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| Cat.No | ACP08017 | Target Name | DNAJB14 |
|---|---|---|---|
| Target Synonyms | DNAJB14; UNQ9427/PRO34683; DnaJ homolog subfamily B member 14 | Form | Lyophilized powder |
| Expression System | Custom Production. Please inquire and provide the desire expression system. | Protein Length | Partial |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q8TBM8 |
|---|
Uniprot Id
Q8TBM8
Target Species
Human
Target Name
DNAJB14
Target Full Name
DnaJ homolog subfamily B member 14
Target 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. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear.; (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection.
Target Subcellular Location
Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
Target Protein Families
DnaJ family, DNAJB12/DNAJB14 subfamily
Target Synonyms
DNAJB14; UNQ9427/PRO34683; DnaJ homolog subfamily B member 14
Target Background
Enables Hsp70 protein binding activity. Involved in cellular protein-containing complex assembly and chaperone cofactor-dependent protein refolding. Located in endoplasmic reticulum.
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