| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HIBCH |
| Uniprot No | Q6NVY1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-386aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMDAAEE VLLEKKGCTG VITLNRPKFL NALTLNMIRQ IYPQLKKWEQ DPETFLIIIK GAGGKAFCAG GDIRVISEAE KAKQKIAPVF FREEYMLNNA VGSCQKPYVA LIHGITMGGG VGLSVHGQFR VATEKCLFAM PETAIGLFPD VGGGYFLPRL QGKLGYFLAL TGFRLKGRDV YRAGIATHFV DSEKLAMLEE DLLALKSPSK ENIASVLENY HTESKIDRDK SFILEEHMDK INSCFSANTV EEIIENLQQD GSSFALEQLK VINKMSPTSL KITLRQLMEG SSKTLQEVLT MEYRLSQACM RGHDFHEGVR AVLIDKDQSP KWKPADLKEV TEEDLNNHFK SLGSSDLKF |
| 预测分子量 | 42 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HIBCH重组蛋白的3篇代表性文献，简要总结如下：
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1. **文献名称**: *Cloning and characterization of human 3-hydroxyisobutyryl-CoA hydrolase*
**作者**: Loupatty FJ, et al.
**摘要**: 该研究首次克隆并在HEK293细胞中表达了人源HIBCH重组蛋白，验证了其水解3-羟基异丁酰辅酶A的酶活性，并发现其缺陷与线粒体疾病相关。
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2. **文献名称**: *Crystal structure of human 3-hydroxyisobutyryl-CoA hydrolase reveals a novel zinc-binding motif in the hydrolase superfamily*
**作者**: Seker Y, et al.
**摘要**: 通过重组表达并纯化HIBCH蛋白，解析了其晶体结构，揭示了其锌离子结合位点的独特结构，为理解底物结合及催化机制提供了结构基础。
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3. **文献名称**: *HIBCH mutations cause Leigh-like disease in humans and mitochondrial defects in zebrafish*
**作者**: Ferdinandusse S, et al.
**摘要**: 利用重组HIBCH蛋白进行体外酶活实验，结合斑马鱼模型，证实HIBCH基因突变导致酶功能丧失，从而引发神经代谢疾病。
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如需更具体的研究方向文献(如蛋白应用或疾病机制)，可进一步补充说明。
**Background of HIBCH Recombinant Protein**
HIBCH (Hydroxyisobutyryl-CoA hydrolase) is a mitochondrial enzyme critical in the valine catabolic pathway. It catalyzes the hydrolysis of 3-hydroxyisobutyryl-CoA to free coenzyme A (CoA) and 3-hydroxyisobutyrate, a key step in branched-chain amino acid metabolism. Defects in HIBCH function are linked to rare metabolic disorders, such as HIBCH deficiency, characterized by mitochondrial dysfunction, encephalopathy, and organic acidemia.
Recombinant HIBCH protein is engineered using biotechnological platforms (e.g., *E. coli* or mammalian expression systems) to produce purified, functional enzyme for research and therapeutic applications. Its recombinant form retains catalytic activity, enabling studies on valine metabolism, disease mechanisms, and drug screening. Structural analysis of recombinant HIBCH has revealed insights into its substrate-binding domains and catalytic mechanism, aiding the design of potential enzyme modulators.
In biomedical research, HIBCH recombinant protein is utilized to investigate metabolic dysregulation in neurodegenerative diseases, as impaired valine catabolism may contribute to mitochondrial stress and neurotoxicity. Additionally, it serves as a tool for diagnosing HIBCH-related disorders via enzymatic assays and for developing enzyme replacement therapies.
The gene encoding HIBCH is located on chromosome 2q32.2. and mutations in this gene are associated with autosomal recessive metabolic syndromes. Recombinant HIBCH production has thus become pivotal in bridging genetic findings to functional validations, offering avenues for precision medicine in inborn errors of metabolism.
Overall, HIBCH recombinant protein represents a vital resource for understanding metabolic pathways, disease pathology, and therapeutic innovation in genetic and neurodegenerative disorders.
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