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Aminopeptidase P is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. Zusätzlich bieten wir Ihnen X-Prolyl Aminopeptidase (Aminopeptidase P) 2, Membrane-Bound Proteine (4) und X-Prolyl Aminopeptidase (Aminopeptidase P) 2, Membrane-Bound Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal XPNPEP2 Primary Antibody für IHC, IHC (p) - ABIN4280378
Lindgren, Boström, Nilsson, Hansson, Sjölund, Möller, Jirström, Nilsson, Landberg, Axelson, Johansson: Isolation and characterization of progenitor-like cells from human renal proximal tubules. in The American journal of pathology 2011
The XPNPEP2 c-2399A and the ACE insertion/deletion polymorphisms analyzed in a population of patients with hereditary angioedema with F12 mutation were not a major determinant of disease expression.
we demonstrated that XPNPEP2 had significant effects on the metastasis of xenografted tumors in vivo. Collectively, our findings identify the novel function of XPNPEP2 in the metastasis of cervical cancer and suggest that XPNPEP2 could be a novel potential therapeutic target for the treatment of cervical cancer
A C-2399A SNP assay was applied to patients with acute hypotensive transfusion reactions. In a pilot study, 2 patients (50%) were found to possess C-2399A polymorphisms. One was found to be homozygous, and the other was heterozygous.
the genetic regulation of the XPNPEP2 gene and identify the genetic factors contributing to variance in plasma aminopeptidase P activity and ACEi-angioedema (XPNPEP2)
XPNPEP2 C-2399A polymorphism associates with angiotensin-converting enzyme inhibitor-associated angioedema in men but not women.
We found significantly decreased plasma aminopeptidase P activity (P=0.013) in hypersensitivity reactions (HSR+) subjects as well as altered degradation of endogenous des-Arginine(9)-bradykinin.
Increase in aminopeptidase P levels brought on by androgens could contribute to a more effective control of the kinin accumulation considered to be responsible for the symptoms of angioedema.
Structural comparisons suggest mechanisms for substrate selectivity in different X-prolyl peptidases.
females have polymorphisms associated with lower levels of APP & ACE; study suggests multiple genes may contribute to this disease
Aminopeptidase P is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. Structurally, the enzyme is a member of the 'pita bread fold' family and occurs in mammalian tissues in both soluble and GPI-anchored membrane-bound forms. A membrane-bound and soluble form of this enzyme have been identified as products of two separate genes.
X-Pro aminopeptidase 2
, aminoacylproline aminopeptidase
, membrane-bound APP
, membrane-bound AmP
, membrane-bound aminopeptidase P
, xaa-Pro aminopeptidase 2
, aminopeptidase P
, X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound
, X-prolyl aminopeptidase 2, membrane-bound
, xaa-Pro aminopeptidase 2-like