| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LDHA |
| Uniprot No | P00338 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-332aa |
| 氨基酸序列 | ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF |
| 预测分子量 | 44.1 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LDHA(乳酸脱氢酶A)重组蛋白的3篇参考文献摘要示例(文献名称及内容为模拟示例，供参考)：
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1. **文献名称**：*Recombinant Human LDHA: Expression, Purification, and Enzymatic Characterization*
**作者**：Smith J, et al.
**摘要**：本研究通过大肠杆菌系统成功表达并纯化重组人源LDHA蛋白，验证其催化乳酸生成的酶活性和动力学参数，为后续靶向LDHA的抗癌药物筛选提供实验基础。
2. **文献名称**：*Structural Insights into LDHA Inhibition by Small Molecules Using Recombinant Protein Crystallography*
**作者**：Chen L, et al.
**摘要**：基于重组LDHA蛋白的晶体结构解析，揭示了小分子抑制剂与LDHA活性位点的结合模式，为优化靶向肿瘤代谢的高效抑制剂提供了结构生物学依据。
3. **文献名称**：*Role of Recombinant LDHA in Metabolic Reprogramming and Cancer Cell Proliferation*
**作者**：Wang Y, et al.
**摘要**：利用重组LDHA蛋白进行体外功能实验，证明其通过调控糖酵解通量促进肿瘤细胞增殖，并验证了LDHA基因沉默对癌细胞代谢的抑制作用。
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注：以上文献为示例性内容，实际引用时需查询真实文献(可参考NCBI PubMed或Web of Science数据库)。
**Background of LDHA Recombinant Protein**
Lactate dehydrogenase A (LDHA) is a critical enzyme in the glycolytic pathway, catalyzing the conversion of pyruvate to lactate with concomitant regeneration of NAD⁺, essential for sustaining glycolysis under hypoxic conditions. As a key isoform of the lactate dehydrogenase family, LDHA is predominantly expressed in metabolically active tissues and is frequently upregulated in cancers due to the Warburg effect, a phenomenon where cancer cells preferentially rely on glycolysis for energy production even in oxygen-rich environments. This metabolic reprogramming supports rapid proliferation, immune evasion, and metastasis, making LDHA a promising therapeutic target in oncology.
Recombinant LDHA protein is produced using genetic engineering techniques, where the LDHA gene is cloned into expression vectors and expressed in host systems like *E. coli* or mammalian cells. This allows large-scale production of purified, bioactive LDHA for functional and structural studies. Researchers utilize recombinant LDHA to investigate its enzymatic kinetics, regulatory mechanisms, and interactions with potential inhibitors. It also serves as a tool for drug discovery, enabling high-throughput screening of compounds aimed at disrupting cancer metabolism. Additionally, studies on recombinant LDHA contribute to understanding its role in non-cancer pathologies, including metabolic disorders and inflammatory diseases.
The development of LDHA-targeted therapies, such as small-molecule inhibitors or monoclonal antibodies, relies heavily on recombinant protein-based assays to validate efficacy and specificity. Beyond therapeutic applications, LDHA recombinant proteins are employed in diagnostic research, aiding in the identification of metabolic biomarkers. Overall, LDHA recombinant protein bridges biochemical research and translational medicine, offering insights into cellular metabolism and paving the way for novel treatments.
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