| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJC12 |
| Uniprot No | Q9UKB3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-198aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMDAILN YRSEDTEDYY TLLGCDELSS VEQILAEFKV RALECHPDKH PENPKAVETF QKLQKAKEIL TNEESRARYD HWRRSQMSMP FQQWEALNDS VKTSMHWVVR GKKDLMLEES DKTHTTKMEN EECNEQRERK KEELASTAEK TEQKEPKPLE KSVSPQNSDS SGFADVNGWH LRFRWSKDAP SELLRKFRNY EI |
| 预测分子量 | 26 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DNAJC12重组蛋白的虚构参考文献示例(仅供格式参考)：
1. **文献名称**: *DNAJC12重组蛋白在HSP70依赖性蛋白折叠中的功能研究*
**作者**: Zhang L, et al.
**摘要**: 本研究通过体外重组表达DNAJC12蛋白，证实其作为HSP70共伴侣分子，可特异性增强HSP70对错误折叠蛋白的再折叠能力，尤其在线粒体相关蛋白质量控制中起关键作用。
2. **文献名称**: *DNAJC12与神经退行性疾病中错误折叠蛋白的相互作用*
**作者**: Smith JR, et al.
**摘要**: 利用重组DNAJC12蛋白和细胞模型，发现其通过调控tau蛋白和α-突触核蛋白的聚集，延缓帕金森病和阿尔茨海默病相关病理进程。
3. **文献名称**: *DNAJC12重组蛋白的结构解析及其底物结合域鉴定*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学揭示了DNAJC12的J结构域三维构象，并证明其C端结构域与客户蛋白的结合能力依赖于保守的疏水残基。
4. **文献名称**: *DNAJC12基因敲除细胞系中重组蛋白的补偿效应研究*
**作者**: Wang H, et al.
**摘要**: 在DNAJC12缺陷型细胞中外源性添加重组DNAJC12蛋白，可恢复HSP70介导的线粒体自噬功能，改善细胞氧化应激损伤。
(注：以上文献为示例性内容，实际引用需以真实出版物为准。)
**Background of DNAJC12 Recombinant Protein**
DNAJC12 is a member of the DNAJ/Hsp40 family of molecular chaperones, which play critical roles in regulating protein folding, stability, and degradation by collaborating with Hsp70 chaperones. As a co-chaperone, DNAJC12 facilitates Hsp70’s ATPase activity, enabling its function in resolving misfolded proteins, maintaining proteostasis, and supporting cellular stress responses. The protein is encoded by the *DNAJC12* gene, located on human chromosome 10q21.3. and is ubiquitously expressed, with notable presence in the brain, liver, and kidneys.
Recombinant DNAJC12 is engineered through genetic cloning and expression in heterologous systems (e.g., *E. coli* or mammalian cells), allowing large-scale production of the purified protein for research and therapeutic applications. Its recombinant form retains the conserved J-domain, a hallmark of DNAJ proteins responsible for Hsp70 interaction, along with additional domains that mediate substrate recognition and cellular localization. Dysregulation of DNAJC12 has been linked to neurological disorders, including early-onset Parkinson’s disease and dopa-responsive dystonia, due to its role in stabilizing aromatic amino acid hydroxylases (e.g., tyrosine hydroxylase), enzymes critical for neurotransmitter synthesis.
Recent studies highlight DNAJC12’s involvement in cancer progression, where it modulates oncoprotein stability and stress adaptation in tumors. Additionally, it is implicated in metabolic disorders, such as phenylketonuria, through interactions with phenylalanine hydroxylase. Recombinant DNAJC12 serves as a vital tool for elucidating chaperone-mediated mechanisms in disease pathogenesis and exploring targeted therapies. Challenges remain in fully characterizing its structure-function relationships, tissue-specific roles, and post-translational modifications. Ongoing research aims to harness recombinant DNAJC12 for restoring proteostasis in neurodegenerative and metabolic diseases, positioning it as a promising candidate for biomedical innovation.
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