| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPA1L |
| Uniprot No | P34931 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-641aa |
| 氨基酸序列 | MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV 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HSPA1L重组蛋白的模拟参考文献示例(基于公开研究主题概括，非真实文献)：
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1. **文献名称**: *"Expression and purification of recombinant HSPA1L in Escherichia coli for structural analysis"*
**作者**: Smith J, et al.
**摘要**: 本研究报道了利用大肠杆菌表达系统高效表达HSPA1L重组蛋白，并通过亲和层析和离子交换层析纯化获得高纯度蛋白。作者进一步利用圆二色谱和X射线晶体学分析了其结构特征，揭示了HSPA1L的ATP结合域构象变化机制。
2. **文献名称**: *"HSPA1L recombinant protein protects neuronal cells against oxidative stress in vitro"*
**作者**: Chen L, et al.
**摘要**: 通过体外实验证明，重组HSPA1L蛋白能够抑制过氧化氢诱导的神经元细胞凋亡，并减少活性氧(ROS)积累。研究提示HSPA1L可能通过激活PI3K/Akt通路发挥神经保护作用，为神经退行性疾病治疗提供潜在靶点。
3. **文献名称**: *"Functional characterization of HSPA1L polymorphisms using recombinant protein variants"*
**作者**: Gupta R, et al.
**摘要**: 作者构建了不同单核苷酸多态性(SNP)位点的HSPA1L重组突变体，并比较其分子伴侣活性和热稳定性。结果显示rs2227956位点的变异显著影响HSPA1L与底物蛋白的结合能力，可能解释其与某些疾病易感性的关联。
4. **文献名称**: *"Recombinant HSPA1L enhances chemotherapy sensitivity in cancer cells by modulating autophagy"*
**作者**: Wang Y, et al.
**摘要**: 研究发现，外源性添加重组HSPA1L蛋白可增强顺铂对肝癌细胞的杀伤效果，机制可能与抑制过度自噬相关。该成果为HSPA1L作为化疗增敏剂的开发提供了实验依据。
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注：以上为模拟内容，实际引用时需查询真实文献数据库(如PubMed)。
HSPA1L, a member of the heat shock protein 70 (HSP70) family, is a stress-inducible molecular chaperone critical for cellular proteostasis. It shares high sequence homology with HSPA1A and HSPA1B (HSP70-1 isoforms) but differs in regulatory elements and expression patterns. Encoded by the *HSPA1L* gene on chromosome 6p21.3. this protein is constitutively expressed in certain tissues (e.g., testis) and induced under stress conditions like heat, oxidative stress, or inflammation. Its primary role involves assisting in protein folding, preventing aggregation, and facilitating degradation of misfolded proteins via interaction with co-chaperones.
Recombinant HSPA1L is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified protein for functional studies. The recombinant form retains ATPase activity and substrate-binding capacity, enabling research on its chaperone mechanisms. Structural studies reveal a conserved N-terminal ATPase domain and C-terminal substrate-binding domain connected by a flexible linker. Polymorphisms in *HSPA1L* (e.g., rs2227956) are linked to disease susceptibility, including HIV progression, cancer chemotherapy resistance, and transplant outcomes, making the recombinant protein valuable for investigating genotype-phenotype relationships.
In biomedical research, recombinant HSPA1L is used to study its cytoprotective effects in neurodegenerative diseases, inflammatory responses, and ischemia-reperfusion injury. It also serves as an immunomodulatory agent in vaccine development due to HSP70's role in antigen presentation. Challenges in production include maintaining post-translational modifications and avoiding endotoxin contamination. Ongoing studies focus on optimizing expression systems and exploring therapeutic applications in stress-related pathologies.
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