Xpnpep1 Mouse Monoclonal Antibody [Clone ID: JG12C9C10]

Specifications

Product Data
Clone Name	JG12C9C10
Applications	IF, IHC
Recommend Dilution	Immunohistochemistry on Frozen and Paraffin Sections.
Reactivity	Rat
Host	Mouse
Clonality	Monoclonal
Immunogen	Membrane protein fraction of solated Rat glomeruli
Specificity	This antibody recognizes Rat Aminopeptidase P. Other species not tested.
Formulation	PBS pH 6.0 State: Purified State: Lyophilized purified IgG fraction from Cell Culture Supernatant Stabilizer: None
Reconstitution Method	Restore in sterile water to a concentration of 0.1-1.0 mg/ml. Centrifuge vial prior to opening.
Purification	Protein G Chromatography
Conjugation	Unconjugated
Storage Condition	Store lyophilized at 2-8°C for 6 months or at -20°C long term. After reconstitution store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C long term. Avoid repeated freezing and thawing.
Gene Name	X-prolyl aminopeptidase (aminopeptidase P) 1, soluble
Database Link	Entrez Gene 170751 Rat UniProt ID O54975
Background	Aminopeptidase P (AP-P; X-Pro aminopeptidase) has the unique ability to leave the N-terminal amino acid residue from peptides having proline as the penultimate amino acid residue. Biologically active peptides comprise an important and diverse class of extracellular chemical messengers that mediate a wide range of intercellular interactions. Several bioactive peptides including hormones, neuropeptides, neurotransmitters escape non-specific protease degradation by having an Xaa-Pro motif at their amino termini. Due to its cyclic nature, proline confers resistance to such peptide bonds so that aminopeptidases with broad specificity cannot act upon such peptides. There are a limited number of peptidases that act on peptide bonds involving a proline residue, such as dipeptidyl peptidase II (DPPII) and dipeptidyl peptidase W (DPPIV), and prolidase (which cleaves the Xaa-Pro bond only in dipeptides), or endopeptidases such as prolyl endopeptidase (which cleaves on the carbonyl side of proline residues within a protein or peptide). However, none of these enzymes have been reported to hydrolyze Xaa-Pro bonds located at the N-terminus of peptides and proteins. Therefore, role of AP-P is crucial in this respect. AP-P activity is ubiquitous and has been found in a wide range of organisms including bacteria, yeast and vertebrates. Mammalian AP-Ps exist in membrane-bound and cytosolic forms, which represent two distinct gene products. The cytosolic (soluble) form of aminopeptidase P is found in human leukocytes and rat brain.
Synonyms	XPNPEPL, XPNPEPL1
Reference Data

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