CPZ Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, E |
---|---|
Primary Accession | Q66K79 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 73655 Da |
Antigen Region | 143-172 aa |
Gene ID | 8532 |
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Other Names | Carboxypeptidase Z, CPZ, 3417-, CPZ |
Target/Specificity | This CPZ antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 143-172 amino acids from the N-terminal region of human CPZ. |
Dilution | WB~~1:1000 IHC-P~~1:50~100 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | CPZ Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CPZ |
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Function | Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing. |
Cellular Location | Secreted, extracellular space, extracellular matrix |
Tissue Location | In placenta, it is present within invasive trophoblasts and in the surrounding extracellular space. Also present in amnion cells, but is not readily apparent in the extracellular matrix of this cell type. Present in normal pituitary gland and neoplastic pituitary gland (especially POMC-, GH- and PRL-producing adenomas) (at protein level). Widely expressed |
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Provided below are standard protocols that you may find useful for product applications.
Background
CPZ is a member of the metallocarboxypeptidase family. This enzyme displays carboxypeptidase activity towards substrates with basic C-terminal residues. It is most active at neutral pH and is inhibited by active site-directed inhibitors of metallocarboxypeptidases.
References
Fan,X., J. Histochem. Cytochem. 50 (11), 1509-1516 (2002)
Reznik,S.E., Cell. Mol. Life Sci. 58 (12-13), 1790-1804 (2001)
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