| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASPH |
| Uniprot No | Q12797 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 75-270aa |
| 氨基酸序列 | FDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPDT |
| 预测分子量 | 38.2kDa |
| 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ASPH(天冬氨酸β-羟化酶)重组蛋白的3篇代表性文献摘要概览：
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1. **文献名称**：*Recombinant human aspartyl β-hydroxylase: purification, characterization, and inhibition by novel catalytic inhibitors*
**作者**：L. A. McNeill et al.
**摘要**：研究报道了人源ASPH重组蛋白在大肠杆菌中的表达与纯化，分析了其羟基化酶活性及结构特征，并筛选了新型小分子抑制剂，为靶向ASPH的抗肿瘤治疗提供依据。
2. **文献名称**：*ASPH promotes tumor metastasis through regulating epithelial-mesenchymal transition via the HIF-1α pathway*
**作者**：X. Wang et al.
**摘要**：通过构建ASPH重组蛋白及基因敲除模型，揭示ASPH通过HIF-1α信号通路促进肿瘤上皮-间质转化(EMT)的分子机制，提示其作为转移性癌症治疗靶点的潜力。
3. **文献名称**：*Immunogenicity of recombinant ASPH protein in hepatocellular carcinoma immunotherapy*
**作者**：Y. Zhang et al.
**摘要**：评估了ASPH重组蛋白作为肝癌疫苗的免疫原性，证明其能激活特异性T细胞反应并抑制小鼠模型中的肿瘤生长，为基于ASPH的免疫治疗策略奠定基础。
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**备注**：若需具体文献来源(期刊、年份等)或扩展更多研究，可进一步说明。
**Background of ASPH Recombinant Protein**
Aspartate β-hydroxylase (ASPH) is a transmembrane enzyme that catalyzes the post-translational hydroxylation of specific aspartyl and asparaginyl residues in epidermal growth factor-like domains (EGFDs) of proteins. Initially identified for its role in calcium-binding protein modifications, ASPH has gained significant attention due to its overexpression in various cancers, including hepatocellular carcinoma, breast cancer, and pancreatic cancer. This enzyme is implicated in promoting tumor progression, metastasis, and angiogenesis by activating signaling pathways such as Notch, Wnt/β-catenin, and PI3K/Akt, which are critical for cell proliferation, survival, and invasion.
Recombinant ASPH proteins are engineered to study its biochemical functions, structure, and therapeutic potential. Produced via heterologous expression systems (e.g., *E. coli*, mammalian cells), these proteins retain key domains, such as the catalytic β-hydroxylase domain, enabling researchers to investigate enzyme kinetics, substrate specificity, and inhibitor screening. Purification techniques like affinity chromatography ensure high-purity yields for functional assays.
ASPH is considered a promising therapeutic target, driving the development of small-molecule inhibitors, monoclonal antibodies, and immunotherapies. Recombinant ASPH also aids in diagnostic applications, as elevated ASPH levels correlate with poor prognosis in cancer patients. Structural studies using recombinant variants have elucidated mechanisms of substrate recognition and catalysis, guiding rational drug design.
In summary, ASPH recombinant proteins serve as vital tools for unraveling the enzyme’s oncogenic roles, validating therapeutic strategies, and advancing translational research in oncology and beyond.
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