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Recombinant Human OXM protein

  • 中文名: 胃泌酸调节素(OXM)重组蛋白
  • 别    名: OXM;Olfactory receptor 51M1
货号: PA2000-1603
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点OXM
Uniprot No P01275
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 53-89aa
氨基酸序列HSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIA
预测分子量 6.4 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3篇与OXM(Oxyntomodulin)重组蛋白相关的文献摘要示例:

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1. **文献名称**:*Recombinant Oxyntomodulin Exhibits Dual Agonist Activity at GLP-1 and Glucagon Receptors and Promotes Weight Loss in Diet-Induced Obese Mice*

**作者**:Druce, M.R. et al.

**摘要**:本研究通过基因工程技术在大肠杆菌中表达并纯化重组OXM蛋白,验证其对GLP-1和胰高血糖素受体的双重激动作用。动物实验表明,重组OXM能显著降低高脂饮食诱导的肥胖小鼠体重,并改善糖代谢,提示其在代谢疾病治疗中的潜力。

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2. **文献名称**:*PEGylated Oxyntomodulin: A Long-Acting Recombinant Protein for Obesity Therapy*

**作者**:Chen, Q. et al.

**摘要**:作者通过聚乙二醇(PEG)修饰重组OXM蛋白以延长其半衰期。药代动力学研究显示,PEG化OXM的血浆清除率显著降低,且在小鼠模型中持续抑制食欲并减少脂肪积累,为长效OXM制剂的开发提供依据。

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3. **文献名称**:*Expression and Purification of Bioactive Recombinant Oxyntomodulin in Pichia pastoris*

**作者**:Zhang, Y. et al.

**摘要**:研究利用毕赤酵母系统高效表达重组OXM蛋白,并通过两步层析法纯化获得高纯度产物。体外实验证实,重组OXM可激活人源GLP-1受体,并促进胰岛素分泌,展示了其在糖尿病治疗中的应用前景。

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注:以上文献为示例性质,实际引用需根据具体研究补充完整信息。建议通过PubMed、Web of Science等数据库以关键词“recombinant oxyntomodulin”或“OXM expression”检索最新文献。

背景信息

OXM (Oxyntomodulin) is a naturally occurring peptide hormone derived from the post-translational processing of proglucagon in enteroendocrine L-cells of the small intestine. Structurally, it consists of 37 amino acids and shares sequence homology with both glucagon and glucagon-like peptide-1 (GLP-1), containing the full glucagon sequence (29 amino acids) followed by an 8-amino acid C-terminal extension. This dual structure enables OXM to interact with both the glucagon receptor (GCGR) and GLP-1 receptor (GLP-1R), positioning it as a unique dual agonist in metabolic regulation.

Discovered in the 1980s, OXM gained research attention for its combined anorexigenic and energy-expenditure effects. Unlike single-target agonists, its dual receptor activation simultaneously reduces appetite through central nervous system signaling and enhances thermogenesis via peripheral mechanisms. These properties make it a promising therapeutic candidate for metabolic disorders, particularly obesity and type 2 diabetes. Studies show OXM improves glucose homeostasis, promotes weight loss, and may benefit non-alcoholic fatty liver disease (NAFLD).

Recombinant OXM production utilizes genetic engineering in microbial (E. coli, yeast) or mammalian cell systems, followed by purification processes to ensure bioactivity. Current research focuses on overcoming pharmacokinetic limitations—native OXM's short half-life (~7-12 minutes) requires frequent administration. Strategies include structural modifications (PEGylation, amino acid substitutions) and sustained-release formulations to enhance therapeutic viability.

Phase I/II clinical trials demonstrate favorable safety profiles and dose-dependent metabolic improvements. However, balancing GCGR/GLP-1R activation ratios remains crucial to optimize efficacy while minimizing potential side effects. As a multifunctional peptide, OXM represents a paradigm shift in developing combinatorial therapies for complex metabolic diseases.

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