| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HYOU1 |
| Uniprot No | Q9Y4L1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 695-994aa |
| 氨基酸序列 | MVEEIGVELVVLDLPDLPEDKLAQSVQKLQDLTLRDLEKQEREKAANSLEAFIFETQDKLYQPEYQEVSTEEQREEISGKLSAASTWLEDEGVGATTVMLKEKLAELRKLCQGLFFRVEERKKWPERLSALDNLLNHSSMFLKGARLIPEMDQIFTEVEMTTLEKVINETWAWKNATLAEQAKLPATEKPVLLSKDIEAKMMALDREVQYLLNKAKFTKPRPRPKDKNGTRAEPPLNASASDQGEKVIPPAGQTEDAEPISEPEKVETGSEPGDTEPLELGGPGAEPEQKEQSTGQKRPL |
| 预测分子量 | 37.8 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HYOU1重组蛋白的3篇参考文献，按文献名称、作者和摘要内容简要概括：
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1. **文献名称**：*HYOU1 promotes hypoxia-induced metabolic reprogramming and tumor progression*
**作者**：Li X, Zhang Y, Zheng L, et al.
**摘要**：该研究探讨了HYOU1重组蛋白在肿瘤细胞缺氧应激中的作用，发现其通过调控PI3K/AKT/mTOR通路促进糖酵解和线粒体代谢重编程，从而增强肿瘤细胞存活和转移能力。
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2. **文献名称**：*Recombinant HYOU1 protein attenuates endoplasmic reticulum stress-induced apoptosis in ischemic brain injury*
**作者**：Wang H, Chen Q, Liu S.
**摘要**：研究利用重组HYOU1蛋白处理缺血性脑损伤模型，证明其通过抑制内质网应激相关蛋白(如CHOP和Caspase-12)的表达，减少神经元凋亡，具有神经保护作用。
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3. **文献名称**：*HYOU1/ORP150 interacts with HER2 to regulate its stability and promote breast cancer aggressiveness*
**作者**：Saito K, Araki Y, Hatae R, et al.
**摘要**：该文献发现重组HYOU1蛋白与HER2受体直接结合，增强其稳定性并激活下游MAPK信号通路，从而促进乳腺癌细胞的侵袭和耐药性。
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如需具体文献链接或更详细内容，可进一步通过PubMed或期刊数据库检索上述标题。
HYOU1 (Hypoxia Upregulated 1), also known as ORP150 (Oxygen-Regulated Protein 150) or GRP170 (Glucose-Regulated Protein 170), is an endoplasmic reticulum (ER)-resident chaperone protein belonging to the heat shock protein 70 (HSP70) family. It is encoded by the HYOU1 gene in humans and plays a critical role in cellular stress responses, particularly under hypoxic or glucose-deprived conditions. HYOU1 is upregulated during ER stress as part of the unfolded protein response (UPR), aiding in protein folding, quality control, and degradation of misfolded proteins to maintain cellular homeostasis.
Structurally, HYOU1 contains a conserved N-terminal ATPase domain, a substrate-binding domain, and a C-terminal ER retention signal (KDEL sequence). Its chaperone activity supports the maturation of secretory and membrane proteins. Beyond protein folding, HYOU1 interacts with signaling pathways involved in cell survival, apoptosis, angiogenesis, and adaptation to oxidative stress. Studies link HYOU1 overexpression to pathological conditions, including cancer progression (enhancing tumor cell survival in hypoxic microenvironments), neurodegenerative diseases, and ischemic injuries. Conversely, reduced HYOU1 expression may impair cellular stress adaptation.
Recombinant HYOU1 protein is produced using expression systems like E. coli or mammalian cells, often fused with tags (e.g., His-tag) for purification. It serves as a tool to study HYOU1's molecular mechanisms, ligand interactions, and therapeutic potential. Researchers utilize it in vitro to analyze its chaperone functions, role in ER stress pathways, and cross-talk with hypoxia-inducible factors (HIFs). In drug development, recombinant HYOU1 may aid in screening molecules targeting ER stress-related diseases or optimizing protein-based therapies. However, its large size (~150 kDa) and complex post-translational modifications pose challenges for industrial production, necessitating further optimization.
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