纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ITGa10 |
Uniprot No | O75578 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1167aa |
氨基酸序列 | MELPFVTHLFLPLVFLTGLCSPFNLDEHHPRLFPGPPEAEFGYSVLQHVGGGQRWMLVGAPWDGPSGDRRGDVYRCPVGGAHNAPCAKGHLGDYQLGNSSHPAVNMHLGMSLLETDGDGGFMACAPLWSRACGSSVFSSGICARVDASFQPQGSLAPTAQRCPTYMDVVIVLDGSNSIYPWSEVQTFLRRLVGKLFIDPEQIQVGLVQYGESPVHEWSLGDFRTKEEVVRAAKNLSRREGRETKTAQAIMVACTEGFSQSHGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRQRDPSSFLREIRTIASDPDERFFFNVTDEAALTDIVDALGDRIFGLEGSHAENESSFGLEMSQIGFSTHRLKDGILFGMVGAYDWGGSVLWLEGGHRLFPPRMALEDEFPPALQNHAAYLGYSVSSMLLRGGRRLFLSGAPRFRHRGKVIAFQLKKDGAVRVAQSLQGEQIGSYFGSELCPLDTDRDGTTDVLLVAAPMFLGPQNKETGRVYVYLVGQQSLLTLQGTLQPEPPQDARFGFAMGALPDLNQDGFADVAVGAPLEDGHQGALYLYHGTQSGVRPHPAQRIAAASMPHALSYFGRSVDGRLDLDGDDLVDVAVGAQGAAILLSSRPIVHLTPSLEVTPQAISVVQRDCRRRGQEAVCLTAALCFQVTSRTPGRWDHQFYMRFTASLDEWTAGARAAFDGSGQRLSPRRLRLSVGNVTCEQLHFHVLDTSDYLRPVALTVTFALDNTTKPGPVLNEGSPTSIQKLVPFSKDCGPDNECVTDLVLQVNMDIRGSRKAPFVVRGGRRKVLVSTTLENRKENAYNTSLSLIFSRNLHLASLTPQRESPIKVECAAPSAHARLCSVGHPVFQTGAKVTFLLEFEFSCSSLLSQVFVKLTASSDSLERNGTLQDNTAQTSAYIQYEPHLLFSSESTLHRYEVHPYGTLPVGPGPEFKTTLRVQNLGCYVVSGLIISALLPAVAHGGNYFLSLSQVITNNASCIVQNLTEPPGPPVHPEELQHTNRLNGSNTQCQVVRCHLGQLAKGTEVSVGLLRLVHNEFFRRAKFKSLTVVSTFELGTEEGSVLQLTEASRWSESLLEVVQTRPILISLWILIGSVLGGLLLLALLVFCLWKLGFFAHKKIPEEEKREEKLEQ |
预测分子量 | 127 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ITGa10(整合素α10)重组蛋白的示例性参考文献(注:文献信息为假设性示例,实际研究中请核实具体文献):
1. **文献名称**: *"Cloning and Functional Characterization of Integrin Alpha 10 Subunit in Cartilage Development"*
**作者**: Camper L, et al.
**摘要**: 本研究克隆了人ITGa10基因,并在CHO细胞中成功表达其重组蛋白。研究发现,ITGa10与β1整合素亚基结合形成受体,特异性识别胶原蛋白VI和XVIII,对软骨细胞分化和软骨基质形成起关键作用。
2. **文献名称**: *"Recombinant ITGa10 as a Biomarker for Osteoarthritis Progression"*
**作者**: Knutson SK, et al.
**摘要**: 通过重组ITGa10蛋白的体外实验,发现其在骨关节炎患者的软骨组织中表达显著上调。研究提示,ITGa10可能通过调控细胞-基质黏附参与疾病进展,或成为潜在的治疗靶点。
3. **文献名称**: *"Structural Analysis of Integrin Alpha10beta1 and Its Collagen-Binding Domains"*
**作者**: Barczyk M, et al.
**摘要**: 利用重组ITGa10β1蛋白解析其晶体结构,揭示了其与胶原结合的关键表位,并通过突变实验验证了特定氨基酸在配体识别中的必要性,为开发靶向药物提供了结构基础。
4. **文献名称**: *"ITGa10 Recombinant Protein Enhances Mesenchymal Stem Cell Chondrogenesis"*
**作者**: Li Y, et al.
**摘要**: 研究发现,外源性添加重组ITGa10蛋白可显著促进间充质干细胞的软骨分化能力,表明其在软骨组织工程中的应用潜力。
(注:以上文献为模拟示例,实际引用时需通过PubMed或专业数据库检索真实文献。)
Integrin alpha-10 (ITGA10) is a transmembrane glycoprotein belonging to the integrin family of cell adhesion receptors. It pairs exclusively with the beta-1 subunit (ITGB1) to form the α10β1 heterodimer, which serves as a collagen-binding receptor. ITGA10 is primarily expressed in chondrocytes, the specialized cells responsible for cartilage formation and maintenance, where it plays a critical role in mediating cell-matrix interactions during skeletal development and tissue homeostasis. Its extracellular domain recognizes collagen types II, IV, and VI, facilitating cellular adhesion, migration, and signaling in cartilage and other collagen-rich tissues.
Structurally, ITGA10 consists of a large extracellular region with a β-propeller domain, thigh and calf domains, a single-pass transmembrane helix, and a short cytoplasmic tail. The protein's collagen-binding activity depends on a metal ion-dependent adhesion site (MIDAS) motif, which coordinates divalent cations like Mg²⁺ for ligand recognition. Dysregulation of ITGA10 has been implicated in cartilage-related pathologies, including osteoarthritis and cartilage repair defects, making it a potential biomarker or therapeutic target.
Recombinant ITGA10 proteins are typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper glycosylation and structural integrity. These purified proteins are widely used to study integrin-collagen interactions, screen for modulators of chondrocyte function, or generate antibodies for diagnostic applications. Recent studies also explore its role in tumor microenvironments, particularly in cancers involving collagen remodeling. Its tissue-specific expression and functional specialization in cartilage biology continue to drive research in regenerative medicine and musculoskeletal disease models.
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