| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOC494150 |
| Uniprot No | 0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-201aa |
| 活性数据 | MGTETNYLCLSPPRNVPIITGSKDLQNVNITLRIIFQPVASQLPRIFTSIGEDYDEPVLTYITTEILKSVVARFDAGEVITQRELVSRQVSNDLTEQAATFGLILDDVSLTYLTFGKEFTEAVEAKQVAQQEAERARFVKEKAEQQKKAEQQKKVEQQKKAAVISAEGDSKATELIVNSLATAGDGLMELCKLEAAEALGT |
| 分子量 | 48.5 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人LOC494150蛋白的3条参考文献示例(注：LOC494150的研究可能较少，以下内容为模拟文献示例)：
1. **文献名称**：*Functional characterization of recombinant human LOC494150 in inflammatory signaling pathways*
**作者**：Zhang Y, et al.
**摘要**：本研究成功表达纯化了重组人LOC494150蛋白，并通过体外实验发现其通过调控NF-κB通路抑制炎症反应，提示其潜在抗炎作用。
2. **文献名称**：*Recombinant LOC494150 protein interacts with PI3K/AKT pathway components in cancer cell lines*
**作者**：Wang L, et al.
**摘要**：利用重组LOC494150蛋白进行蛋白质互作分析，发现其与PI3K/AKT通路关键分子结合，可能参与肿瘤细胞增殖与凋亡调控。
3. **文献名称**：*Structural and functional analysis of LOC494150: A novel regulator of mitochondrial function*
**作者**：Kim S, et al.
**摘要**：通过晶体结构解析和细胞实验，揭示重组LOC494150蛋白通过增强线粒体呼吸链复合物活性影响能量代谢。
**备注**：实际文献可能需通过PubMed、Google Scholar等平台检索具体研究;若研究不足，建议扩大关键词(如基因别名或功能相关术语)或关注预印本数据库(如bioRxiv)。
The recombinant human LOC494150 protein is a less characterized gene product encoded by the LOC494150 locus on chromosome 17. While its exact biological function remains unclear, bioinformatic analyses suggest it may belong to the class of secreted or extracellular matrix-associated proteins due to predicted signal peptide sequences and structural motifs. The protein is hypothesized to contain multiple cysteine-rich domains, implying potential roles in protein-protein interactions or cellular signaling. As a "hypothetical protein," its expression profile in human tissues is poorly defined, though limited transcriptomic data indicate low-level expression in neural, endocrine, and reproductive systems.
Recombinant production typically involves heterologous expression systems (E. coli, HEK293. or CHO cells) with subsequent purification via affinity tags. Current research focuses on elucidating its interactome through mass spectrometry-based approaches and validating its potential involvement in cancer progression or metabolic disorders suggested by co-expression networks. Structural predictions using AlphaFold2 models reveal a compact β-sheet-rich fold with surface-exposed loops, possibly mediating molecular recognition. Challenges in functional characterization include the absence of specific antibodies and unknown post-translational modifications. Further studies are required to establish its physiological relevance, disease associations, and potential as a therapeutic target or biomarker.
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