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Recombinant E.coli CNCbl protein

  • 中文名: 氰钴胺素(CNCbl)牛血清白蛋白偶联物
  • 别    名: CNCbl;Cyanocobalamin reductase / alkylcobalamin dealkylase
货号: PA2000-412DB
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属E.coli
靶点CNCbl
Uniprot NoC1E237
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-300aa
氨基酸序列MKKPEPVVKVDETGPPKAAVAGAVGVAVAVAWRLFISRMRNAGGAGRNNAWKTVTADAKEKLAAAGFDIVAPLKLRWYNEIAPDSAKIAPGGAMGEDALVILVGNSAALWPVFCDAHNARPEIGDAENPVDTYVDIEVNRVFRGKIRRVFYAHETKPGRLVAVQRMAHVAGVAHLDERSHLSIHPTLGPWLAFRAVVVLDDARGPGDGQKPRPPPNPLAFDPSARARVDEAFDDALDGYEAPGGPSEGQWRLWVAVRDAVEPGHPARYPEDQVAYHYNCLDGRERARIRSRLRGGFEPSD
预测分子量32,5 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3-4条关于 **CNCbl(钴胺素,维生素B12)重组蛋白** 的参考文献示例及其摘要概括:

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1. **文献名称**:*"Expression and Purification of Recombinant Human Transcobalamin in E. coli for Vitamin B12 Delivery Studies"*

**作者**:Smith A, et al.

**摘要**:研究报道了利用大肠杆菌表达系统高效表达和纯化重组人转钴胺素(Transcobalamin),该蛋白可特异性结合CNCbl,并探究其在维生素B12靶向递送中的应用潜力。

2. **文献名称**:*"Engineering a Cyanocobalamin-Binding Protein from Lactobacillus reuteri for Biosensor Applications"*

**作者**:Johnson R, et al.

**摘要**:通过基因工程改造乳酸菌来源的钴胺素结合蛋白,优化其与CNCbl的结合亲和力,开发出用于检测维生素B12水平的高灵敏度生物传感器。

3. **文献名称**:*"Structural Insights into the Binding Mechanism of CNCbl to Recombinant Intrinsic Factor"*

**作者**:Lee S, et al.

**摘要**:通过X射线晶体学解析重组内因子(Intrinsic Factor)与CNCbl的复合物结构,揭示了二者相互作用的分子机制,为维生素B12吸收障碍疾病的治疗提供依据。

4. **文献名称**:*"Heterologous Production of a Cyanocobalamin-Dependent Enzyme in Saccharomyces cerevisiae"*

**作者**:Chen X, et al.

**摘要**:在酵母中异源表达依赖CNCbl的甲硫氨酸合成酶,研究重组酶活性与钴胺素辅因子的结合关系,为维生素B12依赖性代谢工程提供新策略。

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注:以上文献为示例,实际引用时请核对真实存在的论文信息及数据库(如PubMed、ScienceDirect)。如需具体文献,可进一步提供研究方向或补充关键词。

背景信息

**Background of CNCbl Recombinant Proteins**

Cyanocobalamin (CNCbl), a form of vitamin B12. plays a critical role in cellular metabolism as a cofactor for enzymes involved in DNA synthesis, energy production, and nervous system function. Recombinant proteins incorporating CNCbl or its derivatives have gained attention in biotechnology and therapeutic research due to their potential to address B12 deficiency-related disorders and enhance targeted drug delivery systems.

The development of CNCbl recombinant proteins typically involves genetic engineering techniques to fuse CNCbl-binding domains or analogs with therapeutic or functional proteins. For instance, B12-dependent enzymes or transport proteins, such as intrinsic factor (IF) or transcobalamin (TC), are often utilized as scaffolds. These engineered proteins leverage CNCbl’s high-affinity binding to improve stability, bioavailability, or tissue-specific targeting.

In therapeutics, CNCbl recombinant systems are explored for treating pernicious anemia, neurodegenerative diseases, and metabolic disorders. Their ability to cross biological barriers, including the blood-brain barrier, makes them promising carriers for CNS-targeted therapies. Additionally, CNCbl’s role in bacterial metabolism has spurred applications in industrial biotechnology, such as optimizing microbial production of biofuels or fine chemicals.

Recent advances focus on optimizing expression systems (e.g., *E. coli* or yeast) to enhance yield and functionality. Challenges include maintaining protein stability during CNCbl conjugation and minimizing immunogenicity. Ongoing research also investigates hybrid systems combining CNCbl with nanoparticles or antibodies for multifunctional platforms.

Overall, CNCbl recombinant proteins represent a versatile toolset bridging nutrition, medicine, and biomanufacturing, driven by the vitamin’s unique biochemical properties and compatibility with engineered biological systems.

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