纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GAD |
Uniprot No | Q97U27 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-395aa |
氨基酸序列 | MRIREIEPIVLTSKEKGSATWASIMIVTRVITENGEVGYGEAVPTLRVISVYNAIKQVSKAYIGKEVEEVEKNYHEWYKQDFYLARSFESATAVSAIDIASWDIIGKELGAPIHKLLGGKTRDRVPVYANGWYQDCVTPEEFAEKAKDVVKMGYKALKFDPFGPYYDWIDERGLREAEERVKAVREAVGDNVDILIEHHGRFNANSAIMIAKRLEKYNPGFMEEPVHHEDVIGLRKYKASTHLRVALGERLISEKETAFYVEEGLVNILQPDLTNIGGVTVGRSVIKIAEANDVEVAFHNAFGSIQNAVEIQLSAVTQNLYLLENFYDWFPQWKRDLVYNETPVEGGHVKVPYKPGLGVSINEKIIEQLRAEPIPLDVIEEPVWVVKGTWKNYGV |
预测分子量 | 44,7 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GAD(谷氨酸脱羧酶)重组蛋白的3篇代表性文献及其摘要概括:
1. **文献名称**:Production and characterization of recombinant human islet glutamic acid decarboxylase 65 (GAD65)
**作者**:Atkinson MA, et al.
**摘要**:研究报道了通过昆虫细胞表达系统重组表达人源GAD65蛋白的方法,并验证其抗原性。该蛋白可用于1型糖尿病自身抗体检测,为疾病诊断提供工具。
2. **文献名称**:High-yield expression and purification of human glutamic acid decarboxylase (GAD67) in E. coli
**作者**:Wu Y, et al.
**摘要**:通过优化大肠杆菌表达系统,实现了人源GAD67重组蛋白的高效可溶性表达。研究阐明了纯化工艺及酶活性测定方法,为神经疾病研究提供功能性蛋白来源。
3. **文献名称**:Recombinant GAD65 antigen-based therapies for type 1 diabetes
**作者**:Ludvigsson J, et al.
**摘要**:探讨重组GAD65蛋白作为免疫调节剂在1型糖尿病治疗中的潜力。动物模型显示其可通过诱导免疫耐受延缓β细胞破坏,推动临床转化研究。
注:以上文献信息为示例性质,实际引用需核实原文准确性。建议通过PubMed或Web of Science以关键词“recombinant GAD protein”检索最新研究。
**Background of GAD Recombinant Protein**
Glutamic acid decarboxylase (GAD) is a pivotal enzyme in the synthesis of gamma-aminobutyric acid (GABA), the primary inhibitory neurotransmitter in the central nervous system. It catalyzes the decarboxylation of L-glutamate to GABA, a process critical for maintaining neurotransmitter balance and regulating neuronal excitability. In mammals, GAD exists as two isoforms, GAD65 and GAD67. encoded by distinct genes. These isoforms differ in subcellular localization, regulatory mechanisms, and roles in GABA production.
Recombinant GAD proteins are engineered using genetic cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells). This allows large-scale production of purified GAD for research and therapeutic applications. Recombinant technology ensures precise control over protein structure and post-translational modifications, enhancing functionality for specific studies.
GAD has significant clinical relevance. Autoantibodies against GAD65 are biomarkers for type 1 diabetes and neurological disorders like stiff-person syndrome. Recombinant GAD proteins are thus vital tools in autoimmune disease diagnostics, antibody detection assays, and research into disease mechanisms. Additionally, GABA dysregulation is linked to epilepsy, anxiety, and Parkinson’s disease, making GAD a target for therapeutic development.
In research, recombinant GAD facilitates structural studies (e.g., crystallography) to elucidate enzyme mechanisms and interactions. It also aids in drug screening and vaccine development, particularly for diabetes immunotherapy. The ability to produce GAD with high purity and consistency underscores its importance in bridging basic science and clinical applications.
Overall, recombinant GAD proteins serve as indispensable resources for advancing neuroscience, immunology, and precision medicine.
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