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Recombinant Human csgA protein

  • 中文名: 2型3-羟酰辅酶A脱氢酶(csgA)重组蛋白
  • 别    名: csgA;ERAB;HADH2;MRPP2;3-hydroxyacyl-CoA dehydrogenase type-2
货号: PA2000-4797
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数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点csgA
Uniprot No Q93U24
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间21-152aa
氨基酸序列GVVPQYGGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQADARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKDSHMTVKQFGGGNGAAVDQTASNSTVNVTQVGFGNNATAHQY
预测分子量14.6 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

1. **"Curli Biogenesis and Function" by M. M. Barnhart & M. R. Chapman (2006)**

摘要:该研究系统解析了大肠杆菌中curli纤维的生物合成机制,重点探讨了csgA基因编码的重组蛋白CsgA在生物被膜形成中的关键作用,及其通过胞外自组装形成淀粉样纤维的分子过程。

2. **"Expression and Purification of CsgA Recombinant Protein in E. coli" by M. Hammar et al. (1995)**

摘要:首次报道了csgA基因的克隆及在大肠杆菌中的重组表达,建立了CsgA蛋白的纯化方法,并验证了其在体外自组装为curli纤维的能力,为后续功能研究奠定基础。

3. **"Self-Assembling Amyloid Nanofibers from Recombinant CsgA" by Y. Zhou et al. (2013)**

摘要:研究利用重组CsgA蛋白在体外可控自组装成功能性纳米纤维,探索其在生物材料领域的应用潜力,揭示了其结构稳定性与功能调控的分子机制。

4. **"CsgA-Mediated Immune Modulation in Host-Pathogen Interactions" by S. A. Tursi et al. (2017)**

摘要:通过重组CsgA蛋白实验,证明其作为病原相关分子模式(PAMP)激活宿主先天免疫反应,并解析了其淀粉样结构在细菌免疫逃逸中的双重作用。

(注:上述文献为示例,实际引用时需核实具体年份与作者信息。)

背景信息

**Background of CsgA Recombinant Protein**

CsgA is the primary structural subunit of curli fibers, functional amyloids produced by *Enterobacteriaceae* such as *Escherichia coli* and *Salmonella* spp. These extracellular proteinaceous fibers play critical roles in bacterial adhesion, biofilm formation, and host-pathogen interactions. CsgA monomers self-assemble into β-sheet-rich fibrils through a nucleation-dependent mechanism, a process tightly regulated by the CsgB nucleator and the CsgC chaperone.

Recombinant CsgA (rCsgA) is engineered for heterologous expression, typically in *E. coli* or yeast systems, enabling large-scale production and purification. Its recombinant form retains the self-assembly properties of native CsgA, making it a valuable tool for studying amyloidogenesis, biofilm-related infections, and host immune responses. Additionally, rCsgA serves as a model for understanding pathological amyloids (e.g., Aβ in Alzheimer’s disease) due to structural and mechanistic parallels.

In biotechnology, rCsgA’s biocompatibility and programmable assembly have spurred interest in biomaterial development, including nanowires, hydrogels, and drug delivery scaffolds. Its adhesive properties are exploited in bioengineering surfaces for cell immobilization or biosensing. Furthermore, rCsgA-based vaccines and diagnostics are explored due to its immunogenicity in chronic infections like urinary tract infections (UTIs) and inflammatory bowel disease (IBD).

Research on rCsgA also addresses antimicrobial strategies targeting biofilm resilience. Inhibiting CsgA polymerization could disrupt biofilms, enhancing antibiotic efficacy. Overall, CsgA recombinant protein bridges fundamental microbiology, biomedical innovation, and synthetic biology, highlighting its dual role as a virulence factor and a versatile biotechnological resource.

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