P0615
Proteinase 3 from human leukocytes
≥95% (PAGE)
Synonym(s):
AGP7, Myeloblastin, P29B, PR-3, PR3 Ag
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About This Item
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biological source
human leucocytes
assay
≥95% (PAGE)
form
solid
specific activity
≥25 units/mg protein
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... PRTN3(5657)
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General description
Proteinase 3 (PR3) is mapped to human chromosome 19p13.3.[1] Proteinase 3 is present majorly in azurophilic granules and belongs to neutrophil-derived proteases family.[2] PR3 is a peripheral membrane protein and lacks transmembrane domain. It comprises of an unique interfacial binding site (IBS) and two amino acid clusters, one charged and one hydrophobic, for membrane association.[3]
Proteinase 3 is found in high concentration in the primary granules of myeloid leukemia blasts. [4]
Application
Biochem/physiol Actions
Proteinase 3 (PR-3) is a serine protease expressed in the granules of neutrophils and monocytes. Also known as myeloblastin and p29b, it degrades elastin and is associated with myeloid leukemia and Wegener′s granulomatosis. [7]
Used for the detection of anti-PR3 auto-antibodies in immunoassays.
Unit Definition
One unit will hydrolyze 1 μmole of Boc-Ala-Ala-Nva-SBzl per minute at pH 7.5 at 25 deg C.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Genetics and pathophysiology of granulomatosis with polyangiitis (GPA) and its main autoantigen proteinase 3
Relle M, et al.
Molecular and Cellular Probes, 30(6), 366-373 (2016)
Proteinase 3 is a phosphatidylserine binding protein which affects the production and function of microvesicles
Martin KR, et al.
The Journal of biological chemistry, jbc-M115 (2016)
Y M van der Geld et al.
Journal of leukocyte biology, 69(2), 177-190 (2001-03-29)
Proteinase 3 (PR3) is one of four serine protease homologues in the azurophilic granules of neutrophils and granules of monocytes. It is of importance that anti-neutrophil cytoplasmic antibodies (ANCA) in patients with Wegener's granulomatosis (WG) are mainly directed against PR3
J Molldrem et al.
Blood, 88(7), 2450-2457 (1996-10-01)
Proteinase 3 is present in high concentration in the primary granules of acute and chronic myeloid leukemia blasts, and may represent a potential T-cell target antigen. We screened proteinase 3 against the binding motif of HLA-A2.1. Based on its high
R C Kao et al.
The Journal of clinical investigation, 82(6), 1963-1973 (1988-12-01)
Studies were designed to explore the possibility that human polymorphonuclear leukocyte granule constituents in addition to elastase (HLE) had the potential to cause emphysema. A two-step purification of three serine proteinases was developed. Granule extract proteins were initially separated by
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