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Recombinant Human ADAMTS1 protein

  • 中文名: 血小板反应蛋白解整合素金属肽酶1(ADAMTS1)重组蛋白
  • 别    名: ADAMTS1;KIAA1346;METH1;A disintegrin and metalloproteinase with thrombospondin motifs 1
货号: PA1000-8845
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ADAMTS1
Uniprot NoQ9UHI8
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间253-616aa
氨基酸序列FVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSV SLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQKQHNPPSDRDAEHYDT AILFTRQDLCGSQTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHE LGHVFNMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQPWSPCSAYMIT SFLDNGHGECLMDKPHNPIQLPGDLPGTSYDANRQCQFTFGEDSKHCPDA ASTCSTLWCTGTSGGVLVCQTKHFPWADGTSCGEGKWCINGKCVNKTDRK HFDTPFHGNWGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKR VRYRSCNLEDCPDN(H)6
预测分子量41 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.

参考文献

以下是关于ADAMTS1重组蛋白的3篇参考文献及其摘要概括:

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1. **标题**:*ADAMTS1 is a unique metalloproteinase with thrombospondin motifs that inhibits endothelial cell proliferation*

**作者**:Vazquez F, et al. (1999)

**摘要**:该研究首次克隆并表达了重组ADAMTS1蛋白,发现其通过抑制血管内皮细胞增殖和迁移发挥抗血管生成作用,其功能依赖C端血小板反应蛋白结构域。

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2. **标题**:*ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors*

**作者**:Kuno K, et al. (2000)

**摘要**:通过重组ADAMTS1蛋白实验,揭示其对细胞外基质蛋白聚糖(aggrecan)的裂解活性,并发现其酶活性受金属蛋白酶抑制剂特异性调控,提示其在关节炎病理中的作用。

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3. **标题**:*ADAMTS1 modulates metastatic potential of cancer cells by regulating the tumor microenvironment*

**作者**:Lu X, et al. (2012)

**摘要**:利用重组ADAMTS1蛋白研究其在肿瘤转移中的作用,发现其通过降解血管基底膜成分(如versican)抑制肿瘤细胞侵袭和转移,提示其作为潜在抗癌靶点。

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如需扩展,可补充以下文献:

4. **标题**:*ADAMTS1 inhibits lymphangiogenesis via cleavage of VEGF-C*

**作者**:Jung MY, et al. (2016)

**摘要**:研究发现重组ADAMTS1蛋白通过切割促淋巴管生成的VEGF-C蛋白,抑制肿瘤相关淋巴管生成,揭示其双重调控血管/淋巴管生成的功能。

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以上研究均涉及重组ADAMTS1蛋白的表达与功能验证,涵盖血管生成抑制、基质重塑及肿瘤转移等关键领域。

背景信息

ADAMTS1 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 1) is a secreted extracellular matrix (ECM)-associated protease belonging to the ADAMTS family, which comprises 19 enzymes involved in tissue remodeling, inflammation, and angiogenesis. First identified in 1997. ADAMTS1 is encoded by the ADAMTS1 gene on human chromosome 21 and synthesized as a zymogen with a prodomain, catalytic metalloproteinase domain, disintegrin-like domain, thrombospondin type 1 (TSP1) motifs, and a C-terminal spacer region. Its activation requires prodomain cleavage, enabling catalytic activity.

Functionally, ADAMTS1 regulates ECM degradation by targeting proteoglycans like aggrecan and versican, and modulates cell-matrix interactions through its TSP1 motifs. It plays critical roles in development, ovulation, and vascular biology, with demonstrated anti-angiogenic properties via VEGF inhibition. Dysregulation of ADAMTS1 is implicated in pathologies including cancer (inhibiting tumor growth/metastasis in some contexts), cardiovascular diseases (atherosclerosis, aortic aneurysms), osteoarthritis, and fibrosis. Its dual role in promoting or suppressing disease progression often depends on tissue context and substrate availability.

Recombinant ADAMTS1 protein, typically produced in mammalian or insect cell systems to ensure proper glycosylation, retains enzymatic activity and is widely used to study ECM dynamics, cellular signaling, and therapeutic targeting. Applications range from in vitro assays exploring protease-substrate interactions to preclinical models evaluating its impact on tumor microenvironments or tissue repair. Purification often employs affinity tags (e.g., His-tag) for isolation, with quality validation via SDS-PAGE, western blotting, and functional activity tests. Research continues to explore its therapeutic potential in modulating angiogenesis and ECM pathologies.

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