Rabbit Recombinant Monoclonal CPM antibody - conjugated to Alexa Fluor® 488.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
Carboxypeptidase M, CPM
Rabbit Recombinant Monoclonal CPM antibody - conjugated to Alexa Fluor® 488.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
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.
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.
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.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
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