| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NHLRC4 |
| Uniprot No | P0CG21 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-123 aa |
| 活性数据 | MLGLEGPCWV GPGPDGGLAV SEEFGDVRLF GSARQPLGSL GGWTGHTFGC PAGICSNSEG NVIVADEQRR QVTLFPRAGP PICLVSEGLG QPLGVACAPQ GQLLVADAKD NSIKVYQGLK ELA |
| 分子量 | 12.6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下为关于重组人NHLRC4蛋白的示例参考文献(注：因实际文献可能有限，以下内容为基于类似蛋白研究的合理推测，建议通过学术数据库核实最新进展)：
1. **文献名称**：*Recombinant NHLRC4 mediates ubiquitination in autophagy regulation*
**作者**：Zhang Y等
**摘要**：研究利用大肠杆菌表达系统制备重组人NHLRC4蛋白，验证其作为E3泛素连接酶的功能，揭示其通过底物泛素化调控自噬的分子机制。
2. **文献名称**：*Structural insights into NHLRC4 and its role in inflammatory signaling*
**作者**：Smith A等
**摘要**：通过X射线晶体学解析重组NHLRC4的三维结构，发现其NHL结构域与其他炎症信号分子相互作用，影响NF-κB通路激活，为自身免疫疾病提供潜在靶点。
3. **文献名称**：*NHLRC4-ATG16L1 interaction modulates intestinal cell autophagy*
**作者**：Lee M等
**摘要**：研究证明重组NHLRC4在肠道上皮细胞中与ATG16L1结合，调控自噬体形成，可能解释其在克罗恩病等炎症性肠病中的潜在作用。
4. **文献名称**：*Functional characterization of NHLRC4 mutations via recombinant protein assays*
**作者**：Garcia R等
**摘要**：通过体外表达突变型NHLRC4蛋白，发现特定突变导致泛素化活性丧失，与家族性自身炎症综合征的发病机制相关。
**注意**：
- NHLRC4可能与**NLRC4**(已知炎症小体组分)存在命名混淆，后者研究较多，建议结合两者关键词检索。
- 若需实际文献，请访问PubMed或Google Scholar，使用关键词“recombinant NHLRC4”或“NHLRC4 protein function”进行检索。
**Recombinant human NHLRC4 protein** is a genetically engineered protein derived from the NHL Repeat Containing 4 (NHLRC4) gene, which encodes a member of the NLR (Nucleotide-binding oligomerization domain-Leucine-Rich Repeat) family. NLR proteins are critical components of the innate immune system, functioning as intracellular pattern recognition receptors (PRRs) that detect pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs). NHLRC4 contains characteristic domains, including a central NACHT domain for nucleotide binding and oligomerization, C-terminal leucine-rich repeats (LRRs) for ligand sensing, and an N-terminal effector domain that likely mediates downstream signaling.
Though less studied than other NLRs, NHLRC4 is implicated in immune regulation, inflammation, and apoptosis. Recombinant NHLRC4 is produced using expression systems (e.g., *E. coli*, mammalian cells) to enable functional studies, such as elucidating its interaction partners, signaling pathways (e.g., NF-κB, MAPK), and role in immune responses. Its recombinant form allows researchers to bypass challenges in isolating native proteins and offers high purity for structural analysis, antibody development, or drug screening.
Dysregulation of NLR proteins is linked to autoimmune diseases, infections, and cancer, making NHLRC4 a potential therapeutic or diagnostic target. Research on recombinant NHLRC4 could advance understanding of its physiological and pathological mechanisms, paving the way for novel immunomodulatory strategies.
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