Recombinant Human IL32 protein

中文名： 白介素32(IL32)重组蛋白
别名： IL32；NK4；TAIF；Interleukin-32

货号: PA1000-8051

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>95%SDS-PAGE.
种属	Human
靶点	IL32
Uniprot No	P24001-4
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-131aa
氨基酸序列	MCFPKVLSDDMKKLKARMHQAIERFYDKMQNAESGRGQVMSSLAELEDDF KEGYLETVAAYYEEQHPELTPLLEKERDGLRCRGNRSPVPDVEDPATEEP GESFCDKSYGAPRGDKEELTPQKCSEPQSSK
预测分子量	15 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3篇涉及IL-32重组蛋白研究的参考文献摘要概括(注：建议通过学术数据库进一步验证文献准确性)：

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1. **《IL-32: A Novel Pro-Inflammatory Cytokine Induces Monocyte Chemotaxis》**

**作者**：Kim, S.H. et al. (2005)

**摘要**：首次报道IL-32的基因克隆及重组蛋白表达，发现其通过NF-κB通路诱导单核细胞趋化因子(如IL-8、TNF-α)，提示其在炎症反应中的作用。

2. **《IL-32 Is a Molecular Switch Controlling Inflammation and Apoptosis in Tuberculosis》**

**作者**：Netea, M.G. et al. (2006)

**摘要**：利用重组IL-32γ蛋白研究其抗结核机制，发现其通过caspase-3诱导巨噬细胞凋亡，从而抑制分枝杆菌感染。

3. **《IL-32γ Enhances Cytokine Production in Rheumatoid Arthritis through p38/MAPK Pathway》**

**作者**：Heinhuis, B. et al. (2011)

**摘要**：通过重组IL-32γ蛋白刺激滑膜细胞，证实其激活p38/MAPK通路并促进IL-6和IL-1β分泌，与类风湿性关节炎病理相关。

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(注：若需更多文献，建议检索PubMed或Web of Science，以“IL-32 recombinant protein”为关键词筛选近年研究。)

背景信息

**Background of IL-32 Recombinant Protein**

Interleukin-32 (IL-32) is a pro-inflammatory cytokine first identified in 2005. primarily expressed by immune cells (e.g., T cells, NK cells), epithelial cells, and monocytes. It plays a critical role in modulating immune responses, particularly in infections, autoimmune disorders, and cancer. Unlike traditional interleukins, IL-32 lacks a signal peptide and is secreted via non-classical pathways. It exists as multiple splice variants (IL-32α to IL-32θ), with IL-32γ being the most biologically active isoform due to its structural stability.

Recombinant IL-32 proteins are engineered to study its functions and therapeutic potential. Produced using expression systems like *E. coli* or mammalian cells, these proteins retain bioactivity for *in vitro* and *in vivo* studies. IL-32 activates key inflammatory pathways (e.g., NF-κB, MAPK) and induces cytokines like TNF-α and IL-6. Its dual role in diseases—promoting inflammation in conditions like rheumatoid arthritis or Crohn’s disease, yet exhibiting tumor-suppressive effects in certain cancers—highlights its complexity.

Research on recombinant IL-32 aids in developing targeted therapies, such as neutralizing antibodies or inhibitors, to mitigate pathological inflammation. However, challenges remain in understanding isoform-specific interactions and signaling mechanisms. Overall, IL-32 recombinant proteins serve as vital tools for unraveling its multifaceted roles in immunity and disease.