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Recombinant Human GPR128 Protein

  • 中文名: 重组人GPR128蛋白
  • 别    名: ADGRG7; GPR128; Adhesion G-protein coupled receptor G7; G-protein coupled receptor 128
货号: PA2000-8036
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点GPR128
Uniprot NoQ96K78
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-797aa
氨基酸序列MASCRAWNLRVLVAVVCGLLTGIILGLGIWRIVIRIQRGKSTSSSSTPTEFCRNGGTWENGRCICTEEWKGLRCTIANFCENSTYMGFTFARIPVGRYGPSLQTCGKDTPNAGNPMAVRLCSLSLYGEIELQKVTIGNCNENLETLEKQVKDVTAPLNNISSEVQILTSDANKLTAENITSATRVVGQIFNTSRNASPEAKKVAIVTVSQLLDASEDAFQRVAATANDDALTTLIEQMETYSLSLGNQSVVEPNIAIQSANFSSENAVGPSNVRFSVQKGASSSLVSSSTFIHTNVDGLNPDAQTELQVLLNMTKNYTKTCGFVVYQNDKLFQSKTFTAKSDFSQKIISSKTDENEQDQSASVDMVFSPKYNQKEFQLYSYACVYWNLSAKDWDTYGCQKDKGTDGFLRCRCNHTTNFAVLMTFKKDYQYPKSLDILSNVGCALSVTGLALTVIFQIVTRKVRKTSVTWVLVNLCISMLIFNLLFVFGIENSNKNLQTSDGDINNIDFDNNDIPRTDTINIPNPMCTAIAALLHYFLLVTFTWNALSAAQLYYLLIRTMKPLPRHFILFISLIGWGVPAIVVAITVGVIYSQNGNNPQWELDYRQEKICWLAIPEPNGVIKSPLLWSFIVPVTIILISNVVMFITISIKVLWKNNQNLTSTKKVSSMKKIVSTLSVAVVFGITWILAYLMLVNDDSIRIVFSYIFCLFNTTQGLQIFILYTVRTKVFQSEASKVLMLLSSIGRRKSLPSVTRPRLRVKMYNFLRSLPTLHERFRLLETSPSTEEITLSESDNAKESI
分子量88.9 kDa
蛋白标签His tag N-Terminus
缓冲液0
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

以下是关于重组人GPR128蛋白的模拟参考文献示例,基于相关领域研究的典型方向整理:

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### 1. **《Structural and functional characterization of recombinant human GPR128》**

**作者**: Zhang, L. et al.

**摘要**: 本研究通过HEK293细胞表达并纯化了重组人GPR128蛋白,利用冷冻电镜解析其三维结构。结果显示,GPR128属于粘附型G蛋白偶联受体(aGPCR)亚家族,胞外结构域具有潜在的配体结合位点,为研究其信号传导机制奠定基础。

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### 2. **《GPR128 regulates intestinal stem cell maintenance through mechanosensing pathways》**

**作者**: Wang, Y. et al.

**摘要**: 通过构建GPR128基因敲除小鼠模型,发现GPR128在肠道干细胞中高表达,并参与调控类器官形成和分化。重组GPR128蛋白的功能实验表明,其通过感知机械应力激活Hippo-YAP信号通路,影响干细胞自我更新。

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### 3. **《Oncogenic role of GPR128 in myeloid leukemia progression》**

**作者**: Müller, S. et al.

**摘要**: 分析白血病患者样本发现,GPR128在骨髓细胞中异常高表达。体外实验显示,重组GPR128蛋白过表达可促进白血病细胞增殖并抑制凋亡,提示其可能作为潜在治疗靶点。

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### 4. **《Adhesion GPCR GPR128 interacts with extracellular matrix proteins to modulate immune cell adhesion》**

**作者**: Tanaka, K. et al.

**摘要**: 研究证实重组人GPR128蛋白通过胞外域与纤维连接蛋白(Fibronectin)结合,调控T细胞的粘附和迁移。该发现为理解aGPCR在免疫微环境中的作用提供了新视角。

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**备注**:以上文献为示例性内容,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。


背景信息

GPR128 (G protein-coupled receptor 128) is a class A orphan G protein-coupled receptor (GPCR) encoded by the ADGRG7 gene in humans. As a member of the adhesion GPCR subfamily, it features a large extracellular N-terminal domain containing adhesion-like motifs, suggesting potential roles in cell-cell or cell-matrix interactions. Despite its classification, the endogenous ligand, precise signaling pathways, and physiological functions of GPR128 remain poorly characterized, warranting further investigation.

Recombinant human GPR128 protein is typically engineered for experimental studies to overcome challenges in isolating native forms. Produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells), it enables structural and functional analyses. Research highlights its potential involvement in immune regulation, tissue development, and cancer progression. For instance, studies link GPR128 to hematopoietic stem cell maintenance and intestinal stem cell proliferation, while altered expression is observed in gastrointestinal cancers and leukemia.

Current applications of recombinant GPR128 include ligand screening, antibody development, and mechanistic studies exploring its interaction with extracellular matrix components or signaling partners. Its orphan status and disease associations position it as a novel target for therapeutic exploration, though deorphanization efforts and validation of its pathophysiological roles remain critical hurdles.


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