epitope corresponding to amino acids 285-429 mapping at the C-terminus of CPM of human origin
Modification Notes
Carboxypeptidase M (CPM) is a 443 amino acid protein belonging to the metallo-carboxypeptidase (metallo-CP) family. Localized to the cell membrane, CPM contains hydrophobic regions in the N and C- termini and has six potential asparagine-linked glycosylation sites. Functionally, CPM specifically removes C-terminal basic amino acids (arginine or lysine) from proteins and polypeptides and is believed to play a role in monocyte to macrophage differentiation. CPM is also thought to play an important role in the control of peptide hormone and growth factor activity at the cell surface, as well as in the membrane-localized degradation of extracellular proteins. Three isoforms of this protein exist as a result of alternative splicing events.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of CPM of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine and canine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 285-429 mapping at the C-terminus of CPM of human origin
Tissue Specificity
epitope corresponding to amino acids 285-429 mapping at the C-terminus of CPM of human origin
Western blot analysis of CPM expression in BJAB whole cell lysate.
Application Notes
recommended for detection of CPM of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine and canine:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.