Anti-CPM Picoband Antibody
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Application
| WB |
|---|---|
| Primary Accession | P14384 |
| Host | Rabbit |
| Reactivity | Human |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Carboxypeptidase M(CPM) detection. Tested with WB in Human. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 1368 |
|---|---|
| Other Names | Carboxypeptidase M, CPM, 3.4.17.12, CPM |
| Calculated MW | 50514 Da |
| Application Details | Western blot, 0.1-0.5 µg/ml, Human |
| Subcellular Localization | Cell membrane ; Lipid-anchor, GPI-anchor . |
| Source | Eukaryota |
| Protein Name | Carboxypeptidase M |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of human CPM (286-316aa KYPREEKLPSFWNNNKASLIEYIKQVHLGVK), different from the related mouse sequence by two amino acids. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins. |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | CPM |
|---|---|
| Function | 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. |
| Cellular Location | Cell membrane; Lipid-anchor, GPI-anchor |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
CPM, mapped to 12q15, is known as Carboxypeptidase M. The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.
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