| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LATH |
| Uniprot No | Q86YQ2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-179aa |
| 氨基酸序列 | QEVLAGVSSQ LLNDLTQGLL RADFLPSLQT TGLQKPLSSA FDGVSGLLDI FGPPLTNEIN TVSIQVKNPQ LLHVSIESTP QRKEATVQVP FTSELIVQLL TMKPFTANMQ SDIKVQIRLE KNVGGRYELA FGNCRLLPEA IWIQTGVQLA PAQNLLWQT |
| 预测分子量 | 19,4 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LATH(赖氨酰氧化酶样蛋白)重组蛋白的参考文献示例(内容为虚构，仅供格式参考)：
1. **《重组LATH蛋白在大肠杆菌中的高效表达及纯化》**
- 作者：Zhang Y, Li H, et al.
- 摘要：本研究通过优化密码子和大肠杆菌表达系统，成功实现LATH蛋白的可溶性表达，并利用镍柱亲和层析纯化获得高纯度重组蛋白，为后续功能研究奠定基础。
2. **《LATH重组蛋白调控胶原交联的分子机制研究》**
- 作者：Smith J, Brown K, et al.
- 摘要：通过体外实验证明，重组LATH蛋白通过催化胶原纤维交联增强组织机械强度，并揭示其活性中心的关键氨基酸位点。
3. **《LATH重组蛋白在肝纤维化模型中的治疗潜力》**
- 作者：Wang X, Chen L, et al.
- 摘要：利用哺乳动物细胞表达的重组LATH蛋白，在小鼠模型中显著抑制胶原过度沉积，表明其在抗纤维化治疗中的应用价值。
4. **《结构解析：重组人源LATH蛋白的晶体结构分析》**
- 作者：Tanaka R, Sato M, et al.
- 摘要：通过X射线晶体学首次解析了LATH蛋白的三维结构，揭示了其与底物结合的特异性结构域，为靶向药物设计提供依据。
**提示**：实际文献需通过PubMed、Google Scholar等平台检索关键词“LATH recombinant protein”、“LOXL2 recombinant”(若涉及赖氨酰氧化酶家族)或结合具体研究领域调整。
**Background of LATH Recombinant Protein**
LATH (lysyl hydroxylase) recombinant protein is an engineered form of the enzyme lysyl hydroxylase, which plays a critical role in post-translational modification of collagen and other proteins. Native lysyl hydroxylase catalyzes the hydroxylation of lysine residues in collagen chains, a process essential for forming stable cross-links that confer structural integrity to collagen fibrils. This enzyme is pivotal in maintaining tissue strength, particularly in skin, bones, and blood vessels. Dysregulation of lysyl hydroxylase activity is linked to connective tissue disorders, such as Ehlers-Danlos syndrome, and fibrotic diseases.
Recombinant LATH protein is produced using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to ensure high purity and activity. Its production enables detailed study of collagen biosynthesis, disease mechanisms, and therapeutic targeting. Researchers utilize LATH recombinant protein to investigate enzyme kinetics, substrate specificity, and interactions with cofactors like vitamin C and iron. It also serves as a tool for screening inhibitors or modulators for conditions involving abnormal collagen deposition, such as cancer metastasis or organ fibrosis.
In biopharmaceuticals, recombinant LATH holds potential for tissue engineering and regenerative medicine, where controlled collagen modification is crucial. Advances in protein engineering have improved its stability and scalability, addressing challenges like enzyme instability *in vitro*. Additionally, gene-edited cell lines expressing recombinant LATH are used to model diseases or produce hydroxylated collagen for biomedical applications. Overall, LATH recombinant protein bridges fundamental research and clinical innovation, offering insights into extracellular matrix biology and therapeutic development.
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