| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA1A |
| Uniprot No | P08107 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-641aa |
| 氨基酸序列 | AKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D |
| 预测分子量 | 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HSPA1A重组蛋白的3条参考文献示例(内容为虚构，仅供格式参考)：
1. **文献名称**: "Recombinant HSPA1A expression and purification for functional studies in vitro"
**作者**: Zhang et al.
**摘要**: 研究报道了利用大肠杆菌系统高效表达并纯化HSPA1A重组蛋白的方法，通过优化诱导条件和亲和层析技术获得高纯度蛋白，并验证其ATP酶活性及与客户蛋白的相互作用能力。
2. **文献名称**: "HSPA1A-mediated cytoprotection in neuronal cells: Role of recombinant protein delivery"
**作者**: Smith et al.
**摘要**: 通过体外递送重组HSPA1A蛋白至神经元细胞，证明其可显著减少氧化应激诱导的细胞凋亡，机制涉及抑制线粒体途径的Caspase-3活化，提示其在神经退行性疾病中的潜在治疗价值。
3. **文献名称**: "Structural analysis of recombinant human HSPA1A using cryo-EM reveals nucleotide-dependent conformational changes"
**作者**: Li et al.
**摘要**: 利用冷冻电镜技术解析了重组HSPA1A蛋白在结合ATP/ADP不同状态下的三维结构，揭示了其底物结合域与核苷酸结合域的构象动态变化，为靶向HSP70家族的药物设计提供结构基础。
4. **文献名称**: "Recombinant HSPA1A enhances antigen cross-presentation in dendritic cells for cancer immunotherapy"
**作者**: Garcia-Ruiz et al.
**摘要**: 研究证明重组HSPA1A蛋白可通过结合肿瘤抗原肽并激活树突状细胞，显著提高抗原呈递效率，在动物模型中诱导更强的抗肿瘤T细胞反应，为癌症疫苗开发提供新策略。
(注：以上文献信息为模拟生成，实际引用需查询真实数据库如PubMed。)
**Background of HSPA1A Recombinant Protein**
HSPA1A, a member of the heat shock protein 70 (HSP70) family, is a molecular chaperone crucial for cellular stress response and protein homeostasis. It is encoded by the *HSPA1A* gene, located on chromosome 6 in humans, and is rapidly upregulated under stress conditions such as heat shock, oxidative stress, or nutrient deprivation. HSPA1A assists in folding nascent polypeptides, refolding misfolded proteins, and targeting irreparable proteins for degradation, thereby maintaining cellular viability under adverse conditions.
Recombinant HSPA1A protein is produced using biotechnological methods, often through expression in bacterial (e.g., *E. coli*) or mammalian cell systems. The recombinant form retains the functional domains of the native protein: an N-terminal ATPase domain that binds and hydrolyzes ATP, a substrate-binding domain for interacting with client proteins, and a C-terminal domain that regulates substrate release. Tags such as His-tags or fluorescent markers may be added for purification or tracking purposes.
This recombinant protein is widely used in research to study stress response mechanisms, protein-protein interactions, and chaperone-mediated autophagy. It has applications in cancer research, neurodegenerative disease studies (e.g., Alzheimer’s, Parkinson’s), and exploring cellular responses to environmental toxins. Additionally, HSPA1A’s role in antigen presentation and immune modulation makes it relevant in immunology and vaccine development.
Quality control of recombinant HSPA1A involves verifying its molecular weight (approximately 70 kDa), confirming ATPase activity, and assessing substrate-binding efficiency. Its production and characterization provide a standardized tool for elucidating HSP70 family dynamics and developing therapeutic strategies targeting protein misfolding disorders.
×
