| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSA2 |
| Uniprot No | P10155 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3-535aa |
| 氨基酸序列 | ESVNQMQPLNEKQIANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDAAFYKTFKTVEPTGKRFLLAVDVSASMNQRVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVTTDMTLQQVLMAMSQIPAGGTDCSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTGALDVIRNFTL |
| 预测分子量 | 64.1kDa |
| 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. |
以下是模拟生成的3-4篇关于SSA2重组蛋白的参考文献示例(非真实文献，供格式参考)：
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1. **文献名称**: *"High-yield expression and purification of recombinant SSA2 in Escherichia coli for structural studies"*
**作者**: Smith, J. et al.
**摘要**: 本研究报道了通过优化密码子和诱导条件，在大肠杆菌系统中高效表达酵母SSA2重组蛋白，并利用镍柱亲和层析技术纯化获得高纯度蛋白，为后续结构解析奠定基础。
2. **文献名称**: *"SSA2 recombinant protein as a diagnostic antigen for autoimmune diseases: Sensitivity and specificity analysis"*
**作者**: Lee, H. & Kim, S.
**摘要**: 通过重组表达人源SSA2蛋白，评估其作为抗Ro/SSA自身抗体检测抗原的效能，证明其与患者血清反应的高特异性，为临床诊断提供新工具。
3. **文献名称**: *"Crystal structure of the SSA2 Hsp70 chaperone reveals ATP-dependent conformational changes"*
**作者**: Zhang, Y. et al.
**摘要**: 解析了重组SSA2蛋白的晶体结构，阐明其ATP结合域构象变化机制，揭示了Hsp70家族分子伴侣在蛋白质折叠中的动态调控机制。
4. **文献名称**: *"Functional characterization of recombinant SSA2 in yeast stress response pathways"*
**作者**: Garcia, R. et al.
**摘要**: 利用重组SSA2回补酵母突变体，证实其在热休克应激反应中的关键作用，并发现其与共伴侣蛋白协同调控未折叠蛋白应答的分子机制。
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**提示**：以上为模拟文献，实际文献需通过PubMed/Google Scholar等平台检索关键词(如"SSA2 recombinant"或"SSA2 protein expression")。建议结合具体研究场景筛选，如分子机制、诊断应用或结构生物学方向。
**Background of SSA2 Recombinant Protein**
The SSA2 recombinant protein is derived from the *SSA2* gene, which encodes a member of the heat shock protein 70 (Hsp70) family in *Saccharomyces cerevisiae* (budding yeast). Hsp70 proteins are evolutionarily conserved molecular chaperones critical for maintaining cellular proteostasis. They assist in protein folding, prevent aggregation under stress conditions, and facilitate the degradation of misfolded proteins. SSA2. along with its paralogs (SSA1. SSA3. and SSA4), plays a central role in cytosolic protein quality control.
SSA2 is constitutively expressed but upregulated during stress, such as heat shock or nutrient deprivation. Structurally, it comprises an N-terminal ATPase domain and a C-terminal substrate-binding domain, enabling ATP-dependent binding to exposed hydrophobic regions of client proteins. Its function is tightly regulated by co-chaperones like Hsp40 (Ydj1) and nucleotide-exchange factors (Fes1/Sse1), which modulate its ATPase cycle.
Recombinant SSA2 is produced using heterologous expression systems (e.g., *E. coli* or yeast) for biochemical and structural studies. Its recombinant form allows researchers to dissect chaperone mechanisms, substrate interactions, and roles in stress adaptation. Notably, SSA2 homologs in higher eukaryotes (e.g., HSPA8 in humans) share functional conservation, making SSA2 a valuable model for studying Hsp70 dysregulation in diseases like neurodegeneration or cancer.
Applications of recombinant SSA2 include in vitro protein refolding assays, drug screening for chaperone-targeted therapies, and elucidating stress response pathways. Challenges in production involve optimizing solubility and preserving native activity, often addressed through expression condition tuning or fusion tags. Ongoing research continues to explore its interplay with other chaperones and potential biotechnological uses in industrial enzyme production or synthetic biology.
In summary, SSA2 recombinant protein serves as a pivotal tool for understanding Hsp70 biology, stress responses, and developing therapeutic strategies against protein-misfolding disorders.
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