| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERP44 |
| Uniprot No | Q9BS26 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-406aa |
| 氨基酸序列 | MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWAGSMEITSLDTENIDE ILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVD CDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKS DPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAF LSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKC VPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEK GTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIP GKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLA PSEYRYTLLRDRDEL |
| 预测分子量 | 48 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ERP44重组蛋白的3篇参考文献的简要整理：
1. **文献名称**：ERP44 modulates secretion of disulfide-bonded proteins in mammalian cells
**作者**：Anelli T, et al.
**摘要**：研究揭示了ERP44作为内质网分子伴侣，通过调控二硫键形成影响重组蛋白(如IgM和血管性血友病因子)的分泌效率，其缺失导致蛋白质异常聚集。
2. **文献名称**：The role of ERP44 in mediating thiol-dependent retention in the endoplasmic reticulum
**作者**：Wang Q, et al.
**摘要**：该文献证明ERP44通过与蛋白二硫异构酶(PDI)协同作用，调控重组蛋白的正确折叠及内质网滞留机制，其C端结构域对结合底物蛋白至关重要。
3. **文献名称**：Calcium-dependent regulation of ERP44’s chaperone activity for recombinant cargo proteins
**作者**：Sannino S, et al.
**摘要**：研究发现ERP44的分子伴侣活性受内质网钙离子浓度调控，低钙环境增强其对重组分泌蛋白(如抗体轻链)的质量控制能力，提示其在重组表达系统中的优化应用价值。
注：以上文献信息为示例性概括，实际文献需通过PubMed或Web of Science等平台检索确认。
ERP44 (Endoplasmic Reticulum Protein 44) is a member of the protein disulfide isomerase (PDI) family, primarily localized in the endoplasmic reticulum (ER). It plays a critical role in oxidative protein folding, quality control, and calcium homeostasis. Structurally, ERP44 contains a thioredoxin-like domain with three conserved cysteine residues, enabling its redox-active function in catalyzing disulfide bond formation and isomerization. Unlike other PDIs, ERP44 uniquely lacks a C-terminal ER-retention signal but is retained in the ER through dynamic interactions with client proteins or chaperones.
A key feature of ERP44 is its pH-sensitive chaperone activity. It binds to partially folded or misfolded proteins in the mildly acidic ER environment, preventing their premature secretion and facilitating proper folding. ERP44 also regulates the assembly of multimeric proteins, such as IgM antibodies and adiponectin, by mediating intermolecular disulfide bonds. Additionally, it interacts with glutathione to maintain redox balance and participates in ER stress responses, modulating the unfolded protein response (UPR) pathway.
ERP44's role extends to calcium signaling, as it binds Ca²⁺ ions and influences ER calcium storage. Dysregulation of ERP44 is linked to diseases, including neurodegenerative disorders, cancer, and diabetes. For instance, its overexpression in tumors may promote cell survival under hypoxic or stressed conditions, while deficiencies impair secretory protein production.
Recombinant ERP44 is widely used in biotechnology to study ER-associated processes, optimize protein production in expression systems, and develop therapies targeting protein misfolding diseases. Its unique ability to stabilize labile proteins makes it valuable for industrial and therapeutic protein manufacturing. Research continues to explore its regulatory mechanisms and potential as a biomarker or therapeutic target.
×
