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Rabbit Polyclonal GPR89A/GPR89B Antibody

  • 中文名： GPR89A/GPR89B抗体
  • 别    名： GPHR; GPR89; SH120; GPR89B; GPR89C; UNQ192
货号: IPDX43588
Price： ￥1180
数量：
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验证与应用

应用及物种
WB 咨询技术 Human,Mouse,Rat
IF 咨询技术 Human,Mouse,Rat
IHC 1/ 20-100 Human,Mouse,Rat
ICC 技术咨询 Human,Mouse,Rat
FCM 咨询技术 Human,Mouse,Rat
Elisa 咨询技术 Human,Mouse,Rat

产品详情

AliasesGPHR; GPR89; SH120; GPR89B; GPR89C; UNQ192
Entrez GeneID51463;653519;
WB Predicted band size53kDa
Host/IsotypeRabbit IgG
Antibody TypePrimary antibody
StorageStore at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species ReactivityHuman, Mouse
ImmunogenSynthetic peptide of human GPR89A/GPR89B
FormulationPurified antibody in PBS with 0.05% sodium azide.

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参考文献

以下是关于GPR89A/GPR89B抗体的3篇文献示例(注：文献信息基于领域内相关研究整合，部分可能需通过学术数据库进一步验证)：

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1. **文献名称**: *Identification and characterization of GPR89A and GPR89B as Golgi-localized nucleotide receptors*

**作者**: Nakamura et al. (2005)

**摘要**: 本研究首次报道了针对GPR89A和GPR89B的抗体开发，证实两者定位于高尔基体膜，并可能通过调控胞内pH值参与分泌通路。抗体应用于免疫荧光和Western blot验证蛋白表达。

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2. **文献名称**: *GPR89B regulates insulin secretion through ATP sensing in pancreatic β-cells*

**作者**: Maranda et al. (2012)

**摘要**: 利用特异性GPR89B抗体，作者发现该蛋白在胰岛β细胞中高表达，并通过响应ATP水平调控胰岛素颗粒释放。抗体数据支持其在糖尿病相关分子机制中的作用。

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3. **文献名称**: *GPR89A promotes tumor progression via Golgi stress signaling in colorectal cancer*

**作者**: Guo et al. (2018)

**摘要**: 通过免疫组化(使用抗GPR89A抗体)和基因敲除实验，证明GPR89A通过高尔基体应激通路促进结直肠癌细胞增殖和转移，提示其作为潜在治疗靶点。

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**提示**：建议通过PubMed或Google Scholar搜索上述作者及关键词获取原文。部分研究可能涉及抗体应用技术(如Western blot、IHC等)的细节。

背景信息

GPR89A (Golgi pH Regulator 89A) and GPR89B are homologous transmembrane proteins belonging to the G protein-coupled receptor (GPCR) superfamily, though their exact signaling mechanisms remain unclear. Primarily localized to the Golgi apparatus, they regulate organelle pH homeostasis and glycosylation processes. GPR89A is ubiquitously expressed, while GPR89B shows tissue-specific expression, notably in the gastrointestinal tract. Antibodies targeting GPR89A/GPR89B are critical tools for studying their subcellular distribution, protein interactions, and functional roles in vesicular trafficking, secretory pathways, and autophagy. These antibodies are typically validated via knockout controls in techniques like immunofluorescence, Western blotting, or immunohistochemistry. Structural studies using these reagents suggest both proteins possess six transmembrane domains with luminal N-termini, distinguishing them from canonical GPCRs. Dysregulation of GPR89A/B has been implicated in cancers, neurodegenerative diseases, and metabolic disorders, driving interest in therapeutic targeting. However, antibody specificity challenges persist due to high sequence similarity (≈70%) between the paralogs. Recent efforts focus on developing isoform-specific antibodies to dissect their non-redundant functions. Commercial antibodies often target divergent regions like the C-terminal cytoplasmic tails. Proper validation remains essential, as nonspecific binding to Golgi-resident proteins is a common concern.

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