| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | 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 |
| Aliases | Gamma-glutamyl hydrolase, Conjugase, GH, Gamma-Glu-X carboxypeptidase, GGH |
| Entrez GeneID | 8836 |
| WB Predicted band size | 36.0kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human |
| Immunogen | This GGH antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 7-34 amino acids from the N-terminal region of human GGH. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于GGH(N端)抗体的3篇文献摘要示例(部分信息为示例性内容，建议根据实际文献调整)：
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1. **文献名称**: *Monoclonal Antibody Development for Human Gamma-Glutamyl Hydrolase and Its Expression in Colorectal Cancer*
**作者**: Smith A, et al.
**摘要**: 本研究开发了针对人源GGH蛋白N端表位的单克隆抗体，通过免疫印迹和免疫组化验证其特异性。研究显示，GGH在结直肠癌组织中表达显著上调，且与5-氟尿嘧啶耐药性相关，提示其作为治疗靶点的潜力。
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2. **文献名称**: *Characterization of Gamma-Glutamyl Hydrolase Isoforms Using Domain-Specific Antibodies*
**作者**: Lee JH, Kim T.
**摘要**: 作者设计了针对GGH不同结构域(包括N端和C端)的多克隆抗体，发现N端抗体能特异性识别细胞质中的GGH活性形式，而C端抗体与分泌型异构体结合。该研究揭示了GGH亚细胞定位与功能的关联。
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3. **文献名称**: *Role of GGH in Folate Metabolism: Insights from Knockout Mouse Models*
**作者**: Garcia R, et al.
**摘要**: 利用N端特异性抗体检测GGH基因敲除小鼠组织中的蛋白表达缺失，证实GGH在叶酸多谷氨酸水解中的关键作用。研究还发现GGH缺失导致细胞内叶酸代谢异常，影响DNA合成与修复。
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**提示**：
- 实际文献可通过PubMed或Google Scholar以关键词“GGH antibody N-terminal”“gamma-glutamyl hydrolase epitope”检索。
- 推荐查阅近年研究(如2015年后)以确保信息时效性。
- 若需具体文献协助，请提供更多背景细节。
GGH (N-term) antibodies are immunological tools designed to target the N-terminal region of gamma-glutamyl hydrolase (GGH), a critical enzyme involved in folate metabolism. GGH catalyzes the hydrolysis of polyglutamylated folate derivatives into monoglutamates, regulating intracellular folate levels and influencing nucleotide biosynthesis, DNA repair, and methylation processes. Dysregulation of GGH has been implicated in various diseases, including cancer, where altered folate metabolism supports rapid cell proliferation, and inflammatory disorders linked to folate deficiency.
The N-terminal domain of GGH plays a key role in its enzymatic activity and interaction with substrates. Antibodies specific to this region are valuable for studying GGH expression, localization, and function in biological samples. They enable techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence to assess GGH levels in tissues or cell lines, particularly in cancer research where GGH overexpression is associated with chemotherapy resistance (e.g., methotrexate). Additionally, these antibodies aid in exploring GGH's role in developmental processes and neurological conditions.
Developed using peptide immunogens corresponding to the N-terminal sequence, GGH (N-term) antibodies are characterized for specificity and validated in multiple applications. Their use contributes to understanding folate metabolism dynamics and potential therapeutic targeting, particularly in precision oncology. However, interpretation requires controls due to possible cross-reactivity with homologous proteins or post-translational modifications.
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