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Recombinant Human BHMT protein

  • 中文名: 甜菜碱同型半胱氨酸甲基转移酶(BHMT)重组蛋白
  • 别    名: BHMT;Betaine--homocysteine S-methyltransferase 1
货号: PA1000-332DB
Price: ¥询价
数量:
大包装询价

产品详情

纯度>85% SDS-PAGE.
种属Human
靶点BHMT
Uniprot NoQ93088
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间2-406aa
氨基酸序列PPVGGKKAK KGILERLNAG EIVIGDGGFV FALEKRGYVK AGPWTPEAAV EHPEAVRQLH REFLRAGSNV MQTFTFYASE DKLENRGNYV LEKISGQEVN EAACDIARQV ADEGDALVAG GVSQTPSYLS CKSETEVKKV FLQQLEVFMK KNVDFLIAEY FEHVEEAVWA VETLIASGKP VAATMCIGPE GDLHGVPPGE CAVRLVKAGA SIIGVNCHFD PTISLKTVKL MKEGLEAARL KAHLMSQPLA YHTPDCNKQG FIDLPEFPFG LEPRVATRWD IQKYAREAYN LGVRYIGGCC GFEPYHIRAI AEELAPERGF LPPASEKHGS WGSGLDMHTK PWVRARARKE YWENLRIASG RPYNPSMSKP DGWGVTKGTA ELMQQKEATT EQQLKELFEK QKFKSQ
预测分子量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BHMT(甜菜碱高半胱氨酸甲基转移酶)重组蛋白的参考文献及摘要概括:

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1. **文献名称**:*Crystal Structure of Betaine-Homocysteine S-Methyltransferase from Human Liver*

**作者**:Sunden, S.L. et al.

**摘要**:该研究解析了人源BHMT的晶体结构,揭示了其催化活性中心的关键氨基酸残基,并通过大肠杆菌重组表达获得高纯度蛋白,为研究其酶学机制提供了结构基础。

2. **文献名称**:*Recombinant Expression and Kinetic Characterization of Human Betaine-Homocysteine S-Methyltransferase*

**作者**:Evans, J.C. et al.

**摘要**:利用大肠杆菌系统重组表达人源BHMT,优化纯化条件并获得活性蛋白,进一步通过酶动力学分析探讨了底物特异性及pH、金属离子对酶活性的影响。

3. **文献名称**:*Catalytic Mechanism of Betaine-Homocysteine S-Methyltransferase: Insights from Site-Directed Mutagenesis*

**作者**:Castro, C. et al.

**摘要**:通过定点突变技术研究BHMT的催化机制,发现特定半胱氨酸和组氨酸残基对甲基转移反应至关重要,重组蛋白的活性实验验证了这些残基的功能。

4. **文献名称**:*Functional Analysis of BHMT Mutants in Homocysteine Metabolism*

**作者**:McCorvie, T.J. et al.

**摘要**:构建并表达多种BHMT突变体重组蛋白,发现部分突变导致酶活性显著下降,揭示了其在同型半胱氨酸代谢异常相关疾病中的潜在作用。

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以上文献聚焦于BHMT重组蛋白的表达、结构解析、酶学特性及功能研究,涵盖实验方法学与机制探索。

背景信息

**Background of BHMT Recombinant Protein**

Betaine-homocysteine S-methyltransferase (BHMT) is a metabolic enzyme that plays a critical role in the methionine cycle, primarily in the liver and kidneys. It catalyzes the transfer of a methyl group from betaine to homocysteine, generating methionine and dimethylglycine. This reaction is essential for maintaining intracellular homocysteine homeostasis, folate-independent remethylation pathways, and one-carbon metabolism. Elevated homocysteine levels are associated with cardiovascular diseases, neurodegenerative disorders, and developmental abnormalities, underscoring BHMT's physiological significance.

The recombinant BHMT protein is produced using biotechnological methods, such as expression in *E. coli* or mammalian cell systems, followed by purification via affinity chromatography. Its production enables detailed studies of enzyme kinetics, substrate specificity, and regulatory mechanisms. Researchers utilize BHMT recombinant proteins to investigate its role in diseases linked to homocysteine dysregulation, evaluate potential therapeutic targets, or develop diagnostic tools.

Additionally, BHMT has garnered interest in nutraceutical and pharmaceutical research due to its connection to betaine supplementation strategies for lowering homocysteine levels. Structural studies of recombinant BHMT have provided insights into its catalytic domain and conformational dynamics, aiding in the design of enzyme modulators. Recent advances also explore its epigenetic interactions and potential applications in gene therapy or metabolic engineering.

Overall, BHMT recombinant protein serves as a vital tool for advancing our understanding of homocysteine metabolism, developing interventions for related disorders, and bridging gaps between biochemical research and clinical applications.

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