| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADAMTS8 |
| Uniprot No | Q9UP79 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 214-889aa |
| 氨基酸序列 | FVSEARF VETLLVADAS MAAFYGADLQ NHILTLMSVA ARIYKHPSIK NSINLMVVKV LIVEDEKWGP EVSDNGGLTL RNFCNWQRRF NQPSDRHPEH YDTAILLTRQ NFCGQEGLCD TLGVADIGTI CDPNKSCSVI EDEGLQAAHT LAHELGHVLS MPHDDSKPCT RLFGPMGKHH VMAPLFVHLN QTLPWSPCSA MYLTELLDGG HGDCLLDAPA AALPLPTGLP GRMALYQLDQ QCRQIFGPDF RHCPNTSAQD VCAQLWCHTD GAEPLCHTKN GSLPWADGTP CGPGHLCSEG SCLPEEEVER PKPVADGGWA PWGPWGECSR TCGGGVQFSH RECKDPEPQN GGRYCLGRRA KYQSCHTEEC PPDGKSFREQ QCEKYNAYNY TDMDGNLLQW VPKYAGVSPR DRCKLFCRAR GRSEFKVFEA KVIDGTLCGP ETLAICVRGQ CVKAGCDHVV DSPRKLDKCG VCGGKGNSCR KVSGSLTPTN YGYNDIVTIP AGATNIDVKQ RSHPGVQNDG NYLALKTADG QYLLNGNLAI SAIEQDILVK GTILKYSGSI ATLERLQSFR PLPEPLTVQL LTVPGEVFPP KVKYTFFVPN DVDFSMQSSK ERATTNIIQP LLHAQWVLGD WSECSSTCGA GWQRRTVECR DPSGQASATC NKALKPEDAK PCESQLCPL |
| 预测分子量 | 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ADAMTS8重组蛋白的3篇参考文献的简要总结(注：内容为示例性概括，实际文献需通过学术数据库检索确认)：
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1. **标题**：ADAMTS8重组蛋白的制备及其在肿瘤抑制中的功能研究
**作者**：Zhang Y, Wang L, et al.
**摘要**：本研究通过哺乳动物表达系统成功制备了重组ADAMTS8蛋白，并验证其具有金属蛋白酶活性。实验表明，ADAMTS8重组蛋白可通过降解细胞外基质蛋白(如Versican)抑制肿瘤细胞迁移和血管生成，提示其在肿瘤微环境调控中的潜在作用。
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2. **标题**：ADAMTS8重组蛋白的抗纤维化机制分析
**作者**：Chen X, Li H, et al.
**摘要**：该研究利用原核系统表达并纯化了ADAMTS8重组蛋白，发现其能够特异性切割细胞外基质中的COMP蛋白。在肺纤维化模型中，ADAMTS8重组蛋白通过调节TGF-β信号通路显著减轻纤维化程度，为其作为治疗靶点提供了依据。
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3. **标题**：ADAMTS8在心血管疾病中的功能及其重组蛋白活性鉴定
**作者**：Smith J, Patel R, et al.
**摘要**：作者通过昆虫细胞表达系统获得高纯度ADAMTS8重组蛋白，并证实其具有胶原水解酶活性。进一步研究发现，该蛋白可通过抑制血管平滑肌细胞异常增殖减缓动脉粥样硬化进展，揭示了其在心血管疾病中的保护作用。
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如需具体文献，建议通过PubMed、Web of Science等平台检索关键词“ADAMTS8 recombinant protein”或结合研究领域(如肿瘤、纤维化)筛选近期论文。
ADAMTS8 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 8) is a secreted extracellular matrix (ECM)-associated protease belonging to the ADAMTS family. This protein family is characterized by a conserved modular structure, including a prodomain, metalloproteinase domain, disintegrin-like domain, thrombospondin type 1 repeats (TSRs), and a cysteine-rich region. ADAMTS8 is primarily known for its role in ECM remodeling through proteolytic cleavage of components like aggrecan and versican, influencing tissue organization and cellular signaling pathways. It also exhibits anti-angiogenic properties by interacting with vascular endothelial growth factor (VEGF) or other mediators, suggesting potential roles in regulating tumor growth and metastasis.
Research has linked ADAMTS8 to various physiological and pathological processes. In cancer, it is often downregulated in malignancies such as lung, breast, and colorectal cancers, where its loss may promote tumor progression and angiogenesis. Conversely, in cardiovascular and fibrotic diseases, ADAMTS8 overexpression has been associated with adverse ECM remodeling, contributing to tissue stiffness and dysfunction. Despite its proposed tumor-suppressive functions, some studies suggest context-dependent roles, highlighting the need for further mechanistic exploration.
Recombinant ADAMTS8 protein is typically produced in mammalian or insect expression systems to ensure proper post-translational modifications. It serves as a critical tool for studying protease-substrate interactions, angiogenesis assays, and therapeutic development. Current investigations focus on harnessing its anti-angiogenic or ECM-modulating properties for targeted therapies, while its diagnostic potential as a biomarker for disease progression is also under evaluation. However, challenges remain in understanding its regulatory networks and tissue-specific functions across different pathological contexts.
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