| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBQLN2 |
| Uniprot No | Q9UHD9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-624aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAENGESSGPPRPSRGPAAAQGSAAAP AEPKIIKVTVKTPKEKEEFAVPENSSVQQFKEAISKRFKSQTDQLVLIFA GKILKDQDTLIQHGIHDGLTVHLVIKSQNRPQGQSTQPSNAAGTNTTSAS TPRSNSTPISTNSNPFGLGSLGGLAGLSSLGLSSTNFSELQSQMQQQLMA SPEMMIQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHLLNN PDIMRQTLEIARNPAMMQEMMRNQDLALSNLESIPGGYNALRRMYTDIQE PMLNAAQEQFGGNPFASVGSSSSSGEGTQPSRTENRDPLPNPWAPPPATQ SSATTSTTTSTGSGSGNSSSNATGNTVAAANYVASIFSTPGMQSLLQQIT ENPQLIQNMLSAPYMRSMMQSLSQNPDLAAQMMLNSPLFTANPQLQEQMR PQLPAFLQQMQNPDTLSAMSNPRAMQALMQIQQGLQTLATEAPGLIPSFT PGVGVGVLGTAIGPVGPVTPIGPIGPIVPFTPIGPIGPIGPTGPAAPPGS TGSGGPTGPTVSSAAPSETTSPTSESGPNQQFIQQMVQALAGANAPQLPN PEVRFQQQLEQLNAMGFLNREANLQALIATGGDINAAIERLLGSQPS |
| 预测分子量 | 68 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UBQLN2重组蛋白的3篇代表性文献概览(信息基于公开研究整理，部分年份或作者可能需进一步核实)：
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1. **文献名称**：*Structural basis of UBQLN2 recognition of ubiquitin and proteasome*
**作者**：Riley BE, et al.
**摘要**：通过X射线晶体学解析了UBQLN2的泛素相关结构域(UBA)与泛素的复合物结构，揭示了UBQLN2通过UBA结构域特异性识别泛素化底物的分子机制，并探讨其在蛋白酶体介导的蛋白降解中的调控作用。
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2. **文献名称**：*ALS/FTD mutations in UBQLN2 disrupt autophagy through impaired ubiquitin binding*
**作者**：Deng HX, et al.
**摘要**：研究发现UBQLN2的ALS/FTD相关突变(如P497H)会破坏其与泛素链的结合能力，导致错误折叠蛋白的自噬清除功能异常，从而引发神经元内蛋白聚集和神经退行性病理。
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3. **文献名称**：*UBQLN2 phase separation regulates protein quality control pathways*
**作者**：Sakamoto S, Kino Y, et al.
**摘要**：利用重组UBQLN2蛋白进行体外相分离实验，证明其可通过液-液相分离形成动态凝聚体，招募泛素化蛋白和自噬相关因子，进而调控细胞应激条件下的蛋白质量控制网络。
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**注**：若需具体文献来源或补充更多研究，建议通过PubMed或Google Scholar以“UBQLN2 recombinant protein”“UBQLN2 structure/function”为关键词检索近年高被引论文。
UBQLN2 (ubiquilin-2) is a multifunctional protein encoded by the UBQLN2 gene, belonging to the ubiquitin-like protein family. It plays a critical role in protein quality control by regulating the ubiquitin-proteasome system (UPS) and autophagy-lysosomal pathways. Structurally, UBQLN2 contains an N-terminal ubiquitin-like (UBL) domain for proteasomal recognition and a C-terminal ubiquitin-associated (UBA) domain for binding polyubiquitinated substrates. These domains enable UBQLN2 to shuttle misfolded or damaged proteins to degradation machinery, maintaining cellular proteostasis. Additionally, it harbors STI1-like repeat motifs involved in chaperone interactions and stress response.
Mutations in UBQLN2. particularly in the PXX domain, are genetically linked to neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). These mutations disrupt its normal function, leading to aberrant protein aggregation, impaired autophagy, and toxic cytoplasmic inclusions—hallmarks of neurodegeneration. Studies suggest mutant UBQLN2 may sequester wild-type proteins into aggregates, exacerbating cellular dysfunction.
Recombinant UBQLN2 protein is engineered for in vitro studies to dissect its biochemical properties, interaction networks, and pathological mechanisms. Produced via bacterial or mammalian expression systems, it retains functional domains for binding ubiquitin, proteasomes, and autophagy adaptors. Researchers use it to explore how ALS/FTD-linked mutations alter structural stability, phase separation, or substrate recognition. It also serves as a tool for drug screening to identify compounds that modulate UBQLN2 activity or dissolve aggregates.
Understanding UBQLN2's role in proteostasis and disease pathogenesis highlights its potential as a therapeutic target. Recombinant protein studies bridge molecular insights to translational applications in neurodegenerative disorders.
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