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Recombinant Human LITAF protein

  • 中文名: 脂多糖诱导的肿瘤坏死因子(LITAF)重组蛋白
  • 别    名: LITAF;PIG7;SIMPLE;Lipopolysaccharide-induced tumor necrosis factor-alpha factor
货号: PA1000-1828
Price: ¥询价
数量:
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产品详情

纯度>85%SDS-PAGE.
种属Human
靶点LITAF
Uniprot NoQ99732
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-161aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L
预测分子量19 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LITAF重组蛋白的3篇代表性文献及其摘要简述:

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1. **标题**: *Structural and Functional Analysis of LITAF in TNF-α Regulation*

**作者**: Li, X., et al.

**摘要**: 通过核磁共振解析LITAF重组蛋白的锌指结构域,揭示其结合DNA调控TNF-α表达的分子机制,为炎症疾病治疗提供新靶点。

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2. **标题**: *LITAF Mutations in Charcot-Marie-Tooth Disease*

**作者**: Street, V.A., et al.

**摘要**: 研究LITAF重组蛋白突变体(如W116G)对溶酶体功能的影响,证实其与腓骨肌萎缩症(CMT1C)的关联,揭示异常蛋白降解导致神经病变的机制。

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3. **标题**: *LITAF-Mediated Inflammatory Response in Macrophages*

**作者**: Myokai, F., et al.

**摘要**: 利用重组LITAF蛋白分析其在巨噬细胞中调控炎症因子的通路,发现LITAF通过TLR4/NF-κB信号放大LPS诱导的TNF-α释放,推动脓毒症研究进展。

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(注:以上文献为模拟示例,实际引用需根据具体研究内容调整。)

背景信息

LITAF (Lipopolysaccharide-Induced Tumor Necrosis Factor-α Factor), also known as PIG7 or SIMPLE, is a multifunctional protein encoded by the *LITAF* gene in humans. Initially identified as a transcriptional regulator of TNF-α in response to lipopolysaccharide (LPS) stimulation, LITAF plays roles in immune responses, intracellular trafficking, and lysosomal function. Structurally, it contains an N-terminal DNA-binding domain and a C-terminal proline-rich region, facilitating interactions with other proteins and membranes. Mutations in *LITAF* are linked to Charcot-Marie-Tooth disease type 1C (CMT1C), a hereditary peripheral neuropathy characterized by demyelination.

Recombinant LITAF proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells) to study its biological functions or develop therapeutic/diagnostic tools. These proteins often include affinity tags (e.g., His-tag) for purification and tracking. Research focuses on elucidating LITAF’s role in lysosomal regulation, inflammation modulation, and its pathological mechanisms in CMT1C. Recombinant LITAF also serves in structural studies to map mutation sites and screen potential drugs targeting CMT1C. Its dual involvement in immune signaling and cellular trafficking makes it a unique candidate for exploring cross-talk between inflammation and neurodegenerative processes. Current challenges include optimizing recombinant protein stability and functional fidelity for clinical applications.

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