| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADAM5 |
| Uniprot No | Q6NVV9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-412aa |
| 氨基酸序列 | MQTSILIKSS CRPQFQRRFH HRMQKQIQNI ISILSSASVI NSYDENDIRH SKPLLVQMDC NYNGYVAGIP NSLVTLSVCS GLRGTMQLKN ISYGIEPMEA VSGFIHKIYE EKYADTNILL EENDTYTWFN SEYQVRKSSE KTDFIKLFPR YIEMHIVVDK NLFKPANMIC RKSVGKECDF TEYCNGDLPY CLPDTYVRDG EYCDSGGAFC FQGKCRTFDK QCDDLIGRGS RGAPVFCYDE INTRGDNFGN CGTAHCLFQH ILCGKLVCTW EHRDLISRPN LSVIYAHVRD QTCVSTYLPR RTPPPVNSPI SITSYYSAED RDETFVQDGS MCGPDMYCFE MHCKHVRFLM NLKLCDASNH CDRHGVCNNF NHCHCEKGYN PPYCQPKQGA FGSIDDGHLV PPTERSYMEE GR |
| 预测分子量 | 47,1 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. |
关于ADAM5重组蛋白的研究目前较为有限，以下为基于领域相关性的推测性文献示例(非真实存在，仅作参考框架)：
1. **文献名称**：*ADAM5重组蛋白在精子发生中的功能研究*
**作者**：Smith et al.
**摘要**：本研究成功在大肠杆菌中表达了重组ADAM5胞外域蛋白，并发现其在小鼠睾丸组织中介导细胞黏附信号通路，可能参与生殖细胞分化调控。
2. **文献名称**：*ADAM5金属蛋白酶活性及其底物筛选*
**作者**：Zhang & Lee
**摘要**：通过昆虫细胞系统表达人源ADAM5重组蛋白，证实其具有依赖锌离子的蛋白酶活性，并鉴定出其对细胞外基质蛋白的切割作用。
3. **文献名称**：*ADAM5重组蛋白在肿瘤迁移中的潜在作用*
**作者**：Garcia-Reyes et al.
**摘要**：利用哺乳动物HEK293细胞表达ADAM5重组蛋白，发现其通过调控EGF受体脱落促进乳腺癌细胞侵袭，提示其作为癌症治疗靶点的可能性。
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**注意**：目前公开数据库中暂未检索到明确以“ADAM5”为核心的重组蛋白文献，可能与以下原因相关：
1. ADAM家族成员可能存在命名混淆(如ADAM5在部分物种中未被明确表征);
2. 相关研究可能聚焦于其他ADAMs(如ADAM10/17等热门成员);
3. 建议核实蛋白名称准确性或扩展检索关键词(如结合物种名或功能描述)。
**Background of ADAM5 Recombinant Protein**
ADAM5 (A Disintegrin and Metalloproteinase 5) is a member of the ADAM family of transmembrane proteins, which are characterized by their dual roles in cell adhesion and proteolytic processing. These proteins typically consist of multiple domains, including a prodomain, metalloproteinase domain, disintegrin-like domain, cysteine-rich region, transmembrane segment, and cytoplasmic tail. ADAM5. though less extensively studied than other ADAMs like ADAM17 or ADAM10. is hypothesized to participate in extracellular matrix remodeling, cell signaling, and cell-cell interactions through its proteolytic and adhesive activities.
Functionally, ADAM proteins are implicated in shedding membrane-bound growth factors, cytokines, and receptors, thereby regulating processes such as inflammation, tissue development, and cancer progression. While ADAM5’s specific substrates remain unclear, its structural homology to other ADAMs suggests potential roles in reproductive biology, immune regulation, or neuronal development. For instance, some ADAMs are critical in sperm-egg fusion or neuronal synapse formation, though direct evidence for ADAM5 in these contexts is limited.
Recombinant ADAM5 protein is engineered for experimental studies, often expressed in mammalian or insect cell systems to ensure proper post-translational modifications. The recombinant form typically lacks the transmembrane domain, rendering it soluble for in vitro assays. Researchers utilize this protein to investigate its enzymatic activity, substrate specificity, and interactions with inhibitors or signaling molecules.
Despite its potential, ADAM5 remains undercharacterized compared to other ADAM family members. Current research focuses on elucidating its physiological roles, pathological associations (e.g., in cancer or inflammatory diseases), and therapeutic targeting. Challenges include identifying its natural substrates and clarifying its tissue-specific expression patterns. Advances in structural biology and genetic models may accelerate understanding of ADAM5’s contributions to health and disease, positioning it as a candidate for biomarker discovery or targeted therapy development.
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