Overview
| 别名 | 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 |
| 基因名 | DNAJB11 |
| UniProt ID | Q9UBS4 |
| 反应种属 | Human |
| 应用 | IHC-P |
| 宿主 | Mouse |
| 偶联物 | Unconjugated |
| 修饰 | Unmodified |
| 亚型 | IgG2b |
| 克隆号 | 8T5-B8-X3 |
| 克隆性 | Monoclonal Antibody |
| 分子量 | Calculated MW: 40 kDa |
| 纯化方式 | Affinity Purified |
| 产品形式 | Liquid |
| 推荐稀释比 | IHC-1:500-1:1000 |
| 存储缓冲液 | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% sodium azide |
| 保存温度 | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| 背景信息 | DnaJ heat shock protein family (Hsp40) member B11 (DNAJB11), also known as ERdj3, is a soluble glycoprotein and Type II HSP40 co-chaperone localized to the lumen of the endoplasmic reticulum (ER). It features an N-terminal J-domain that stimulates the ATPase activity of BiP (HSPA5), a master chaperone in the ER. DNAJB11 is unique among HSP40 family members due to its ability to form tetramers, a structural feature that enhances its substrate-binding capacity and facilitates ATP-independent chaperoning. It plays a vital role in protein folding, trafficking, and the degradation of secretory clients such as immunoglobulins and glucocerebrosidase. By coordinating ER-extracellular proteostasis, DNAJB11 ensures the quality control of proteins entering the secretory pathway, particularly during periods of ER stress. Its function is essential for maintaining cellular proteostasis and preventing the accumulation of misfolded proteins. |
检测原理