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Recombinant Human PBLD protein

  • 中文名: 吩嗪生物合成样含结构域蛋白(PBLD)重组蛋白
  • 别    名: PBLD;MAWBP;Phenazine biosynthesis-like domain-containing protein
货号: PA1000-2291
Price: ¥询价
数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点PBLD
Uniprot NoP30039
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-288aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMKLPIFIADAFTARAFRGNPAAVCLLENEL DEDMHQKIAREMNLSETAFIRKLHPTDNFAQSSCFGLRWFTPASEVPLCG HATLASAAVLFHKIKNMNSTLTFVTLSGELRARRAEDGIVLDLPLYPAHP QDFHEVEDLIKTAIGNTLVQDICYSPDTQKLLVRLSDVYNRSFLENLKVN TENLLQVENTGKVKGLILTLKGEPGGQTQAFDFYSRYFAPWVGVAEDPVT GSAHAVLSSYWSQHLGKKEMHAFQCSHRGGELGISLRPDGRVDIRGGAAV VLEGTLTA
预测分子量34 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PBLD(假设为苯丙氨酸解氨酶,Phenylalanine Ammonia-Lyase)重组蛋白的模拟参考文献示例:

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1. **文献名称**:*High-level expression of recombinant PBLD in Escherichia coli and its enzymatic characterization*

**作者**:Li, X., Zhang, Y., & Wang, L.

**摘要**:研究报道了在大肠杆菌BL21中成功表达具有活性的重组PBLD蛋白,通过IPTG诱导优化表达条件,纯化后测定其最适反应温度和pH,证实其在苯丙氨酸代谢中的高效催化活性。

2. **文献名称**:*Structural insights into PBLD through X-ray crystallography and its biotechnological applications*

**作者**:Chen, J., Smith, R., & Tanaka, M.

**摘要**:利用X射线晶体学解析了重组PBLD的三维结构,揭示了其底物结合位点的关键氨基酸残基,为酶工程改造以增强稳定性和活性提供了理论依据。

3. **文献名称**:*Yeast-based production of recombinant PBLD for phenylketonuria therapy*

**作者**:Gupta, S., & Kim, H.

**摘要**:开发了一种在毕赤酵母中高效分泌表达重组PBLD的策略,证明其能有效降解血液中的苯丙氨酸,为苯丙酮尿症(PKU)的酶替代疗法提供了潜在解决方案。

4. **文献名称**:*Optimization of fermentation conditions for PBLD recombinant protein in Pichia pastoris*

**作者**:Wang, Q., Zhao, F., & Liu, G.

**摘要**:通过响应面法优化巴斯德毕赤酵母的发酵参数(温度、pH、甲醇浓度),将重组PBLD的产量提高3倍,并验证了其工业规模化生产的可行性。

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注:以上文献为模拟内容,实际研究中需根据具体研究方向检索真实数据库(如PubMed、Web of Science)。

背景信息

**Background of PBLD Recombinant Proteins**

PBLD (Phenazine Biosynthesis-Like Domain) recombinant proteins are engineered variants derived from naturally occurring proteins associated with secondary metabolite biosynthesis, particularly in microorganisms. The term "PBLD" originates from conserved structural domains resembling those in phenazine-producing enzymes, which are critical for synthesizing aromatic compounds with antimicrobial and redox-active properties. These domains often facilitate interactions with cofactors or substrates involved in specialized metabolic pathways.

Recombinant PBLD proteins are typically produced via genetic engineering, where the target gene is cloned into expression vectors (e.g., plasmids) and introduced into host systems like *E. coli* or yeast. Advanced purification techniques, such as affinity chromatography with His-tags, ensure high yields and purity. Structural studies (e.g., X-ray crystallography) have revealed their modular architecture, including conserved α/β folds and active-site residues critical for enzymatic activity.

Functionally, PBLD proteins are hypothesized to participate in biosynthetic pathways, potentially catalyzing reactions in the formation of bioactive molecules. Their roles in redox regulation or stress response have also been explored, linking them to microbial survival and pathogenicity. In biotechnology, recombinant PBLD variants are leveraged for enzyme engineering, drug discovery, or as biocatalysts in synthesizing complex organic compounds. Additionally, their study aids in understanding evolutionary relationships within microbial secondary metabolism.

Despite progress, challenges remain in elucidating precise mechanistic roles and optimizing industrial applications. Ongoing research focuses on structure-function relationships, substrate specificity, and harnessing their catalytic versatility for sustainable bioprocesses.

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