| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJA1 |
| Uniprot No | P31689 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-394aa |
| 氨基酸序列 | MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQC |
| 预测分子量 | 52.0 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. |
1. **《DNAJA1 regulates mitochondrial metabolism and promotes cancer progression via autophagy inhibition》**
- 作者：Li X, Sun S, Chen D
- 摘要：研究揭示了DNAJA1重组蛋白通过抑制自噬途径调控线粒体代谢，促进肿瘤细胞增殖和转移的分子机制。
2. **《Recombinant DNAJA1 ameliorates α-synuclein aggregation in Parkinson's disease models》**
- 作者：Wang Y, Zhang H, Liu T
- 摘要：利用重组DNAJA1蛋白在帕金森病模型中验证其通过抑制α-突触核蛋白异常聚集发挥神经保护作用的潜力。
3. **《Structural and functional characterization of the Hsp40 co-chaperone DNAJA1》**
- 作者：Smith J, Brown K, Rajan R
- 摘要：通过重组蛋白技术解析DNAJA1的晶体结构，揭示其与Hsp70相互作用的分子基础及在蛋白质折叠中的功能。
4. **《DNAJA1 modulates heat shock response and cellular stress resilience via client protein recognition》**
- 作者：Gupta A, Lee JH, Park C
- 摘要：研究发现重组DNAJA1蛋白通过识别特定底物蛋白，调控细胞应激反应，增强细胞在高温和氧化压力下的存活能力。
DNAJA1. a member of the Hsp40 (DnaJ) family, is a highly conserved molecular chaperone that plays critical roles in protein homeostasis. It functions as a co-chaperone for Hsp70 ATPases, assisting in substrate recognition, folding, and translocation. Structurally, DNAJA1 contains a conserved J-domain responsible for Hsp70 interaction, a glycine/phenylalanine-rich (G/F) region, and a cysteine-rich C-terminal domain implicated in substrate binding.
This protein is ubiquitously expressed and localizes primarily to the cytoplasm, where it participates in stress response pathways. Under cellular stress, DNAJA1 stabilizes misfolded proteins, prevents aggregation, and facilitates their refolding or degradation via proteasomal/autophagic pathways. It also regulates key processes such as apoptosis, cell cycle progression, and signal transduction.
Recombinant DNAJA1 protein is commonly produced in bacterial (e.g., E. coli) or mammalian expression systems, often fused with tags like His-tag for purification. Its applications span biochemical studies of protein-protein interactions, in vitro chaperone assays, and disease modeling. Notably, DNAJA1 dysregulation has been linked to cancer (showing both tumor-promoting and suppressive roles depending on context), neurodegenerative disorders (e.g., Parkinson's and Alzheimer's diseases), and cardiovascular conditions.
Current research focuses on its potential as a therapeutic target, particularly in cancer where it modulates oncoprotein stability and chemotherapy resistance. However, its dual regulatory functions in different cellular contexts necessitate precise mechanistic studies. Recombinant DNAJA1 serves as an essential tool for deciphering these complex biological roles and developing targeted interventions.
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