纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LDHB |
Uniprot No | P07195 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-334aa |
氨基酸序列 | ATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL |
预测分子量 | 43.4 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LDHB重组蛋白的参考文献示例(内容为虚构示例,仅供参考):
1. **文献名称**: "Expression and Purification of Recombinant Human LDHB in Escherichia coli"
**作者**: Zhang Y, et al.
**摘要**: 本研究成功构建了人源LDHB基因的重组质粒,并在大肠杆菌中实现高效可溶性表达。通过亲和层析和离子交换层析纯化获得高纯度蛋白,酶活实验证实其具有乳酸脱氢酶活性,为后续功能研究奠定基础。
2. **文献名称**: "Structural Characterization of LDHB Recombinant Protein and Its Role in Cancer Metabolism"
**作者**: Smith JL, et al.
**摘要**: 通过X射线晶体学解析了重组LDHB蛋白的三维结构,并发现其在肿瘤细胞糖酵解中的调控作用。实验表明,LDHB高表达与癌细胞乳酸生成及耐药性相关。
3. **文献名称**: "Development of a Kinetic Assay for LDHB Activity Using Recombinant Protein"
**作者**: Tanaka K, et al.
**摘要**: 利用重组LDHB蛋白建立了一种高灵敏度酶动力学检测方法,优化了反应条件并评估了抑制剂效果,为药物筛选提供了可靠工具。
4. **文献名称**: "Functional Analysis of LDHB Isoforms Expressed in Pichia pastoris"
**作者**: Müller R, et al.
**摘要**: 在毕赤酵母系统中表达两种LDHB剪接变体,比较其酶学特性差异,发现特定异构体在低氧条件下的活性显著升高,提示其在代谢适应中的作用。
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注:以上文献为示例性质,实际文献需通过PubMed/Google Scholar等平台检索确认。如需真实文献,建议使用关键词 **"LDHB recombinant protein"** 或 **"LDHB expression purification"** 进行精确搜索。
LDHB (Lactate Dehydrogenase B) is a subunit of the lactate dehydrogenase enzyme family, which plays a critical role in cellular energy metabolism. LDH is a tetrameric enzyme composed of combinations of two subunit types, LDHA and LDHB, encoded by distinct genes. LDHB predominates in tissues with high oxidative metabolism, such as the heart, brain, and kidneys, where it catalyzes the reversible conversion of lactate to pyruvate, linking glycolysis to the tricarboxylic acid (TCA) cycle. This reaction is essential for maintaining redox balance by regenerating NAD+ under aerobic conditions.
Recombinant LDHB protein is produced through genetic engineering, typically by expressing the human LDHB gene in bacterial (e.g., *E. coli*), mammalian, or insect cell systems. Its production enables detailed study of LDHB-specific functions, distinct from the hypoxia-associated LDHA isoform. Unlike LDHA, which favors pyruvate-to-lactate conversion (anaerobic glycolysis), LDHB exhibits higher affinity for lactate, promoting its oxidation back to pyruvate in oxygen-rich environments. This functional divergence highlights LDHB's role in metabolic flexibility and its potential implications in diseases like cancer, where altered LDH isoform expression correlates with tumor progression and drug resistance.
Recombinant LDHB is widely used in biochemical assays, drug discovery, and diagnostic research. It aids in exploring metabolic reprogramming in cancer, neurodegenerative disorders, and cardiovascular diseases. Additionally, it serves as a tool for developing isoform-specific inhibitors, aiming to target pathological glycolysis without disrupting normal oxidative metabolism. Its structural and functional characterization continues to advance our understanding of cellular energetics and disease mechanisms.
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