Recombinant Human lspA protein

中文名： 脂蛋白信号肽酶(lspA)重组蛋白
别名： lspA；ls；Lipoprotein signal peptidase

货号: PA2000-1839

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	Human
靶点	lspA
Uniprot No	Q9HVM5
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-169aa
氨基酸序列	MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRSKKSGEAAHG
预测分子量	18,9 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lspA重组蛋白的3篇参考文献示例(注：内容为模拟生成，非真实文献)：

---

1. **标题**: *Cloning and functional characterization of the lspA gene encoding a lipoprotein signal peptidase in Escherichia coli*

**作者**: Smith J, et al.

**摘要**: 研究报道了通过重组技术在大肠杆菌中克隆并表达lspA基因，证实其编码的蛋白酶负责细菌脂蛋白前体的信号肽切割，为革兰氏阴性菌脂蛋白加工机制提供依据。

---

2. **标题**: *Role of recombinant LspA in Staphylococcus aureus virulence and antibiotic resistance*

**作者**: Zhang L, et al.

**摘要**: 通过构建lspA基因敲除突变体及重组蛋白回补实验，证明金黄色葡萄球菌中LspA通过调控脂蛋白成熟影响细菌毒力和β-内酰胺类抗生素耐药性。

---

3. **标题**: *Crystal structure and enzymatic mechanism of the LspA protease from Pseudomonas aeruginosa*

**作者**: Tanaka K, et al.

**摘要**: 利用重组LspA蛋白的纯化与结晶，首次解析了铜绿假单胞菌LspA的3D结构，揭示了其底物识别及催化活性位点，为开发新型抗菌药物提供结构基础。

---

如需真实文献，建议通过PubMed或Google Scholar以关键词“lspA recombinant”、“lipoprotein signal peptidase”进行检索。

背景信息

**Background of LspA Recombinant Protein**

LspA (lipoprotein signal peptidase A) is a bacterial enzyme critical for processing lipoproteins, a class of membrane-associated proteins essential for bacterial viability, virulence, and host-pathogen interactions. It specifically cleaves the signal peptide of precursor lipoproteins, enabling their maturation and proper localization in the bacterial cell envelope. LspA is highly conserved in Gram-negative bacteria, including pathogens like *Escherichia coli*, *Pseudomonas aeruginosa*, and *Salmonella enterica*, making it a potential target for novel antimicrobial therapies.

The recombinant LspA protein is produced through genetic engineering, typically by cloning the *lspA* gene into expression vectors (e.g., in *E. coli*), followed by purification using affinity chromatography. Recombinant LspA retains enzymatic activity, allowing researchers to study its structure-function relationships, substrate specificity, and inhibition mechanisms. Structural studies (e.g., X-ray crystallography or cryo-EM) have revealed its unique aspartic protease-like fold and membrane-embedded catalytic site, providing insights into its role in lipoprotein processing.

Research on LspA recombinant protein is pivotal for developing broad-spectrum antibiotics, particularly as multidrug-resistant bacterial infections rise globally. Inhibitors targeting LspA could disrupt bacterial lipoprotein biogenesis, impairing membrane integrity and virulence. Additionally, LspA studies contribute to understanding bacterial physiology and evolutionary adaptations. Its recombinant form also aids in high-throughput screening for drug candidates and elucidating resistance mechanisms, bridging gaps between basic microbiology and translational antimicrobial development.