| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBL4 |
| Uniprot No | P11441 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-157 aa |
| 活性数据 | MQLTVKALQG RECSLQVPED ELVSTLKQLV SEKLNVPVRQ QRLLFKGKAL ADGKRLSDYS IGPNSKLNLV VKPLEKVLLE EGEAQRLADS PPPQVWQLIS KVLARHFSAA DASRVLEQLQ RDYERSLSRL TLDDIERLAS RFLHPEVTET MEKGFSK |
| 分子量 | 17.7 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. |
以下是与重组人UBL4蛋白相关的3篇文献示例，涵盖功能机制、结构解析及疾病应用研究：
1. **文献名称**: "UBL4A is essential for endoplasmic reticulum-associated protein degradation through interaction with chaperones"
**作者**: Lin Y, et al.
**摘要**: 该研究揭示UBL4A通过结合分子伴侣HSP70和泛素连接酶复合物，调控错误折叠蛋白的内质网相关降解(ERAD)。重组人UBL4A的体外功能实验证实其作为衔接蛋白介导底物识别与泛素化过程。
2. **文献名称**: "Crystal structure of human UBL4A and its functional role in Wnt/β-catenin signaling"
**作者**: Chen L, et al.
**摘要**: 通过解析重组人UBL4A的晶体结构(PDB ID: 4RZP)，研究发现其N端泛素样结构域直接结合β-catenin，抑制Wnt通路异常激活，为癌症治疗的靶向策略提供理论依据。
3. **文献名称**: "UBL4A inhibits hepatocellular carcinoma progression by promoting c-Myc ubiquitination"
**作者**: Wang T, et al.
**摘要**: 研究利用重组UBL4A蛋白证明其通过增强c-Myc的泛素化降解抑制肝细胞癌增殖，体内实验显示UBL4A过表达显著降低肿瘤生长，提示其作为抑癌蛋白的潜在临床应用价值。
**备注**：以上文献标题与摘要为示例性内容，建议通过PubMed或Web of Science以“UBL4A”或“UBL4A recombinant”为关键词检索最新研究。部分研究可能使用别称(如GDX或UBL4)进行发表，需注意术语差异。
Recombinant human UBL4A (Ubiquitin-like 4A), also known as GET5 or BAG5. is a member of the ubiquitin-like (UBL) protein family. Unlike ubiquitin, UBL4A does not conjugate to target proteins but functions as a co-chaperone in cellular protein quality control. It harbors an N-terminal UBL domain and a C-terminal BAG domain, enabling interactions with molecular chaperones like HSP70 and components of the GET (Guided Entry of Tail-anchored proteins) pathway. UBL4A plays dual roles: it assists in the biogenesis of tail-anchored membrane proteins by facilitating their delivery to the endoplasmic reticulum (ER) via the GET complex and participates in cytosolic protein degradation by linking misfolded proteins to the 26S proteasome. Studies highlight its involvement in ER-associated degradation (ERAD) and stress responses, including heat shock and oxidative stress. UBL4A is widely expressed, with elevated levels in the brain, liver, and testes. Dysregulation of UBL4A has been implicated in neurodegenerative diseases, cancer progression, and immune disorders. Its recombinant form, generated through bacterial or mammalian expression systems, serves as a critical tool for in vitro studies exploring protein homeostasis, chaperone networks, and disease mechanisms. Recent research also suggests potential roles in DNA repair and apoptosis regulation.
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