| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSA1 |
| Uniprot No | P19474 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-475aa |
| 氨基酸序列 | MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQSRKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKLEVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQRQLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDRRCHSSALELLQEVIIVLERSESWNLKDLDITSPELRSVCHVPGLKKMLRTCAVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCPLNIGSQGSTDY |
| 预测分子量 | 56.2 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SSA1重组蛋白的参考文献示例(内容为虚构，仅供格式参考)：
1. **文献名称**: "Expression and purification of recombinant SSA1 in Saccharomyces cerevisiae"
**作者**: Smith A, et al.
**摘要**: 研究报道了在酿酒酵母中高效表达并纯化重组SSA1蛋白的策略，通过优化启动子和纯化步骤，获得高纯度蛋白用于体外分子伴侣活性分析。
2. **文献名称**: "Structural insights into SSA1's role in protein folding by cryo-EM"
**作者**: Zhang L, et al.
**摘要**: 利用冷冻电镜技术解析了重组SSA1蛋白与底物结合的复合物结构，揭示了其ATP依赖的底物结合与释放机制。
3. **文献名称**: "Functional characterization of SSA1 mutants in stress response"
**作者**: Johnson R, et al.
**摘要**: 通过体外重组SSA1蛋白突变体实验，验证了其N端结构域在酵母热应激反应中的关键作用，并发现特定位点影响ATP酶活性。
4. **文献名称**: "SSA1 as a potential therapeutic target: In vitro aggregation inhibition assay"
**作者**: Chen H, et al.
**摘要**: 研究表明，重组SSA1蛋白可有效抑制淀粉样蛋白聚集，提示其在神经退行性疾病治疗中的应用潜力。
注：以上为模拟内容，实际文献需通过数据库(如PubMed)检索。
**Background of SSA1 Recombinant Protein**
SSA1. a member of the heat shock protein 70 (Hsp70) family, is a conserved molecular chaperone critical for protein homeostasis. Originally identified in *Saccharomyces cerevisiae* (yeast), SSA1 plays a central role in facilitating protein folding, preventing aggregation, and assisting in the translocation of nascent polypeptides across cellular membranes. It is constitutively expressed under normal conditions but upregulated during stress, such as heat shock, to mitigate proteotoxic damage. Structurally, SSA1 comprises an N-terminal ATPase domain and a C-terminal substrate-binding domain, enabling ATP-dependent cycles of substrate binding and release.
Recombinant SSA1 refers to the protein produced through genetic engineering in heterologous systems like *E. coli* or mammalian cell cultures. This approach allows large-scale production of pure, functional SSA1 for research and therapeutic applications. The recombinant protein retains its chaperone activity, making it invaluable for studying protein misfolding diseases (e.g., Alzheimer’s, Parkinson’s) and stress response mechanisms. Additionally, SSA1 homologs in humans (e.g., HSPA1A/B) are implicated in autoimmune disorders like lupus, where anti-SSA antibodies serve as diagnostic markers. Recombinant SSA1 is thus used in immunoassays to detect autoimmune responses.
In biotechnology, recombinant SSA1 aids in optimizing protein expression systems by enhancing solubility of aggregation-prone proteins. Its role in cancer biology is also explored, as Hsp70 proteins are often overexpressed in tumors, promoting cell survival. Engineering SSA1 variants with altered ATPase activity or substrate specificity further expands its utility in synthetic biology and drug discovery. Overall, recombinant SSA1 serves as a versatile tool for dissecting chaperone-mediated processes and developing targeted therapies.
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