| WB | 1/1000 | 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 | Carboxypeptidase N catalytic chain, CPN, Anaphylatoxin inactivator, Arginine carboxypeptidase, Carboxypeptidase N polypeptide 1, Carboxypeptidase N small subunit, Kininase-1, Lysine carboxypeptidase, Plasma carboxypeptidase B, Serum carboxypeptidase N, SCPN, CPN1, ACBP |
| Entrez GeneID | 1369 |
| WB Predicted band size | 52.3kDa |
| 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, Mouse |
| Immunogen | This CPN1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 52-81 amino acids from the N-terminal region of human CPN1. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,1%BSA and 50% glycerol.prepared by Saturated Ammonium Sulfate (SAS) . |
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以下是关于 CPN1(N-terminal)抗体的参考文献示例(内容为模拟概括，实际引用请核对原文)：
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1. **文献名称**: *Carboxypeptidase N: A Key Regulator of Inflammation and Coagulation*
**作者**: Levin, Y. et al.
**摘要**: 研究探讨了CPN1(N端结构域)在炎症反应和凝血级联中的调控作用，利用特异性N端抗体证实了CPN1通过降解缓激肽和补体肽调节血管通透性，为抗炎治疗提供潜在靶点。
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2. **文献名称**: *Structural Characterization of Human Carboxypeptidase N Subunit 1*
**作者**: Skidgel, R.A. & Erdös, E.G.
**摘要**: 通过X射线晶体学解析CPN1的N端结构域三维构象，使用N端抗体验证其功能表位，揭示了底物结合的关键位点及其与酶活性的关系。
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3. **文献名称**: *Genetic Deficiency of CPN1 Alters Plasma Peptide Homeostasis*
**作者**: Platt, O.S. et al.
**摘要**: 研究CPN1基因缺陷患者的血浆样本，通过N端抗体检测发现CPN1水平显著降低，导致血管活性肽(如C5a、des-Arg9-bradykinin)累积，与遗传性血管水肿相关。
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4. **文献名称**: *Role of CPN1 in Sepsis-Induced Coagulopathy*
**作者**: Matthews, K.W. & Sang, Y.
**摘要**: 利用CPN1(N-term)抗体分析脓毒症模型小鼠，发现CPN1通过降解促凝血肽抑制血栓形成，其表达下调加剧多器官衰竭，提示其临床预后价值。
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**注**：以上文献为示例性内容，实际引用时需查询真实数据库(如PubMed)并核对作者、标题及摘要准确性。
The CPN1 (N-term) antibody is designed to target the amino-terminal region of carboxypeptidase N1 (CPN1), a key enzyme in the regulation of bioactive peptides. CPN1. also known as kininase I or anaphylatox inase, is a zinc-dependent metalloprotease primarily synthesized in the liver and secreted into plasma. It plays a critical role in modulating inflammatory and immune responses by cleaving C-terminal arginine or lysine residues from peptides such as bradykinin, anaphylatoxins (C3a, C4a, C5a), and fibrinopeptides, thereby regulating their bioactivity. The N-terminal region of CPN1 is involved in substrate recognition and enzyme activation, making it a strategic epitope for functional studies.
This antibody is widely used in research to investigate CPN1 expression, localization, and function in physiological and pathological contexts, including inflammation, sepsis, and cardiovascular diseases. It is commonly applied in techniques like Western blotting, immunohistochemistry, and ELISA to detect CPN1 in biological samples. Commercial CPN1 (N-term) antibodies are often raised in rabbits or mice and validated for specificity using knockout controls or recombinant protein assays.
Studies utilizing this antibody have contributed to understanding CPN1’s role in modulating blood pressure, vascular permeability, and immune activation. Dysregulation of CPN1 is linked to hereditary angioedema, thrombosis, and cancer progression, underscoring its clinical relevance. The N-term specificity ensures minimal cross-reactivity with other carboxypeptidases, enhancing experimental accuracy.
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