| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HCy |
| Uniprot No | Q12525 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-324aa |
| 氨基酸序列 | MKRIPIKELIVEHPGKVLILDGGQGTELENRGININSPVWSAAPFTSESFWEPSSQERKVVEEMYRDFMIAGANILMTITYQANFQSISENTSIKTLAAYKRFLDKIVSFTREFIGEERYLIGSIGPWAAHVSCEYTGDYGPHPENIDYYGFFKPQLENFNQNRDIDLIGFETIPNFHELKAILSWDEDIISKPFYIGLSVDDNSLLRDGTTLEEISVHIKGLGNKINKNLLLMGVNCVSFNQSALILKMLHEHLPGMPLLVYPNSGEIYNPKEKTWHRPTNKLDDWETTVKKFVDNGARIIGGCCRTSPKDIAEIASAVDKYS |
| 预测分子量 | 40.7 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. |
以下是关于HCy(假设为同型半胱氨酸相关)重组蛋白的参考文献示例，内容基于典型研究方向整理：
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1. **标题**：*Expression and Purification of Recombinant Human Cystathionine Beta-Synthase for Homocysteine Metabolism Studies*
**作者**：Skovby, F., Kraus, J.P.
**摘要**：研究报道了在大肠杆菌中高效表达并纯化重组人胱硫醚β-合酶(CBS)，该酶参与同型半胱氨酸代谢。通过优化表达条件，获得高活性蛋白，为探究高同型半胱氨酸血症的病理机制及药物筛选提供工具。
2. **标题**：*Functional Characterization of Recombinant Methylenetetrahydrofolate Reductase Mutants in Hyperhomocysteinemia*
**作者**：Goyette, P., Rozen, R.
**摘要**：本研究在昆虫细胞系统中表达重组人MTHFR蛋白，分析常见突变体(如C677T)的酶活性和热稳定性，揭示其导致同型半胱氨酸水平升高的分子机制，为遗传性代谢疾病研究提供依据。
3. **标题**：*A Recombinant Enzymatic Biosensor for Ultrasensitive Detection of Serum Homocysteine*
**作者**：Smith, J., Wang, L.
**摘要**：开发了一种基于重组胱硫醚γ-裂解酶(CSE)的荧光生物传感器，用于检测血清中的同型半胱氨酸。该方法灵敏度高、特异性强，为心血管疾病风险评估提供新策略。
4. **标题**：*Crystal Structure of Recombinant Homocysteine-Binding Protein HcyS from Escherichia coli*
**作者**：Lee, C., Leustek, T.
**摘要**：解析了来源于大肠杆菌的同型半胱氨酸结合蛋白HcyS的重组晶体结构，阐明其底物结合位点及催化机制，为设计同型半胱氨酸代谢调控剂奠定结构基础。
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**注**：以上文献为示例性质，实际引用时建议通过PubMed、Web of Science等数据库检索最新且真实存在的文献，并核对作者及摘要准确性。若HCy指代特定蛋白(如某专利命名)，需结合具体背景调整关键词。
**Background of HCy Recombinant Protein**
Homocysteine (HCy) is a sulfur-containing amino acid derived from methionine metabolism, playing a critical role in cellular methylation and redox regulation. Elevated homocysteine levels (hyperhomocysteinemia) are associated with cardiovascular diseases, neurodegenerative disorders, and developmental abnormalities. To study its molecular mechanisms and therapeutic potential, researchers have developed recombinant HCy-related proteins, including enzymes and binding proteins involved in its metabolic pathways.
HCy recombinant proteins are typically produced using *in vitro* expression systems, such as *E. coli* or mammalian cell cultures, to ensure high purity and functional activity. Key targets include cystathionine β-synthase (CBS), methylenetetrahydrofolate reductase (MTHFR), and methionine synthase—enzymes critical for HCy metabolism. These recombinant proteins enable detailed structural analysis, enzyme kinetics studies, and drug screening for disorders linked to homocysteine imbalance.
In biomedical research, HCy recombinant proteins are utilized to investigate pathological processes, such as endothelial dysfunction, oxidative stress, and DNA hypomethylation. They also serve as antigens for antibody development in diagnostic assays to measure HCy levels or detect genetic mutations affecting its metabolism. Additionally, recombinant enzymes like CBS are explored for enzyme replacement therapies in rare genetic disorders like homocystinuria.
Recent advancements in protein engineering, such as site-directed mutagenesis and fusion tags, have improved the stability and functionality of HCy-related recombinant proteins. However, challenges remain, including maintaining post-translational modifications in prokaryotic systems and scaling production for clinical applications. Ongoing research aims to optimize these tools for personalized medicine and targeted therapies, emphasizing their role in understanding and mitigating homocysteine-related pathologies.
This field bridges biochemistry, genetics, and clinical medicine, offering insights into metabolic regulation and novel intervention strategies.
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