| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERP29 |
| Uniprot No | P30040 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-251aa |
| 氨基酸序列 | PLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLVAEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKVGAIQRWLKGQGVYLGMPGCLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAF |
| 预测分子量 | 51.0 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ERP29重组蛋白的3篇参考文献摘要概括：
1. **文献名称**: *ERP29 promotes the maturation of recombinant human thyroglobulin in CHO cells by accelerating protein folding and lysosomal degradation*
**作者**: Zhang Y. et al.
**摘要**: 研究通过CHO细胞表达系统发现，ERP29作为分子伴侣参与重组人甲状腺球蛋白(rhTG)的折叠与分泌，通过促进正确二硫键形成并加速错误折叠蛋白的溶酶体降解，显著提高重组蛋白产量。
2. **文献名称**: *ERP29 interacts with SERPINB1 to regulate unfolded protein response in cancer cells*
**作者**: Sorensen S. et al.
**摘要**: 本文揭示了ERP29通过结合SERPINB1调控内质网应激反应，维持癌细胞中未折叠蛋白应答(UPR)平衡，其重组表达可缓解应激诱导的细胞凋亡，提示其在肿瘤耐药性中的作用。
3. **文献名称**: *Structural insights into ERP29 function as a chaperone in the early secretory pathway*
**作者**: Hsu C.C. et al.
**摘要**: 通过X射线晶体学解析ERP29重组蛋白的结构，阐明其通过柔性C端结构域捕获未成熟分泌蛋白，辅助早期分泌途径中的蛋白质量控制，为优化重组蛋白生产提供理论依据。
(注：以上文献信息为示例性概括，实际文献需通过学术数据库验证。)
**Background of ERP29 Recombinant Protein**
ERP29 (Endoplasmic Reticulum Protein 29 kDa), also known as ERp29. is a conserved protein disulfide isomerase (PDI)-family member predominantly localized in the endoplasmic reticulum (ER). Unlike classical PDIs, ERP29 lacks a thioredoxin-like catalytic domain, suggesting a distinct role in protein folding and quality control. It is ubiquitously expressed across tissues and plays critical roles in facilitating the maturation, secretion, and stability of client proteins, particularly those with complex disulfide-bonded structures.
Structurally, ERP29 consists of two domains: an N-terminal thioredoxin-like domain and a C-terminal helical domain. The protein functions as a dimer, leveraging its unique architecture to interact with nascent polypeptides and chaperones like BiP/GRP78. Its activity is linked to cellular stress responses, including the unfolded protein response (UPR), where it aids in mitigating ER stress by enhancing protein folding efficiency or targeting misfolded proteins for degradation.
ERP29 has garnered attention in recombinant protein production due to its ability to enhance the yield and solubility of heterologous proteins. Studies show that co-expressing ERP29 with target proteins in expression systems (e.g., mammalian or insect cells) can improve proper folding and secretion, particularly for therapeutic antibodies or complex glycoproteins. Additionally, ERP29 dysregulation is implicated in diseases such as cancer, neurodegenerative disorders, and cystic fibrosis, highlighting its dual significance in basic research and biotechnology. Current research focuses on elucidating its mechanistic roles and optimizing its application in biomanufacturing and therapeutic development.
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