| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBAP2 |
| Uniprot No | Q5T6F2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1119aa |
| 氨基酸序列 | MMTSVSSDHCRGAREKPQISAAQSTQPQKQVVQATAEQMRLAQVIFDKNDSDFEAKVKQLMEVTGKNQDECIVALHDCNGDVNKAINILLEGNSDTTSWETVGCKKKNFAKENSENKENREKKSEKESSRGRGNNNRKGRGGNRGREFRGEENGIDCNQVDKPSDRGKRARGRGFGRGRGRGAGRFSTQGMGTFNPADYSDSTSTDVCGTKLVVWEAAQNGADEGTELASNTHNIAQDLSNKSSYGLKGAWKNSVEEWTTEDWTEDLSETKVFTASSAPAENHILPGQSIDLVALLQKPVPHSQASEANSFETSQQQGFGQALVFTNSQHNNQMAPGTGSSTAVNSCSPQSLSSVLGSGFGELAPPKMANITSSQILDQLKAPSLGQFTTTPSTQQNSTSHPTTTTSWDLKPPTSQSSVLSHLDFKSQPEPSPVLSQLSQRQQHQSQAVTVPPPGLESFPSQAKLRESTPGDSPSTVNKLLQLPSTTIENISVSVHQPQPKHIKLAKRRIPPASKIPASAVEMPGSADVTGLNVQFGALEFGSEPSLSEFGSAPSSENSNQIPISLYSKSLSEPLNTSLSMTSAVQNSTYTTSVITSCSLTSSSLNSASPVAMSSSYDQSSVHNRIPYQSPVSSSESAPGTIMNGHGGGRSQQTLDTPKTTGPPSALPSVSSLPSTTSCTALLPSTSQHTGDLTSSPLSQLSSSLSSHQSSLSAHAALSSSTSHTHASVESASSHQSSATFSTAATSVSSSASSGASLSSSMNTANSLCLGGTPASASSSSSRAAPLVTSGKAPPNLPQGVPPLLHNQYLVGPGGLLPAYPIYGYDELQMLQSRLPVDYYGIPFAAPTALASRDGSLANNPYPGDVTKFGRGDSASPAPATTPAQPQQSQSQTHHTAQQPFVNPALPPGYSYTGLPYYTGMPSAFQYGPTMFVPPASAKQHGVNLSTPTPPFQQASGYGQHGYSTGYDDLTQGTAAGDYSKGGYAGSSQAPNKSAGSGPGKGVSVSSSTTGLPDMTGSVYNKTQTFDKQGFHAGTPPPFSLPSVLGSTGPLASGAAPGYAPPPFLHILPAHQQPHSQLLHHHLPQDAQSGSGQRSQPSSLQPKSQASKPAYGNSPYWTN |
| 预测分子量 | 117,1 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. |
以下是关于UBAP2重组蛋白的3篇参考文献示例(注：文献信息为模拟示例，实际文献需通过学术数据库检索获取)：
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1. **文献名称**：*UBAP2 is a component of the ESCRT-I complex essential for HIV-1 viral budding*
**作者**：Smith A, et al.
**摘要**：该研究通过重组UBAP2蛋白的体外表达，揭示了其在ESCRT-I复合体中的关键作用，证明UBAP2通过与泛素化信号结合促进HIV-1病毒颗粒的出芽过程。
2. **文献名称**：*Structural insights into the ubiquitin recognition mechanism of UBAP2*
**作者**：Zhang L, Wang Y, et al.
**摘要**：利用重组UBAP2蛋白的晶体结构解析，阐明了其UBASS结构域与泛素分子的特异性结合模式，为泛素依赖性分选途径提供了分子机制依据。
3. **文献名称**：*UBAP2 regulates autophagy via modulating mTORC1 signaling in cancer cells*
**作者**：Tanaka K, et al.
**摘要**：研究通过重组UBAP2蛋白的功能实验，发现其通过抑制mTORC1通路增强自噬活性，提示UBAP2在肿瘤细胞代谢调控中的潜在治疗靶点价值。
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**注**：以上文献信息为示例性质，实际研究中建议通过PubMed、Web of Science等平台检索最新文献。若需具体文献协助，可提供更详细的研究方向或关键词。
UBAP2 (Ubiquitin-associated protein 2) is a conserved eukaryotic protein implicated in ubiquitin-dependent cellular processes. It belongs to the UBAP protein family, characterized by ubiquitin-binding domains that enable interactions with ubiquitinated substrates. UBAP2 is involved in endosomal sorting, stress granule assembly, and cell cycle regulation. Studies suggest it acts as a molecular chaperone or adaptor, facilitating the recognition and trafficking of ubiquitin-tagged proteins through pathways like the Endosomal Sorting Complex Required for Transport (ESCRT) system. Its role in maintaining proteostasis and regulating protein degradation underscores its importance in cellular stress responses.
Recombinant UBAP2 protein is engineered for in vitro studies to dissect its molecular mechanisms. Produced using expression systems like *E. coli* or mammalian cell lines, the recombinant protein retains functional domains, including the ubiquitin-binding UBA domain and prion-like low-complexity regions. Purification often involves affinity chromatography (e.g., His-tag) to ensure high purity and activity. Researchers utilize UBAP2 recombinant proteins to investigate its interactions with ubiquitin chains, RNA molecules, or ESCRT components, as well as its phase separation behavior in stress granule formation.
Dysregulation of UBAP2 is linked to diseases such as cancer and neurodegenerative disorders. Overexpression has been observed in certain tumors, correlating with poor prognosis, while its aggregation may contribute to pathologies like amyotrophic lateral sclerosis (ALS). Additionally, UBAP2's role in viral budding (e.g., HIV-1) highlights its therapeutic potential. Current research focuses on mapping its structural motifs, post-translational modifications, and context-specific binding partners to develop targeted interventions. The recombinant protein serves as a critical tool for these explorations.
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