AQPEP Antibody (C-Term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q6Q4G3 |
Reactivity | Human |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 113283 Da |
Gene ID | 206338 |
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Other Names | Aminopeptidase Q, AP-Q, 3411-, CHL2 antigen, Laeverin, AQPEP, LVRN |
Target/Specificity | This AQPEP antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 844-877 amino acids from human AQPEP. |
Dilution | WB~~1:2000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
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 | AQPEP Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | LVRN (HGNC:26904) |
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Function | Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys- LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. |
Cellular Location | Membrane; Single- pass type II membrane protein |
Tissue Location | Specifically expressed in placenta and not in other tissues. Mainly found at the cell surface region of the extravillous trophoblasts. Detected on extravillous trophoblasts in the outer layer of the chorion laeve in the fetal membrane Not detected on either fetal amnionic epithelial cells or maternal decidual cells. Also detected in the migrating extravillous trophoblasts in the maternal decidual tissues (at protein level). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.
References
Fujiwara H.,et al.Biochem. Biophys. Res. Commun. 313:962-968(2004).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Schmutz J.,et al.Nature 431:268-274(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Maruyama M.,et al.J. Biol. Chem. 282:20088-20096(2007).
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