Recombinant E.coli alaA protein

中文名： 谷氨酸-丙酮酸转氨酶(alaA)重组蛋白
别名： alaA；ACVRLK1；ALK1；Serine/threonine-protein kinase receptor R3

货号: PA2000-2808

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	E.coli
靶点	alaA
Uniprot No	P0A959
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-405aa
氨基酸序列	MSPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAPDEILVDVIRNLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIGNGVSELIVQAMQALLNSGDEMLVPAPDYPLWTAAVSLSSGKAVHYLCDESSDWFPDLDDIRAKITPRTRGIVIINPNNPTGAVYSKELLMEIVEIARQHNLIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSKTYRVAGFRQGWMVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFITPGGRLYEQRNRAWELINDIPGVSCVKPRGALYMFPKIDAKRFNIHDDQKMVLDFLLQEKVLLVQGTAFNWPWPDHFRIVTLPRVDDIELSLSKFARFLSGYHQL
预测分子量	61.5 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

以下是关于alaA重组蛋白的模拟参考文献示例(仅供参考，实际文献需通过学术数据库查询)：

1. **标题**: "Heterologous Expression and Enzymatic Characterization of alaA-Encoded Alanine Aminotransferase from *Bacillus subtilis*"

**作者**: Zhang, Y. et al.

**摘要**: 本研究在大肠杆菌中成功表达了来自枯草芽孢杆菌的alaA基因编码的丙氨酸氨基转移酶，通过纯化获得重组蛋白，并分析了其最适pH、温度及底物特异性，证实其在丙氨酸代谢中的关键作用。

2. **标题**: "Functional Role of Recombinant alaA Protein in Bacterial Alanine Biosynthesis"

**作者**: Lee, S. & Kim, H.

**摘要**: 文章通过基因敲除和回补实验，结合重组alaA蛋白的体外活性测定，揭示了该酶在铜绿假单胞菌丙氨酸合成途径中的必要性及其对菌体生长的调控机制。

3. **标题**: "High-Yield Purification of alaA Recombinant Protein via Nickel-Affinity Chromatography"

**作者**: Smith, J. et al.

**摘要**: 优化了alaA重组蛋白的纯化流程，采用His标签亲和层析技术，获得高纯度蛋白，并验证其稳定性，为后续结构解析奠定基础。

4. **标题**: "Biotechnological Application of alaA Recombinant Enzyme in Industrial Alanine Production"

**作者**: Wang, L. et al.

**摘要**: 探讨了重组alaA酶在固定化反应器中的催化效率，证明其可提升丙氨酸工业化生产的产率，具有潜在经济价值。

**注意**：以上为模拟数据，实际文献需通过PubMed、Web of Science等平台检索。建议结合具体研究方向调整关键词(如物种名、应用领域等)。

背景信息

AlaA recombinant protein is a engineered form of the alanine aminotransferase (ALT) enzyme, typically derived from bacterial or eukaryotic sources through genetic recombination technology. ALT enzymes, classified under EC 2.6.1.2. play a pivotal role in amino acid metabolism by catalyzing the reversible transfer of an amino group between alanine and α-ketoglutarate to produce pyruvate and glutamate. This reaction is critical in the glucose-alanine cycle, linking carbohydrate and nitrogen metabolism in organisms.

The recombinant AlaA protein is commonly produced by cloning the *alaA* gene into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production with high purity and consistency. Its recombinant form offers advantages over native enzymes, including enhanced stability, customizable activity, and reduced batch-to-batch variability, making it valuable for industrial and research applications.

In biotechnology, AlaA is utilized in metabolic engineering to optimize microbial pathways for amino acid synthesis, biofuel production, or pharmaceutical intermediates. In medicine, it serves as a biomarker for liver injury, as ALT levels in blood correlate with hepatic damage. Researchers also employ recombinant AlaA to study enzyme kinetics, substrate specificity, and to develop inhibitors for therapeutic purposes, such as targeting metabolic disorders or parasitic infections.

Recent studies focus on protein engineering to improve AlaA's catalytic efficiency or thermostability, expanding its utility in harsh industrial conditions. Additionally, its role in nitrogen metabolism has implications for agricultural research, particularly in enhancing crop nitrogen-use efficiency. As a well-characterized enzyme, AlaA continues to be a model system for understanding pyridoxal 5′-phosphate (PLP)-dependent enzymes and their regulatory mechanisms.