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Azurocidin (Cationic antimicrobial protein CAP37) (Heparin-binding protein) (HBP) (hHBP)

 CAP7_HUMAN              Reviewed;         251 AA.
P20160; P80014; Q52LG4; Q9UCM1; Q9UCT5;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 3.
28-FEB-2018, entry version 181.
RecName: Full=Azurocidin {ECO:0000303|PubMed:2501794};
AltName: Full=Cationic antimicrobial protein CAP37 {ECO:0000303|PubMed:2226832};
AltName: Full=Heparin-binding protein {ECO:0000303|PubMed:2026172};
Short=HBP {ECO:0000303|PubMed:2026172};
Short=hHBP {ECO:0000303|PubMed:2026172};
Flags: Precursor;
Name=AZU1 {ECO:0000312|HGNC:HGNC:913};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1919011;
Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K.,
Guerra M.E., Larrick J.L.;
"Cloning of the cDNA for the serine protease homolog CAP37/azurocidin,
a microbicidal and chemotactic protein from human granulocytes.";
J. Immunol. 147:3210-3214(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [MRNA] OF 3-251.
TISSUE=Neutrophil;
PubMed=2049091; DOI=10.1016/0006-291X(91)91843-2;
Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.;
"Complementary DNA sequence of human neutrophil azurocidin, an
antibiotic with extensive homology to serine proteases.";
Biochem. Biophys. Res. Commun. 177:688-695(1991).
[6]
PROTEIN SEQUENCE OF 27-248.
PubMed=2226832; DOI=10.1016/0014-5793(90)80484-Z;
Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.;
"Amino acid sequence of CAP37, a human neutrophil granule-derived
antibacterial and monocyte-specific chemotactic glycoprotein
structurally similar to neutrophil elastase.";
FEBS Lett. 272:200-204(1990).
[7]
PROTEIN SEQUENCE OF 27-248.
TISSUE=Neutrophil;
PubMed=2026172; DOI=10.1111/j.1432-1033.1991.tb15942.x;
Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J.,
Engels M., Wollmer A.;
"Covalent structure of two novel neutrophile leucocyte-derived
proteins of porcine and human origin. Neutrophile elastase homologues
with strong monocyte and fibroblast chemotactic activities.";
Eur. J. Biochem. 197:535-547(1991).
[8]
PROTEIN SEQUENCE OF 27-68.
TISSUE=Neutrophil;
PubMed=2332502; DOI=10.1172/JCI114593;
Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.;
"CAP37, a human neutrophil-derived chemotactic factor with monocyte
specific activity.";
J. Clin. Invest. 85:1468-1476(1990).
[9]
PROTEIN SEQUENCE OF 27-67.
TISSUE=Neutrophil;
PubMed=2406527; DOI=10.1016/0024-3205(90)90104-Y;
Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J.,
Palings I., Larrick J.W.;
"CAP 37, a 37 kD human neutrophil granule cationic protein shares
homology with inflammatory proteinases.";
Life Sci. 46:189-196(1990).
[10]
PROTEIN SEQUENCE OF 27-48, AND FUNCTION.
TISSUE=Leukocyte;
PubMed=1937776;
Wasiluk K.R., Skubitz K.M., Gray B.H.;
"Comparison of granule proteins from human polymorphonuclear
leukocytes which are bactericidal toward Pseudomonas aeruginosa.";
Infect. Immun. 59:4193-4200(1991).
[11]
PROTEIN SEQUENCE OF 27-47.
PubMed=1897955; DOI=10.1016/0003-9861(91)90042-H;
Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W.,
Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S.,
Walakovits L., Knight W.B.;
"PMN elastases: a comparison of the specificity of human isozymes and
the enzyme from other species toward substrates and inhibitors.";
Arch. Biochem. Biophys. 286:284-292(1991).
[12]
PROTEIN SEQUENCE OF 27-46, AND SUBCELLULAR LOCATION.
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).
[13]
PROTEIN SEQUENCE OF 27-46 AND 194-217.
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 27-46, AND FUNCTION.
PubMed=1399008;
Miyasaki K.T., Bodeau A.L.;
"Human neutrophil azurocidin synergizes with leukocyte elastase and
cathepsin G in the killing of Capnocytophaga sputigena.";
Infect. Immun. 60:4973-4975(1992).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=2312733; DOI=10.1172/JCI114518;
Campanelli D., Detmers P.A., Nathan C.F., Gabay J.E.;
"Azurocidin and a homologous serine protease from neutrophils.
Differential antimicrobial and proteolytic properties.";
J. Clin. Invest. 85:904-915(1990).
[16]
REVIEW.
PubMed=1755383;
Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K.,
Larrick J.W.;
"Human neutrophil granule cationic protein CAP37 is a specific
macrophage chemotaxin that shares homology with inflammatory
proteinases.";
Adv. Exp. Med. Biol. 305:89-96(1991).
[17]
SYNTHESIS OF 46-70, MUTAGENESIS OF CYS-52 AND CYS-68, AND REGION.
PubMed=8506327; DOI=10.1073/pnas.90.10.4733;
Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.;
"Synthetic bactericidal peptide based on CAP37: a 37-kDa human
neutrophil granule-associated cationic antimicrobial protein
chemotactic for monocytes.";
Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993).
[18]
PROPEPTIDE CLEAVAGE.
PubMed=10534120;
Lindmark A., Garwicz D., Rasmussen P.B., Flodgaard H., Gullberg U.;
"Characterization of the biosynthesis, processing, and sorting of
human HBP/CAP37/azurocidin.";
J. Leukoc. Biol. 66:634-643(1999).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-140 AND ASN-171.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[20]
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).
[21]
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).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=9095193; DOI=10.1038/nsb0497-265;
Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C.,
Flodgaard H.J., Larsen I.K.;
"Structure of HBP, a multifunctional protein with a serine proteinase
fold.";
Nat. Struct. Biol. 4:265-268(1997).
[23]
X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=9761855; DOI=10.1107/S0907444997016193;
Karlsen S., Iversen L.F., Larsen I.K., Flodgaard H.J., Kastrup J.S.;
"Atomic resolution structure of human HBP/CAP37/azurocidin.";
Acta Crystallogr. D 54:598-609(1998).
-!- FUNCTION: This is a neutrophil granule-derived antibacterial and
monocyte- and fibroblast-specific chemotactic glycoprotein. Binds
heparin. The cytotoxic action is limited to many species of Gram-
negative bacteria; this specificity may be explained by a strong
affinity of the very basic N-terminal half for the negatively
charged lipopolysaccharides that are unique to the Gram-negative
bacterial outer envelope. It may play a role in mediating
recruitment of monocytes in the second wave of inflammation. Has
antibacterial activity against the Gram-nagative bacterium
P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.
Acting alone, it does not have antimicrobial activity against the
Gram-negative bacteria A.actinomycetemcomitans ATCC 29532,
A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4,
H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC
33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872
or E.coli ML-35. Has antibacterial activity against C.sputigena
ATCC 33123 when acting synergistically with either elastase or
cathepsin G. {ECO:0000269|PubMed:1399008,
ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2312733}.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
{ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794};
Peripheral membrane protein {ECO:0000269|PubMed:2312733};
Cytoplasmic side {ECO:0000269|PubMed:2312733}. Note=Localizes to
azurophil granules of neutrophil granulocytes. Also called primary
granules, these specialized lysosomes of the neutrophil formed
early during promyelocyte development store antibacterial proteins
and peptides. {ECO:0000269|PubMed:2312733,
ECO:0000269|PubMed:2501794}.
-!- PTM: Cleavage of the N-terminal propeptide which is composed of 7
amino acids occurs in two steps. The initial cleavage of 5 amino
acids is followed by the cleavage of a dipeptide to produce the
mature form. {ECO:0000269|PubMed:10534120}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Elastase
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M96326; AAB59353.1; -; Genomic_DNA.
EMBL; AC004799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069495; AAH69495.1; -; mRNA.
EMBL; BC093931; AAH93931.1; -; mRNA.
EMBL; BC093933; AAH93933.1; -; mRNA.
EMBL; X58794; CAA41601.1; -; mRNA.
CCDS; CCDS12044.1; -.
PIR; A46268; TRHUAZ.
RefSeq; NP_001691.1; NM_001700.4.
UniGene; Hs.72885; -.
PDB; 1A7S; X-ray; 1.12 A; A=27-251.
PDB; 1AE5; X-ray; 2.30 A; A=27-251.
PDB; 1FY1; X-ray; 2.50 A; A=27-251.
PDB; 1FY3; X-ray; 1.89 A; A=27-251.
PDBsum; 1A7S; -.
PDBsum; 1AE5; -.
PDBsum; 1FY1; -.
PDBsum; 1FY3; -.
ProteinModelPortal; P20160; -.
SMR; P20160; -.
BioGrid; 107043; 14.
IntAct; P20160; 2.
MINT; P20160; -.
STRING; 9606.ENSP00000233997; -.
MEROPS; S01.971; -.
iPTMnet; P20160; -.
BioMuta; AZU1; -.
DMDM; 416746; -.
EPD; P20160; -.
PaxDb; P20160; -.
PeptideAtlas; P20160; -.
PRIDE; P20160; -.
DNASU; 566; -.
Ensembl; ENST00000233997; ENSP00000233997; ENSG00000172232.
Ensembl; ENST00000620695; ENSP00000479183; ENSG00000278624.
GeneID; 566; -.
KEGG; hsa:566; -.
UCSC; uc002lpz.2; human.
CTD; 566; -.
DisGeNET; 566; -.
EuPathDB; HostDB:ENSG00000172232.9; -.
GeneCards; AZU1; -.
HGNC; HGNC:913; AZU1.
HPA; HPA055851; -.
MIM; 162815; gene.
neXtProt; NX_P20160; -.
OpenTargets; ENSG00000172232; -.
PharmGKB; PA25206; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00910000144219; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P20160; -.
OMA; ASIQNQG; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P20160; -.
TreeFam; TF335284; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P20160; -.
GeneWiki; Azurocidin_1; -.
GenomeRNAi; 566; -.
PRO; PR:P20160; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000172232; -.
CleanEx; HS_AZU1; -.
ExpressionAtlas; P20160; baseline and differential.
Genevisible; P20160; HS.
GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0035577; C:azurophil granule membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IMP:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0015643; F:toxic substance binding; NAS:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; IMP:UniProtKB.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0045123; P:cellular extravasation; NAS:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0008347; P:glial cell migration; IDA:UniProtKB.
GO; GO:0050930; P:induction of positive chemotaxis; NAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
GO; GO:0048246; P:macrophage chemotaxis; NAS:UniProtKB.
GO; GO:0001774; P:microglial cell activation; IEP:UniProtKB.
GO; GO:0042117; P:monocyte activation; TAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070944; P:neutrophil mediated killing of bacterium; IDA:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0050754; P:positive regulation of fractalkine biosynthetic process; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IDA:UniProtKB.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEP:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IDA:UniProtKB.
GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0043114; P:regulation of vascular permeability; NAS:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial; Chemotaxis;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Heparin-binding; Membrane; Reference proteome;
Serine protease homolog; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:10534120}.
PROPEP 20 26 Removed in mature form.
{ECO:0000269|PubMed:10534120,
ECO:0000269|PubMed:1399008,
ECO:0000269|PubMed:1897955,
ECO:0000269|PubMed:1937776,
ECO:0000269|PubMed:2026172,
ECO:0000269|PubMed:2226832,
ECO:0000269|PubMed:2332502,
ECO:0000269|PubMed:2404977,
ECO:0000269|PubMed:2406527,
ECO:0000269|PubMed:2501794}.
/FTId=PRO_0000435372.
PROPEP 25 26 Dipeptide found in non-mature form.
{ECO:0000269|PubMed:10534120}.
/FTId=PRO_0000435373.
CHAIN 27 248 Azurocidin. {ECO:0000269|PubMed:2026172,
ECO:0000269|PubMed:2226832}.
/FTId=PRO_0000027705.
PROPEP 249 251 Removed in mature form.
{ECO:0000269|PubMed:2026172,
ECO:0000269|PubMed:2226832}.
/FTId=PRO_0000027706.
DOMAIN 27 244 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 46 70 Possesses antibiotic activity.
{ECO:0000269|PubMed:8506327}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2226832}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2226832}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2226832}.
DISULFID 52 68 {ECO:0000269|PubMed:9095193,
ECO:0000269|PubMed:9761855}.
DISULFID 149 207 {ECO:0000269|PubMed:9095193,
ECO:0000269|PubMed:9761855}.
DISULFID 180 186 {ECO:0000269|PubMed:9095193,
ECO:0000269|PubMed:9761855}.
DISULFID 197 222 {ECO:0000269|PubMed:9095193,
ECO:0000269|PubMed:9761855}.
MUTAGEN 52 52 C->S: Loss of antibiotic activity.
{ECO:0000269|PubMed:8506327}.
MUTAGEN 68 68 C->S: Loss of antibiotic activity.
{ECO:0000269|PubMed:8506327}.
CONFLICT 36 36 R -> H (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 130 130 S -> N (in Ref. 7; AA sequence).
{ECO:0000305}.
STRAND 41 46 {ECO:0000244|PDB:1A7S}.
STRAND 49 58 {ECO:0000244|PDB:1A7S}.
STRAND 61 64 {ECO:0000244|PDB:1A7S}.
HELIX 66 68 {ECO:0000244|PDB:1A7S}.
STRAND 76 82 {ECO:0000244|PDB:1A7S}.
TURN 91 93 {ECO:0000244|PDB:1A7S}.
STRAND 95 103 {ECO:0000244|PDB:1A7S}.
TURN 109 112 {ECO:0000244|PDB:1A7S}.
STRAND 117 123 {ECO:0000244|PDB:1A7S}.
STRAND 148 154 {ECO:0000244|PDB:1A7S}.
STRAND 157 160 {ECO:0000244|PDB:1FY1}.
STRAND 168 174 {ECO:0000244|PDB:1A7S}.
HELIX 177 179 {ECO:0000244|PDB:1A7S}.
STRAND 184 188 {ECO:0000244|PDB:1A7S}.
STRAND 190 193 {ECO:0000244|PDB:1A7S}.
STRAND 204 207 {ECO:0000244|PDB:1A7S}.
STRAND 210 218 {ECO:0000244|PDB:1A7S}.
STRAND 227 231 {ECO:0000244|PDB:1A7S}.
HELIX 232 235 {ECO:0000244|PDB:1A7S}.
HELIX 236 244 {ECO:0000244|PDB:1A7S}.
SEQUENCE 251 AA; 26886 MW; 22F80D9EBE87DE60 CRC64;
MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH FCGGALIHAR
FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS SMSENGYDPQ QNLNDLMLLQ
LDREANLTSS VTILPLPLQN ATVEAGTRCQ VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC
RPNNVCTGVL TRRGGICNGD GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID
GVLNNPGPGP A


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Catalog number Product name Quantity
U1461h CLIA AZU1,Azurocidin,Cationic antimicrobial protein CAP37,HBP,Heparin-binding protein,Homo sapiens,Human 96T
E1461h ELISA kit AZU1,Azurocidin,Cationic antimicrobial protein CAP37,HBP,Heparin-binding protein,Homo sapiens,Human 96T
E1461h ELISA AZU1,Azurocidin,Cationic antimicrobial protein CAP37,HBP,Heparin-binding protein,Homo sapiens,Human 96T
AZC15-N-50 Azurocidin, Human Neutrophil (CAP37, Cationic protein 37) 50 ug
AZC15-N-50 Azurocidin, Human Neutrophil (CAP37, Cationic protein 37) Species Reactivity: Human 50 ug Product tipe: Pure Protein
EIAAB05233 18 kDa cationic antimicrobial protein,CAMP,CAP18,CAP-18,Cathelicidin antimicrobial peptide,FALL39,hCAP-18,Homo sapiens,HSD26,Human
EIAAB05283 18 kDa cationic protein,18 kDa lipopolysaccharide-binding protein,Antimicrobial protein CAP18,CAP18,CAP18-A,Oryctolagus cuniculus,Rabbit
ER753 Azurocidin per Heparin Binding Protein Elisa Kit 96T
CSB-E09698h Human Azurocidin per Heparin Binding Protein(AZU per HBP) ELISA Kit 96T
7287-100 Azurocidin, Human Neutrophil (Cationic protein 37) 100 μg
101-M223 Azurocidin Anti-Human Host: Mouse AZU1; AZU; HBP; NAZC; AZAMP; CAP37; HUMAZUR 100
101-M223 Azurocidin, Host: Mouse, Species: Anti-Human, Synonyms: AZU1; AZU; HBP; NAZC; AZAMP; CAP37; HUMAZUR 100 ug
orb82271 Human Azurocidin protein Azurocidin is a purified autoimmune reagent. For research use only. 0.2 mg
orb82605 Murine BD2 protein Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are 5
E1309h ELISA HBBM,HB-GAM,HBGF-8,HBNF1,HBNF-1,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neurite outgrowth-promoting factor 1,Homo 96T
U1309h CLIA HBBM,HB-GAM,HBGF-8,HBNF1,HBNF-1,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neurite outgrowth-promoting factor 1,Homo 96T
U1309m CLIA HBBM,HB-GAM,HBGF-8,HBNF,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neutrophic factor,Mouse,Mus musculus,OSF-1,Osteobl 96T
U1309b CLIA Bos taurus,Bovine,HBBM,HB-GAM,HBGF-8,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neurite-promoting factor,p18,Pleiotro 96T
E1309h ELISA kit HBBM,HB-GAM,HBGF-8,HBNF1,HBNF-1,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neurite outgrowth-promoting factor 1 96T
E1309m ELISA HBBM,HB-GAM,HBGF-8,HBNF,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neutrophic factor,Mouse,Mus musculus,OSF-1,Osteob 96T
E1309r ELISA HBBM,HB-GAM,HBGF-8,HBNF,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neutrophic factor,OSF-1,Osteoblast-specific facto 96T
E1309b ELISA Bos taurus,Bovine,HBBM,HB-GAM,HBGF-8,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neurite-promoting factor,p18,Pleiotr 96T
EIAAB34981 60S ribosomal protein L22,EAP,EBER-associated protein,Epstein-Barr virus small RNA-associated protein,Heparin-binding protein HBp15,Homo sapiens,Human,RPL22
E1309m ELISA kit HBBM,HB-GAM,HBGF-8,HBNF,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neutrophic factor,Mouse,Mus musculus,OSF-1,O 96T
E1309r ELISA kit HBBM,HB-GAM,HBGF-8,HBNF,Heparin-binding brain mitogen,Heparin-binding growth factor 8,Heparin-binding growth-associated molecule,Heparin-binding neutrophic factor,OSF-1,Osteoblast-specific 96T


 

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