ECO:0000312|HGNC:HGNC:14891} |
|---|---|
| Function | Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum- associated degradation (ERAD) pathway (PubMed:21150129, PubMed:21148293). Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities (PubMed:21148293). Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers (PubMed:27916661). While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear (PubMed:24732912). |
| Cellular Location | Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. Note=Localizes to the endoplasmic reticulum membrane (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661) When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). |
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Provided below are standard protocols that you may find useful for product applications.
Background
DNAJB12 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 acysteine-rich domain containing 4 motifs resembling a zinc fingerdomain (Ohtsuka and Hata, 2000 [PubMed 11147971]).[supplied byOMIM].
References
Lamesch, P., et al. Genomics 89(3):307-315(2007)Ohtsuka, K., et al. Cell Stress Chaperones 5(2):98-112(2000)
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