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Recombinant Human NHLRC2 Protein

  • 中文名: 重组人(NHLRC2)蛋白
  • 别    名: 1200003G01Rik; DKFZp779F115; FLJ20147; FLJ25621; FLJ33312; MGC45492; NHL repeat containing 2; NHL repeat-containing protein 2; NHLC2_HUMAN; NHLRC2; Novel NHL repeat domain containing protein; OTTHUMP00000020518
货号: PA2000-9701
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点NHLRC2
Uniprot NoQ8NBF2
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-726 aa
活性数据MAAPGGRGRS LSGLLPAQTS LEYALLDAVT QQEKDSLVYQ YLQKVDGWEQ DLSVPEFPEG LEWLNTEEPI SVYKDLCGKI VVLDFFTYCC INCIHLLPDL HALEHTYSDK DGLLIIGVHS AKFPNEKVLD NIKSAVLRYN ITHPMVNDAD ASLWQELEVS CWPTLVILGP RGNMLFSLIG EGHKDKLFLY TSIALKYYKD RGQIRDNKIG IKLYKDSLPP SPLLFPGKVT VDQVTDRLVI ADTGHHRILV VWKNGQIQYS IGGPNPGRKD GIFSESTFNS PQGVAIMNNI IYVADTENHL IRKIDLEAEK VSTVAGIGIQ GTDKEGGAKG EQQPISSPWD VVFGTSGSEV QRGDILWIAM AGTHQIWALL LDSGKLPKKN ELTKGTCLRF AGSGNEENRN NAYPHKAGFA QPSGLSLASE DPWSCLFVAD SESSTVRTVS LKDGAVKHLV GGERDPMNLF AFGDVDGVGI NAKLQHPLGV TWDKKRNLLY VADSYNHKIK VVDPKTKNCT TLAGTGDTNN VTSSSFTEST FNEPGGLCIG ENGELLYVAD TNNHQIKVMD LETKMVSVLP IFRSENAVVD GPFLVEKQKT LPKLPKSAPS IRLSPVTACA GQTLQFKLRL DLPSGSKLTE GVSSCWFLTA EGNEWLLQGQ IAAGDIENIS SQPTISLQIP DDCLSLEAIV SVSVFLYYCS ADSSACMMKA ILFSQPLQIT DTQQGCIAPV ELRYVF
分子量79.4 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.

参考文献

以下是关于重组人NHLRC2蛋白的假设性参考文献示例(内容基于领域内常见研究方向推测,建议通过学术数据库验证具体文献):

1. **标题**:*Structural and Functional Characterization of Recombinant Human NHLRC2 Protein*

**作者**:Li, X., et al.

**摘要**:研究利用大肠杆菌表达系统成功表达并纯化了重组人NHLRC2蛋白,通过晶体学解析其NHL结构域的三维结构,并发现其可能参与泛素化调控通路。

2. **标题**:*NHLRC2 Regulates Autophagy via Interaction with mTOR Signaling Pathway*

**作者**:Yamamoto, K., et al.

**摘要**:该文献报道了重组NHLRC2蛋白在哺乳动物细胞中的过表达实验,证明其通过与mTOR复合物相互作用抑制自噬,为肿瘤微环境研究提供新靶点。

3. **标题**:*Proteomic Analysis of NHLRC2-Associated Complexes in Human Cells*

**作者**:Chen, J., et al.

**摘要**:利用亲和纯化-质谱技术鉴定重组NHLRC2在HEK293细胞中的相互作用蛋白,发现其与E3泛素连接酶复合物成员存在关联,提示其在蛋白质降解中的潜在功能。

4. **标题**:*NHLRC2 Deficiency Leads to Mitochondrial Dysfunction in Cellular Models*

**作者**:Garcia-Ruiz, S., et al.

**摘要**:通过CRISPR敲低NHLRC2并结合重组蛋白回补实验,证明NHLRC2对维持线粒体膜电位和能量代谢具有重要作用。

**注意**:以上为基于领域知识的模拟文献,实际研究中请通过**PubMed**、**Google Scholar**等平台以“NHLRC2 recombinant”、“NHLRC2 function”等关键词检索最新论文。


背景信息

NHLRC2 (NHL repeat-containing protein 2) is a poorly characterized human protein belonging to the NHL (NCL-1. HT2A, and LIN-41) repeat family, a group of evolutionarily conserved proteins often involved in ubiquitination, RNA binding, or protein-protein interactions. Structurally, it contains multiple NHL repeats—β-propeller-like domains known to mediate substrate recognition in E3 ubiquitin ligases. NHLRC2 is ubiquitously expressed across tissues, with higher levels observed in the brain, testis, and certain cancer cells.

Although its precise biological functions remain unclear, emerging studies link NHLRC2 to critical cellular processes. It interacts with components of the ubiquitin-proteasome system, suggesting roles in protein degradation or quality control. Recent work implicates NHLRC2 in regulating cell cycle progression and maintaining genome stability, potentially through modulating DNA repair pathways. Additionally, it has been associated with autophagy and lysosomal function, possibly via interactions with mTOR signaling components.

Dysregulation of NHLRC2 has been tentatively connected to human diseases. Genetic variants are linked to neurodevelopmental disorders and cancer progression. In glioblastoma, NHLRC2 overexpression correlates with poor prognosis, while its downregulation in breast cancer models reduces cell invasion. Recombinant NHLRC2 protein is used in vitro to study its enzymatic activity, interactome, and structural properties, aiding mechanistic insights. Further research is needed to define its molecular targets and pathophysiological roles across contexts.


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