Recombinant Human TLR8 protein

中文名： Toll样受体8(TLR8)重组蛋白
别名： TLR8；Toll-like receptor 8

货号: PA1000-7956

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	TLR8
Uniprot No	Q9NR97
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	27-827aa
氨基酸序列	EENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGNPGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKVCEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFPCVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSFNYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLSENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPDIACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNLKVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASLTELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSNLLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDVT
预测分子量	93.5kDa
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TLR8重组蛋白的参考文献示例(内容为模拟，非真实文献)：

1. **《Functional characterization of recombinant human TLR8 expressed in HEK293 cells》**

- 作者：Smith A, et al.

- 摘要：研究通过哺乳动物表达系统(HEK293细胞)成功表达并纯化重组人TLR8蛋白，证实其能够识别病毒单链RNA类似物(如R848)，并激活NF-κB信号通路，为TLR8的体外功能研究提供工具。

2. **《Crystal structure of TLR8 in complex with a synthetic agonist》**

- 作者：Zhang Y, et al.

- 摘要：利用重组TLR8胞外域蛋白解析其与合成小分子激动剂结合的晶体结构，揭示了TLR8的配体识别机制及构象变化，为靶向TLR8的免疫调节药物设计提供结构基础。

3. **《High-throughput screening of TLR8 agonists using a recombinant TLR8/luciferase reporter system》**

- 作者：Lee H, et al.

- 摘要：构建基于重组TLR8和荧光素酶报告基因的筛选平台，用于大规模筛选TLR8特异性激动剂，鉴定出多个新型免疫激活化合物，可用于疫苗佐剂开发。

4. **《Expression optimization and functional analysis of TLR8 in insect cells》**

- 作者：Chen X, et al.

- 摘要：通过杆状病毒-昆虫细胞系统优化重组TLR8的表达与纯化，验证其与病原体RNA的结合能力及下游炎症因子诱导活性，为TLR8的规模化制备提供方案。

(注：以上文献信息为示例性质，实际引用需查询真实数据库。)

背景信息

Toll-like receptor 8 (TLR8) is a member of the Toll-like receptor family, a critical component of the innate immune system that recognizes pathogen-associated molecular patterns (PAMPs). Located in endosomal compartments, TLR8 specifically detects single-stranded RNA (ssRNA) derived from viruses or bacteria, triggering downstream signaling cascades that activate NF-κB and interferon regulatory factors (IRFs). This leads to the production of pro-inflammatory cytokines and type I interferons, essential for antiviral and antibacterial responses. Unlike TLR7. which is functionally similar, TLR8 exhibits distinct ligand specificity and signaling nuances across species, with human TLR8 being more responsive to synthetic ligands like resiquimod (R848) compared to murine homologs.

Recombinant TLR8 proteins are engineered to study its structural and functional properties, often produced in mammalian (e.g., HEK293), insect (e.g., baculovirus systems), or prokaryotic expression systems. These proteins typically include extracellular leucine-rich repeat (LRR) domains for ligand binding, transmembrane regions, and cytoplasmic Toll/interleukin-1 receptor (TIR) domains for signaling. Purification methods like affinity chromatography (using His-tags or Fc-fusions) ensure high purity for experimental use.

Research applications include elucidating TLR8 activation mechanisms, screening immunomodulatory drugs, and developing adjuvants for vaccines. Structural studies using recombinant TLR8 have revealed ligand-binding specifics and dimerization processes critical for signaling. Challenges remain in maintaining proper post-translational modifications (e.g., glycosylation) during recombinant production, which can affect receptor functionality. Ongoing work focuses on optimizing expression systems and leveraging TLR8’s role in autoimmune and infectious diseases for therapeutic development.