Abcam, ab230868, Anti-CPM antibody

Size: 200µL
Rabbit Polyclonal CPM antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human Carboxypeptidase M aa 200-250 conjugated to Keyhole Limpet Haemocyanin.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:WB, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human Carboxypeptidase M aa 200-250 conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.P14384

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.4Preservative: 0.09% Sodium azideConstituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Carboxypeptidase M (CPM) is an enzyme that cleaves C-terminal basic residues from peptides and proteins. Also known as carboxypeptidase M1 CPM has a molecular weight of approximately 50 kDa. It is expressed on the surface of various cell types such as macrophages epithelial cells and specific tumor cells. CPM functions optimally at physiological pH and high levels of expression are seen in the lung placenta and kidney tissues. This broad expression pattern suggests that CPM plays significant roles in diverse physiological contexts.
Biological function summary
CPM is involved in peptide processing and degradation contributing to the regulation of hormonal and neurotransmitter peptides. As part of a larger proteolytic system CPM modifies the activity and half-life of bioactive peptides by removing terminal residues. Its activity influences the regulation of peptide signaling pathways. In such roles it resounds in processes like local inflammatory response and modulation of cell surface receptors. CPM’s enzymatic activity ensures the proper function of the physiological regulatory mechanisms where peptidase activity is required.
Pathways
CPM is instrumental in the kallikrein-kinin and complement pathways. In the kallikrein-kinin system CPM regulates kinin levels influencing blood pressure and inflammation. It also relates to the complement system interacting with components that participate in immune responses. CPM’s function closely links to other carboxypeptidases in these pathways enhancing its role in regulating peptide effects or degradation. Its enzymatic interactions can influence the outcomes of these pathways ensuring an adequate biological response.
CPM has associations with conditions like hypertension and chronic inflammation. Its influence on the kallikrein-kinin system corresponds to implications for blood pressure regulation connecting CPM to pathways affecting hypertension. In chronic inflammatory conditions CPM affects the local inflammatory response by modulating active peptide levels. Related proteins like carboxypeptidase N and other members of the metallocarboxypeptidase family augment this functional network highlighting CPM’s relevance in managing peptide-mediated pathological processes.