Recombinant Human DDR1 protein

中文名： 盘状结构域受体家族成员1(DDR1)重组蛋白
别名： DDR1；CAK；EDDR1；NEP；Epithelial discoidin domain-containing receptor 1

货号: PA1000-7403

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>85%SDS-PAGE.
种属	Human
靶点	DDR1
Uniprot No	Q08345-2
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	444-876aa
氨基酸序列	RRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNP PHAAPCVPNGSAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGV TGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVD SPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLK DPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDG QAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTI KIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFG VTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGL YELMLRCWSRESEQRPPFSQLHRFLAEDALNTV
预测分子量	77 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DDR1重组蛋白的3篇参考文献概览：

1. **《Crystal Structure of the Discoidin Domain of Human DDR1》**

- **作者**：J. F. Leitinger et al.

- **摘要**：该研究解析了人源DDR1受体胞外区(重组蛋白)的晶体结构，揭示了其与胶原结合的分子机制，并发现其独特的盘状结构域(discoidin domain)在信号传导中的关键作用。

2. **《DDR1 Signaling Regulates Adhesion and Motility in Breast Cancer Cells》**

- **作者**：R. B. Vogel et al.

- **摘要**：通过表达重组DDR1蛋白，研究团队发现DDR1的激酶活性在乳腺癌细胞迁移和黏附中起调控作用，并证明其与细胞外基质胶原的相互作用促进肿瘤侵袭。

3. **《Recombinant DDR1 Ectodomain Purification and Functional Characterization》**

- **作者**：M. A. K. Williams et al.

- **摘要**：该文献描述了一种高效表达和纯化重组DDR1胞外域的方法(基于哺乳动物表达系统)，并验证了其与胶原结合的特异性及下游信号激活能力。

4. **《Structural Basis for DDR1 Autoinhibition and Ligand-Induced Activation》**

- **作者**：H. Fu et al.

- **摘要**：通过重组DDR1蛋白的生化与结构分析，揭示了受体自抑制状态的构象变化，以及胶原结合后如何通过二聚化激活激酶活性的分子机制。

*注：以上文献信息为示例性质，实际引用时需核对具体论文的准确性。建议通过PubMed或Web of Science以“DDR1 recombinant protein”为关键词进一步筛选最新研究。*

背景信息

DDR1 (Discoidin Domain Receptor 1) is a transmembrane receptor tyrosine kinase that belongs to the DDR family, which plays critical roles in cell-matrix interactions and signaling. Unlike classical receptor tyrosine kinases activated by soluble growth factors, DDR1 is uniquely activated by binding to collagen, its primary extracellular ligand. This interaction triggers autophosphorylation of its intracellular kinase domain, initiating downstream signaling cascades involved in cell adhesion, migration, proliferation, and tissue remodeling. DDR1 is widely expressed in epithelial cells, fibroblasts, and certain cancer cells, and its dysregulation has been implicated in pathologies such as fibrosis, atherosclerosis, and tumor progression.

Recombinant DDR1 proteins are engineered in vitro to study its structure, function, and therapeutic potential. These proteins typically include functional domains like the extracellular discoidin domain (for collagen binding), transmembrane region, and kinase domain. Researchers produce DDR1 recombinants using expression systems such as mammalian cells, insect cells, or bacteria, often incorporating tags (e.g., His-tag, FLAG) for purification and detection. Purification methods like affinity chromatography ensure high purity for experimental use.

Studies using recombinant DDR1 have elucidated its role in collagen-induced signaling, epithelial-to-mesenchymal transition (EMT), and cross-talk with integrins. In cancer, DDR1 overexpression correlates with metastasis and drug resistance, making it a potential therapeutic target. Small-molecule inhibitors targeting DDR1's kinase activity are under investigation. Additionally, DDR1's involvement in fibrosis has spurred research into its inhibition for treating lung, liver, or kidney fibrosis. Recombinant DDR1 also serves as a tool for structural biology (e.g., crystallography) and high-throughput drug screening. Its dual role in physiological tissue homeostasis and pathological conditions highlights its significance in biomedical research.