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Myeloblastin (EC 3.4.21.76) (AGP7) (C-ANCA antigen) (Leukocyte proteinase 3) (PR-3) (PR3) (Neutrophil proteinase 4) (NP-4) (P29) (Wegener autoantigen)

 PRTN3_HUMAN             Reviewed;         256 AA.
P24158; P15637; P18078; Q4VB08; Q4VB09; Q6LBM7; Q6LBN2; Q9UD25;
Q9UQD8;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 3.
22-NOV-2017, entry version 191.
RecName: Full=Myeloblastin;
EC=3.4.21.76;
AltName: Full=AGP7;
AltName: Full=C-ANCA antigen;
AltName: Full=Leukocyte proteinase 3;
Short=PR-3;
Short=PR3;
AltName: Full=Neutrophil proteinase 4;
Short=NP-4;
AltName: Full=P29;
AltName: Full=Wegener autoantigen;
Flags: Precursor;
Name=PRTN3; Synonyms=MBN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-119; THR-135 AND SER-136.
PubMed=1681549; DOI=10.1073/pnas.88.20.9253;
Labbaye C., Musette P., Cayre Y.E.;
"Wegener autoantigen and myeloblastin are encoded by a single mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 88:9253-9256(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-119.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-119.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 AND 22-256.
PubMed=1518849; DOI=10.1073/pnas.89.17.8215;
Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P.,
Jenne D.E.;
"Three human elastase-like genes coordinately expressed in the
myelomonocyte lineage are organized as a single genetic locus on
19pter.";
Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-254, AND VARIANTS THR-135 AND
SER-136.
PubMed=1400430;
Sturrock A.B., Franklin K.F., Rao G., Marshall B.C., Rebentisch M.B.,
Lemons R.S., Hoidal J.R.;
"Structure, chromosomal assignment, and expression of the gene for
proteinase-3. The Wegener's granulomatosis autoantigen.";
J. Biol. Chem. 267:21193-21199(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200, AND VARIANT ILE-119.
PubMed=9924693;
Clave E., Molldrem J., Hensel N., Raptis A., Barrett A.J.;
"Donor-recipient polymorphism of the proteinase 3 gene: a potential
target for T-cell alloresponses to myeloid leukemia.";
J. Immunother. 22:1-6(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-42.
PubMed=2001463;
Musette P., Labbaye C., Dorner M.H., Cayre Y.E., Casanova J.-L.,
Kourilsky P.;
"Wegener's autoantigen and leukemia.";
Blood 77:1398-1399(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-256, AND PROTEIN SEQUENCE OF 28-71;
156-181 AND 196-219.
PubMed=2258701; DOI=10.1084/jem.172.6.1709;
Campanelli D., Melchior M., Fu Y., Nakata M., Shuman H., Nathan C.,
Gabay J.E.;
"Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and
autoantigen from human neutrophils.";
J. Exp. Med. 172:1709-1715(1990).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, AND VARIANTS ILE-119; THR-135
AND SER-136.
PubMed=2598267; DOI=10.1016/0092-8674(89)90752-6;
Bories D., Raynal M.-C., Solomon D.H., Darzynkiewicz Z., Cayre Y.E.;
"Down-regulation of a serine protease, myeloblastin, causes growth
arrest and differentiation of promyelocytic leukemia cells.";
Cell 59:959-968(1989).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, PROTEIN SEQUENCE OF 28-48,
VARIANTS ILE-119; THR-135 AND SER-136, AND IDENTITY OF WEGENER'S
AUTOANTIGEN WITH PR-3.
PubMed=2377228; DOI=10.1038/346520a0;
Jenne D.E., Tschopp J., Luedemann J., Utecht B., Gross W.L.;
"Wegener's autoantigen decoded.";
Nature 346:520-520(1990).
[12]
PROTEIN SEQUENCE OF 28-67 AND 228-244.
PubMed=2033050;
Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H.,
Hoidal J.R.;
"Characterization of proteinase-3 (PR-3), a neutrophil serine
proteinase. Structural and functional properties.";
J. Biol. Chem. 266:9540-9548(1991).
[13]
PROTEIN SEQUENCE OF 28-47 AND 196-219.
PubMed=2404977;
Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.;
"Characterization of two azurphil granule proteases with active-site
homology to neutrophil elastase.";
J. Biol. Chem. 265:2038-2041(1990).
[14]
PROTEIN SEQUENCE OF 28-52.
PubMed=2121162;
Ohlsson K., Linder C., Rosengren M.;
"Monoclonal antibodies specific for neutrophil proteinase 4.
Production and use for isolation of the enzyme.";
Biol. Chem. Hoppe-Seyler 371:549-555(1990).
[15]
PROTEIN SEQUENCE OF 28-48.
PubMed=2285532;
Goldschmeding R., Dolman K.M., van den Ende M.E.,
van der Meer-Gerritsen C.H., Sonnenberg A., von dem Borne A.E.;
"The relation of 29 kD C-ANCA antigen to proteinase 3.";
APMIS Suppl. 19:26-27(1990).
[16]
PROTEIN SEQUENCE OF 28-47.
PubMed=2679910;
Niles J.L., McCluskey R.T., Ahmad M.F., Arnaout M.A.;
"Wegener's granulomatosis autoantigen is a novel neutrophil serine
proteinase.";
Blood 74:1888-1893(1989).
[17]
PROTEIN SEQUENCE OF 28-47.
PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
Marra M.N., Seeger M., Nathan C.F.;
"Antibiotic proteins of human polymorphonuclear leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
[18]
PROTEIN SEQUENCE OF 28-47, AND CATALYTIC ACTIVITY.
TISSUE=Neutrophil;
PubMed=7897245; DOI=10.1016/0022-1759(94)00295-8;
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.;
"Use of proteinase 3 purified by reverse phase HPLC to detect
autoantibodies in systemic vasculitis.";
J. Immunol. Methods 180:25-33(1995).
[19]
PROTEIN SEQUENCE OF 28-43.
PubMed=1688612; DOI=10.1084/jem.171.1.357;
Ludemann J., Utecht B., Gross W.L.;
"Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis
recognize an elastinolytic enzyme.";
J. Exp. Med. 171:357-362(1990).
[20]
PROTEIN SEQUENCE OF 110-121, AND VARIANT ILE-119.
TISSUE=Serum;
PubMed=7539799; DOI=10.1074/jbc.270.23.14107;
Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.;
"A novel form of dipeptidylpeptidase IV found in human serum.
Isolation, characterization, and comparison with T lymphocyte membrane
dipeptidylpeptidase IV (CD26).";
J. Biol. Chem. 270:14107-14114(1995).
[21]
IDENTITY OF WEGENER'S AUTOANTIGEN WITH PROTEINASE 3.
PubMed=2242436;
Gupta S.K., Niles J.L., McCluskey R.T., Arnaout M.A.;
"Identity of Wegener's autoantigen (p29) with proteinase 3 and
myeloblastin.";
Blood 76:2162-2162(1990).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=8757293; DOI=10.1006/jmbi.1996.0458;
Fujinaga M., Charnaia M.M., Halenbeck R., Koths K., James M.N.G.;
"The crystal structure of PR3, a neutrophil serine proteinase antigen
of Wegener's granulomatosis antibodies.";
J. Mol. Biol. 261:267-278(1996).
-!- FUNCTION: Polymorphonuclear leukocyte serine protease that
degrades elastin, fibronectin, laminin, vitronectin, and collagen
types I, III, and IV (in vitro) and causes emphysema when
administered by tracheal insufflation to hamsters.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins, including elastin, by
preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.
{ECO:0000269|PubMed:7897245}.
-!- INTERACTION:
P24001-4:IL32; NbExp=3; IntAct=EBI-465028, EBI-15570379;
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=AAA36342.1; Type=Frameshift; Positions=34, 39; Evidence={ECO:0000305};
Sequence=CAA39598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Proteinase 3 entry;
URL="https://en.wikipedia.org/wiki/Proteinase_3";
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EMBL; M75154; AAA59558.1; -; mRNA.
EMBL; AC004799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69591.1; -; Genomic_DNA.
EMBL; BC096183; AAH96183.1; -; mRNA.
EMBL; BC096184; AAH96184.1; -; mRNA.
EMBL; BC096185; AAH96185.1; -; mRNA.
EMBL; BC096186; AAH96186.1; -; mRNA.
EMBL; M96628; AAB59364.1; -; Genomic_DNA.
EMBL; AH005293; AAB59493.1; -; Genomic_DNA.
EMBL; M97911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AH007523; AAD21524.1; -; Genomic_DNA.
EMBL; X56606; CAA39943.1; -; mRNA.
EMBL; X55668; CAA39203.1; -; mRNA.
EMBL; M29142; AAA36342.1; ALT_FRAME; mRNA.
EMBL; X56132; CAA39597.1; -; mRNA.
EMBL; X56132; CAA39598.1; ALT_INIT; mRNA.
CCDS; CCDS32860.1; -.
PIR; A45080; PRHU3.
RefSeq; NP_002768.3; NM_002777.3.
UniGene; Hs.928; -.
PDB; 1FUJ; X-ray; 2.20 A; A/B/C/D=28-248.
PDBsum; 1FUJ; -.
ProteinModelPortal; P24158; -.
SMR; P24158; -.
BioGrid; 111638; 15.
DIP; DIP-31107N; -.
IntAct; P24158; 3.
MINT; MINT-4054660; -.
STRING; 9606.ENSP00000234347; -.
BindingDB; P24158; -.
ChEMBL; CHEMBL3900; -.
DrugBank; DB05161; Elafin.
GuidetoPHARMACOLOGY; 2401; -.
MEROPS; S01.134; -.
BioMuta; PRTN3; -.
DMDM; 6174926; -.
EPD; P24158; -.
PaxDb; P24158; -.
PeptideAtlas; P24158; -.
PRIDE; P24158; -.
DNASU; 5657; -.
Ensembl; ENST00000234347; ENSP00000234347; ENSG00000196415.
Ensembl; ENST00000612112; ENSP00000478977; ENSG00000277804.
GeneID; 5657; -.
KEGG; hsa:5657; -.
UCSC; uc002lqa.2; human.
CTD; 5657; -.
DisGeNET; 5657; -.
EuPathDB; HostDB:ENSG00000196415.9; -.
GeneCards; PRTN3; -.
HGNC; HGNC:9495; PRTN3.
HPA; CAB017558; -.
HPA; HPA005938; -.
MalaCards; PRTN3; -.
MIM; 177020; gene.
neXtProt; NX_P24158; -.
OpenTargets; ENSG00000196415; -.
Orphanet; 900; Granulomatosis with polyangiitis.
PharmGKB; PA33842; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00900000140962; -.
HOVERGEN; HBG013304; -.
InParanoid; P24158; -.
KO; K01350; -.
OMA; PGSHFCG; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P24158; -.
TreeFam; TF335284; -.
BRENDA; 3.4.21.76; 2681.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-449836; Other interleukin signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6803157; Antimicrobial peptides.
EvolutionaryTrace; P24158; -.
GeneWiki; Proteinase_3; -.
GenomeRNAi; 5657; -.
PRO; PR:P24158; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000196415; -.
CleanEx; HS_PRTN3; -.
ExpressionAtlas; P24158; baseline and differential.
Genevisible; P24158; HS.
GO; GO:0035578; C:azurophil granule lumen; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0097029; P:mature conventional dendritic cell differentiation; IDA:UniProtKB.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:UniProtKB.
GO; GO:0050765; P:negative regulation of phagocytosis; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Collagen degradation; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Polymorphism; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 25
PROPEP 26 27
/FTId=PRO_0000027707.
CHAIN 28 248 Myeloblastin.
/FTId=PRO_0000027708.
PROPEP 249 256
/FTId=PRO_0000027709.
DOMAIN 28 248 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 71 71 Charge relay system.
ACT_SITE 118 118 Charge relay system.
ACT_SITE 203 203 Charge relay system.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
DISULFID 56 72
DISULFID 152 209
DISULFID 182 188
DISULFID 199 224
VARIANT 119 119 V -> I (in dbSNP:rs351111).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1681549,
ECO:0000269|PubMed:2377228,
ECO:0000269|PubMed:2598267,
ECO:0000269|PubMed:7539799,
ECO:0000269|PubMed:9924693,
ECO:0000269|Ref.3}.
/FTId=VAR_011691.
VARIANT 135 135 A -> T (in dbSNP:rs1042281).
{ECO:0000269|PubMed:1400430,
ECO:0000269|PubMed:1681549,
ECO:0000269|PubMed:2377228,
ECO:0000269|PubMed:2598267}.
/FTId=VAR_011713.
VARIANT 136 136 T -> S (in dbSNP:rs1042282).
{ECO:0000269|PubMed:1400430,
ECO:0000269|PubMed:1681549,
ECO:0000269|PubMed:2377228,
ECO:0000269|PubMed:2598267}.
/FTId=VAR_011714.
CONFLICT 2 2 A -> R (in Ref. 9; CAA39203).
{ECO:0000305}.
CONFLICT 38 38 S -> I (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 40 40 P -> PI (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 46 46 Q -> E (in Ref. 13; AA sequence and 17;
AA sequence). {ECO:0000305}.
CONFLICT 48 48 R -> A (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 64 64 S -> D (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 70 70 A -> P (in Ref. 1; AAA59558).
{ECO:0000305}.
CONFLICT 255 255 Missing (in Ref. 9; CAA39203).
{ECO:0000305}.
STRAND 42 47 {ECO:0000244|PDB:1FUJ}.
STRAND 56 62 {ECO:0000244|PDB:1FUJ}.
STRAND 65 68 {ECO:0000244|PDB:1FUJ}.
HELIX 70 73 {ECO:0000244|PDB:1FUJ}.
STRAND 74 76 {ECO:0000244|PDB:1FUJ}.
HELIX 78 80 {ECO:0000244|PDB:1FUJ}.
STRAND 81 86 {ECO:0000244|PDB:1FUJ}.
STRAND 98 107 {ECO:0000244|PDB:1FUJ}.
TURN 112 115 {ECO:0000244|PDB:1FUJ}.
STRAND 120 126 {ECO:0000244|PDB:1FUJ}.
STRAND 151 160 {ECO:0000244|PDB:1FUJ}.
STRAND 162 164 {ECO:0000244|PDB:1FUJ}.
STRAND 171 178 {ECO:0000244|PDB:1FUJ}.
STRAND 186 190 {ECO:0000244|PDB:1FUJ}.
STRAND 192 195 {ECO:0000244|PDB:1FUJ}.
STRAND 206 209 {ECO:0000244|PDB:1FUJ}.
STRAND 212 219 {ECO:0000244|PDB:1FUJ}.
STRAND 221 223 {ECO:0000244|PDB:1FUJ}.
STRAND 227 229 {ECO:0000244|PDB:1FUJ}.
STRAND 231 235 {ECO:0000244|PDB:1FUJ}.
HELIX 236 239 {ECO:0000244|PDB:1FUJ}.
HELIX 240 247 {ECO:0000244|PDB:1FUJ}.
SEQUENCE 256 AA; 27807 MW; CBECA36D8C4B2A40 CRC64;
MAHRPPSPAL ASVLLALLLS GAARAAEIVG GHEAQPHSRP YMASLQMRGN PGSHFCGGTL
IHPSFVLTAA HCLRDIPQRL VNVVLGAHNV RTQEPTQQHF SVAQVFLNNY DAENKLNDVL
LIQLSSPANL SASVATVQLP QQDQPVPHGT QCLAMGWGRV GAHDPPAQVL QELNVTVVTF
FCRPHNICTF VPRRKAGICF GDSGGPLICD GIIQGIDSFV IWGCATRLFP DFFTRVALYV
DWIRSTLRRV EAKGRP


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497-50 Source Human Neutrophil PROTEINASE 3, Human (PR3) ANCA 1 mg
497-50 Source Human Neutrophil PROTEINASE 3, Human (PR3) ANCA 500 ug
EIAAB32679 Mouse,Mus musculus,Myeloblastin,PR-3,Proteinase 3,Prtn3
C628 Recombinant Human Proteinase 3 per PRTN3 per Myeloblastin (C-6His) 10ug
A3C192H Proteinase 3 Antigen (cANCA)Human Neutrophil Purified 0.2mg
A3C192H Proteinase 3 Antigen (cANCA) host: Human Neutrophil 0.2mg
497-52 Proteinase 3 (PR-3), Human - C-ANCA 50 ug
497-52 Proteinase 3 (PR-3), Human - C-ANCA 25 ug
497-52 Proteinase 3 (PR-3), Human - C-ANCA 100 ug
E1312h ELISA ALP,Antileukoproteinase,BLPI,Homo sapiens,Human,HUSI-1,MPI,Mucus proteinase inhibitor,Protease inhibitor WAP4,Secretory leukocyte protease inhibitor,Seminal proteinase inhibitor,SLPI,WAP four-di 96T
E1312h ELISA kit ALP,Antileukoproteinase,BLPI,Homo sapiens,Human,HUSI-1,MPI,Mucus proteinase inhibitor,Protease inhibitor WAP4,Secretory leukocyte protease inhibitor,Seminal proteinase inhibitor,SLPI,WAP fo 96T
U1312h CLIA ALP,Antileukoproteinase,BLPI,Homo sapiens,Human,HUSI-1,MPI,Mucus proteinase inhibitor,Protease inhibitor WAP4,Secretory leukocyte protease inhibitor,Seminal proteinase inhibitor,SLPI,WAP four-dis 96T
orb82012 Proteinase 3 Antigen (cANCA) Proteinase 3 Antigen (cANCA) is a purified autoimmune reagent. For research use only. 0.2 mg
497-52 PROTEINASE 3 (PR-3), Human - C-ANCA Liquid 50 ug
497-50 PROTEINASE 3 (PR3), Human - ANCA Liquid 100 ug
497-50 PROTEINASE 3 (PR3), Human - ANCA Liquid 1 mg
497-52 PROTEINASE 3 (PR-3), Human - C-ANCA Liquid 100 ug
497-52 PROTEINASE 3 (PR-3), Human - C-ANCA Liquid 25 ug
497-50 PROTEINASE 3 (PR3), Human - ANCA Liquid 10 ug
497-50 PROTEINASE 3 (PR3), Human - ANCA Liquid 25 ug
497-50 PROTEINASE 3 (PR3), Human - ANCA Liquid 500 ug


 

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