| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA4 |
| Uniprot No | P34932 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-840aa |
| 氨基酸序列 | MSVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACISFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVEAEKSNLAYDIVQLPTGLTGIKVTYMEEERNFTTEQVTAMLLSKLKETAESVLKKPVVDCVVSVPCFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSAYQVSVCAFNRGKLKVLATAFDTTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKIRALLRLSQECEKLKKLMSANASDLPLSIECFMNDVDVSGTMNRGKFLEMCNDLLARVEPPLRSVLEQTKLKKEDIYAVEIVGGATRIPAVKEKISKFFGKELSTTLNADEAVTRGCALQCAILSPAFKVREFSITDVVPYPISLRWNSPAEEGSSDCEVFSKNHAAPFSKVLTFYRKEPFTLEAYYSSPQDLPYPDPAIAQFSVQKVTPQSDGSSSKVKVKVRVNVHGIFSVSSASLVEVHKSEENEEPMETDQNAKEEEKMQVDQEEPHVEEQQQQTPAENKAESEEMETSQAGSKDKKMDQPPQAKKAKVKTSTVDLPIENQLLWQIDREMLNLYIENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSGEYEKFVSEDDRNSFTLKLEDTENWLYEDGEDQPKQVYVDKLAELKNLGQPIKIRFQESEERPKLFEELGKQIQQYMKIISSFKNKEDQYDHLDAADMTKVEKSTNEAMEWMNNKLNLQNKQSLTMDPVVKSKEIEAKIKELTSTCSPIISKPKPKVEPPKEEQKNAEQNGPVDGQGDNPGPQAAEQGTDTAVPSDSDKKLPEMDID |
| 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3篇关于HSPA4重组蛋白的参考文献摘要概括：
1. **文献名称**: "HSPA4 regulates cancer cell metastasis through epithelial-mesenchymal transition"
**作者**: Zhang Y, et al.
**摘要**: 研究利用重组HSPA4蛋白发现其通过激活TGF-β信号通路促进肿瘤细胞上皮-间质转化(EMT)，增强癌细胞侵袭和转移能力。
2. **文献名称**: "Recombinant HSPA4 mitigates tau aggregation in Alzheimer's disease models"
**作者**: Chen L, et al.
**摘要**: 通过体外表达纯化HSPA4重组蛋白，证明其与tau蛋白相互作用并抑制病理性聚集，为神经退行性疾病治疗提供潜在靶点。
3. **文献名称**: "Structural and functional analysis of the HSPA4-HSP70 chaperone complex"
**作者**: Wang X, et al.
**摘要**: 采用重组HSPA4和HSP70蛋白解析两者复合物的晶体结构，揭示其协同作用机制，为热休克蛋白家族的功能研究提供分子基础。
注：以上文献为示例，实际引用需核对真实发表的论文信息。
HSPA4 (Heat Shock Protein Family A Member 4), also known as HSP70RY or APG-2. is a member of the heat shock protein 110 (HSP110) subfamily within the HSP70 superfamily. It functions primarily as a molecular chaperone, assisting in protein folding, preventing aggregation of misfolded proteins, and facilitating cellular stress responses. Structurally, HSPA4 contains an N-terminal ATPase domain and a C-terminal substrate-binding domain, enabling ATP-dependent interactions with client proteins. Unlike canonical HSP70s, HSPA4 exhibits nucleotide exchange factor activity, regulating the chaperone cycle of other HSP70 proteins.
This protein is ubiquitously expressed and plays critical roles in maintaining proteostasis under physiological and stress conditions, such as heat shock, oxidative stress, or nutrient deprivation. It participates in diverse cellular processes, including apoptosis regulation, autophagy, and signal transduction. Dysregulation of HSPA4 has been implicated in pathological conditions. Elevated HSPA4 levels are observed in various cancers, where it promotes tumor cell survival, metastasis, and chemotherapy resistance by stabilizing oncogenic proteins and inhibiting pro-apoptotic pathways. Conversely, reduced HSPA4 activity is linked to neurodegenerative diseases associated with protein aggregation, such as Alzheimer's and Parkinson's diseases.
Recombinant HSPA4 proteins are typically produced in prokaryotic (e.g., E. coli) or eukaryotic expression systems. Production challenges include maintaining proper folding and post-translational modifications, often requiring optimized purification and refolding protocols. These recombinant tools enable mechanistic studies of HSPA4-client interactions, high-throughput drug screening for cancer therapeutics, and development of diagnostic biomarkers. Recent research explores HSPA4 inhibitors as potential anticancer agents and investigates its role as an immunogenic antigen in vaccine development. However, functional studies must account for HSPA4's complex interactions with co-chaperones and its context-dependent roles in cellular stress adaptation.
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