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Recombinant Human TYMP protein

  • 中文名: 胸腺嘧啶磷酸化酶(TYMP)重组蛋白
  • 别    名: TYMP;ECGF1;Thymidine phosphorylase
货号: PA1000-3351
Price: ¥询价
数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点TYMP
Uniprot NoP19971
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间11-482aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMAPPAPGDFSGEGSQGLPDPSPEPKQLPEL IRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETS VLTQALAQSGQQLEWPEAWRQQLVDKHSTGGVGDKVSLVLAPALAACGCK VPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSE QLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGA AVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEE ALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSA LGRFERMLAAQGVDPGLARALCSGSPAERRQLLPRAREQEELLAPADGTV ELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLR VHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPPQQ
预测分子量51 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.

参考文献

以下是关于TYMP(胸腺嘧啶磷酸化酶)重组蛋白的示例参考文献(文献信息为示例,建议通过学术数据库核实具体内容):

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1. **文献名称**: *"Recombinant Thymidine Phosphorylase from E. coli: Production and Antiangiogenic Activity in Solid Tumors"*

**作者**: Smith A, et al.

**摘要**: 研究报道了通过大肠杆菌表达系统高效生产重组TYMP蛋白,并验证其体外酶活性。实验证明该重组蛋白能抑制肿瘤血管生成,为抗癌治疗提供了潜在策略。

2. **文献名称**: *"High-Yield Soluble Expression of Human TYMP in Pichia pastoris for Drug Screening"*

**作者**: Zhang Y, et al.

**摘要**: 采用毕赤酵母系统实现TYMP的可溶性表达,优化纯化流程后获得高活性蛋白。该研究为基于TYMP结构的药物开发(如抗代谢疾病疗法)提供了可靠蛋白来源。

3. **文献名称**: *"Functional Characterization of a Novel TYMP Variant Using Recombinant Protein Analysis in Mitochondrial Disorders"*

**作者**: Johnson R, et al.

**摘要**: 通过重组TYMP蛋白的功能实验,解析了某基因突变导致线粒体脑肌病(MNGIE)的分子机制,为基因治疗提供了理论依据。

4. **文献名称**: *"Crystal Structure of Recombinant Human TYMP and Insights into Substrate Binding"*

**作者**: Tanaka K, et al.

**摘要**: 解析了重组TYMP蛋白的晶体结构,揭示了其底物结合位点及催化机制,为设计特异性TYMP抑制剂奠定结构基础。

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**提示**:实际文献可通过PubMed、Web of Science等平台,以关键词“TYMP recombinant”“thymidine phosphorylase expression”检索,并筛选近5年研究。

背景信息

**Background of TYMP Recombinant Protein**

Thymidine phosphorylase (TYMP), also known as platelet-derived endothelial cell growth factor (PD-ECGF) or gliostatin, is a multifunctional enzyme encoded by the *TYMP* gene. It catalyzes the reversible conversion of thymidine to thymine and 2-deoxy-D-ribose-1-phosphate, playing a critical role in nucleotide metabolism and salvage pathways. Beyond its metabolic function, TYMP exhibits angiogenic properties by promoting endothelial cell migration and proliferation, partly mediated through its catalytic byproduct, 2-deoxy-D-ribose. This has linked TYMP to pathological conditions such as tumor angiogenesis, inflammation, and wound healing.

Structurally, TYMP is a homodimeric protein with each subunit containing a conserved phosphorylase active site. Its recombinant form is typically produced in heterologous expression systems (e.g., *E. coli*, mammalian cells) to ensure high purity and bioactivity for research and therapeutic applications. Recombinant TYMP retains enzymatic and angiogenic functions, making it valuable for studying mechanisms in cancer biology, ischemic diseases, and mitochondrial disorders.

Clinically, TYMP is implicated in mitochondrial neurogastrointestinal encephalomyopathy (MNGIE), a rare autosomal recessive disorder caused by *TYMP* mutations. Recombinant TYMP has been explored as an enzyme replacement therapy to restore thymidine homeostasis in MNGIE patients. Additionally, TYMP overexpression in tumors correlates with resistance to fluoropyrimidine-based chemotherapy (e.g., 5-fluorouracil), highlighting its role as a predictive biomarker.

Overall, TYMP recombinant protein serves as a vital tool for dissecting its biological roles and developing targeted therapies for cancer and genetic metabolic diseases.

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