| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BAG2 |
| Uniprot No | O95816 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-211aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAQAKINAKANEGRFCRSSSMADRSSRLLE SLDQLELRVEALREAATAVEQEKEILLEMIHSIQNSQDMRQISDGEREEL NLTANRLMGRTLTVEVSVETIRNPQQQESLKHATRIIDEVVNKFLDDLGN AKSHLMSLYSACSSEVPHGPVDQKFQSIVIGCALEDQKKIKRRLETLLRN IENSDKAIKLLEHSKGAGSKTLQQNAESRFN |
| 预测分子量 | 26 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BAG2重组蛋白的模拟参考文献示例(仅供参考，实际文献需根据具体研究检索)：
---
1. **文献名称**：*BAG2 regulates protein quality control by mediating CHIP-dependent ubiquitination*
**作者**：Arndt V et al.
**摘要**：本研究揭示了BAG2重组蛋白作为分子伴侣的辅助因子，通过抑制CHIP(E3泛素连接酶)的活性，调控错误折叠蛋白的泛素化-蛋白酶体降解途径，从而维持细胞内蛋白质稳态。
2. **文献名称**：*Recombinant BAG2 attenuates tau aggregation in cellular models of neurodegeneration*
**作者**：Carrettiero DC et al.
**摘要**：通过表达和纯化BAG2重组蛋白，作者发现其能够与tau蛋白直接相互作用，抑制病理性tau聚集，并在阿尔茨海默病细胞模型中减少神经毒性。
3. **文献名称**：*Structural and functional analysis of BAG2 in HSP70 chaperone complex assembly*
**作者**：Xu Z et al.
**摘要**：利用重组BAG2蛋白进行结构解析，阐明了其BAG结构域与HSP70的ATP酶结构域结合机制，揭示了BAG2在调节HSP70介导的蛋白质折叠中的关键作用。
4. **文献名称**：*BAG2 modulates autophagy-lysosomal pathway in Parkinson's disease models*
**作者**：Li Y et al.
**摘要**：研究发现，外源性重组BAG2蛋白可通过增强α-synuclein的自噬性降解，减轻帕金森病模型中的神经元损伤，提示其作为治疗靶点的潜力。
---
**注意**：以上为模拟文献，实际引用时建议通过PubMed、Web of Science等数据库检索真实文献。若需具体文献支持，可提供研究方向(如疾病机制、结构研究等)进一步筛选。
**Background of BAG2 Recombinant Protein**
BAG2 (Bcl-2-associated athanogene 2) is a member of the BAG family of molecular chaperone regulators, which play critical roles in protein quality control, apoptosis, and stress response. As a co-chaperone, BAG2 interacts with heat shock protein 70 (Hsp70) to modulate its activity, influencing the folding, stabilization, or degradation of client proteins. Unlike other BAG family proteins (e.g., BAG1) that promote proteasomal degradation of misfolded proteins, BAG2 uniquely inhibits the ubiquitin-proteasome system, thereby stabilizing certain substrates under stress conditions.
Structurally, BAG2 contains a conserved BAG domain at its C-terminus for Hsp70 binding and a proline-rich N-terminal region involved in substrate recognition. Its function is particularly significant in neurodegenerative diseases, such as Alzheimer’s and Parkinson’s, where it regulates tau and α-synuclein aggregation by balancing chaperone-mediated refolding and degradation pathways. Dysregulation of BAG2 has been linked to impaired protein homeostasis, contributing to disease progression.
Recombinant BAG2 protein is engineered via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical interactions, structural properties, and therapeutic potential. Purified BAG2 is utilized in *in vitro* assays to dissect its role in Hsp70-mediated protein folding, screen for small-molecule modulators, or explore its neuroprotective mechanisms. Its recombinant form enables precise investigation of pathways critical for cellular stress adaptation, offering insights into targeted therapies for protein misfolding disorders.
In summary, BAG2 recombinant protein serves as a vital tool for understanding chaperone-mediated proteostasis and developing strategies to combat diseases associated with protein aggregation and neuronal degeneration.
×
