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Antileukoproteinase (ALP) (BLPI) (HUSI-1) (Mucus proteinase inhibitor) (MPI) (Protease inhibitor WAP4) (Secretory leukocyte protease inhibitor) (Seminal proteinase inhibitor) (WAP four-disulfide core domain protein 4)

 SLPI_HUMAN              Reviewed;         132 AA.
P03973; B2R5H8; P07757;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
18-JUL-2018, entry version 187.
RecName: Full=Antileukoproteinase;
Short=ALP;
AltName: Full=BLPI;
AltName: Full=HUSI-1 {ECO:0000303|PubMed:3485543, ECO:0000303|PubMed:3533531};
AltName: Full=Mucus proteinase inhibitor;
Short=MPI;
AltName: Full=Protease inhibitor WAP4;
AltName: Full=Secretory leukocyte protease inhibitor {ECO:0000303|PubMed:3462719};
AltName: Full=Seminal proteinase inhibitor;
AltName: Full=WAP four-disulfide core domain protein 4;
Flags: Precursor;
Name=SLPI; Synonyms=WAP4, WFDC4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Cervix;
PubMed=3533531; DOI=10.1111/j.1432-1033.1986.tb09940.x;
Heinzel R., Appelhans H., Gassen G., Seemueller U., Machleidt W.,
Fritz H., Steffens G.;
"Molecular cloning and expression of cDNA for human antileukoprotease
from cervix uterus.";
Eur. J. Biochem. 160:61-67(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Parotid gland;
PubMed=3640338; DOI=10.1093/nar/14.20.7883;
Stetler G., Brewer M.T., Thompson R.C.;
"Isolation and sequence of a human gene encoding a potent inhibitor of
leukocyte proteases.";
Nucleic Acids Res. 14:7883-7896(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Intestine;
Si-Tahar M., Merlin D., Sitaraman S., Madara J.L.;
"Cloning and characterization of SLPI from human intestinal
epithelium.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[8]
PROTEIN SEQUENCE OF 26-132, NUCLEOTIDE SEQUENCE [MRNA] OF 26-65,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=3485543; DOI=10.1016/0014-5793(86)81220-0;
Seemueller U., Arnhold M., Fritz H., Wiedenmann K., Machleidt W.,
Heinzel R., Appelhans H., Gassen H.-G., Lottspeich F.;
"The acid-stable proteinase inhibitor of human mucous secretions
(HUSI-I, antileukoprotease). Complete amino acid sequence as revealed
by protein and cDNA sequencing and structural homology to whey
proteins and Red sea turtle proteinase inhibitor.";
FEBS Lett. 199:43-48(1986).
[9]
PROTEIN SEQUENCE OF 26-132, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=3462719; DOI=10.1073/pnas.83.18.6692;
Thompson R.C., Ohlsson K.;
"Isolation, properties, and complete amino acid sequence of human
secretory leukocyte protease inhibitor, a potent inhibitor of
leukocyte elastase.";
Proc. Natl. Acad. Sci. U.S.A. 83:6692-6696(1986).
[10]
PROTEIN SEQUENCE OF 26-52, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND FUNCTION.
PubMed=2039600; DOI=10.1515/bchm3.1991.372.1.13;
Sallenave J.-M., Ryle A.P.;
"Purification and characterization of elastase-specific inhibitor.
Sequence homology with mucus proteinase inhibitor.";
Biol. Chem. Hoppe-Seyler 372:13-21(1991).
[11]
PROTEIN SEQUENCE OF 26-46 AND 94-132, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Tear;
PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
Suarez T., Elortza F.;
"Human basal tear peptidome characterization by CID, HCD, and ETD
followed by in silico and in vitro analyses for antimicrobial peptide
identification.";
J. Proteome Res. 14:2649-2658(2015).
[12]
FUNCTION, AND MUTAGENESIS OF ARG-45; LEU-97; MET-98 AND LEU-99.
PubMed=2110563;
Eisenberg S.P., Hale K.K., Heimdal P., Thompson R.C.;
"Location of the protease-inhibitory region of secretory leukocyte
protease inhibitor.";
J. Biol. Chem. 265:7976-7981(1990).
[13]
FUNCTION, AND MUTAGENESIS OF ARG-45 AND LEU-97.
PubMed=10702419; DOI=10.1016/S0002-9440(10)64971-1;
Mulligan M.S., Lentsch A.B., Huber-Lang M., Guo R.F., Sarma V.,
Wright C.D., Ulich T.R., Ward P.A.;
"Anti-inflammatory effects of mutant forms of secretory leukocyte
protease inhibitor.";
Am. J. Pathol. 156:1033-1039(2000).
[14]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY ELANE, AND TISSUE
SPECIFICITY.
PubMed=24352879; DOI=10.1182/blood-2013-06-508887;
Klimenkova O., Ellerbeck W., Klimiankou M., Unalan M., Kandabarau S.,
Gigina A., Hussein K., Zeidler C., Welte K., Skokowa J.;
"A lack of secretory leukocyte protease inhibitor (SLPI) causes
defects in granulocytic differentiation.";
Blood 123:1239-1249(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHYMOTRYPSIN,
DISULFIDE BONDS, AND REACTIVE BOND.
PubMed=3366116;
Gruetter M.G., Fendrich G., Huber R., Bode W.;
"The 2.5 A X-ray crystal structure of the acid-stable proteinase
inhibitor from human mucous secretions analysed in its complex with
bovine alpha-chymotrypsin.";
EMBO J. 7:345-351(1988).
[16]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 83-132 IN COMPLEX WITH
ELANE, REACTIVE BOND, AND DISULFIDE BONDS.
PubMed=18421166; DOI=10.1107/S0909049507060670;
Koizumi M., Fujino A., Fukushima K., Kamimura T.,
Takimoto-Kamimura M.;
"Complex of human neutrophil elastase with 1/2SLPI.";
J. Synchrotron Radiat. 15:308-311(2008).
[17]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 85-131 IN COMPLEX WITH
TRYPSIN, FUNCTION, REACTIVE BOND, AND DISULFIDE BONDS.
PubMed=24121345; DOI=10.1107/S090904951302133X;
Fukushima K., Kamimura T., Takimoto-Kamimura M.;
"Structure basis 1/2SLPI and porcine pancreas trypsin interaction.";
J. Synchrotron Radiat. 20:943-947(2013).
-!- FUNCTION: Acid-stable proteinase inhibitor with strong affinities
for trypsin, chymotrypsin, elastase, and cathepsin G
(PubMed:3533531, PubMed:3462719, PubMed:2039600, PubMed:2110563,
PubMed:10702419, PubMed:24121345). Modulates the inflammatory and
immune responses after bacterial infection, and after infection by
the intracellular parasite L.major. Down-regulates responses to
bacterial lipopolysaccharide (LPS) (By similarity). Plays a role
in regulating the activation of NF-kappa-B and inflammatory
responses (PubMed:10702419, PubMed:24352879). Has antimicrobial
activity against mycobacteria, but not against salmonella.
Contributes to normal resistance against infection by
M.tuberculosis. Required for normal resistance to infection by
L.major. Required for normal wound healing, probably by preventing
tissue damage by limiting protease activity (By similarity).
Together with ELANE, required for normal differentiation and
proliferation of bone marrow myeloid cells (PubMed:24352879).
{ECO:0000250|UniProtKB:P97430, ECO:0000269|PubMed:10702419,
ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:2110563,
ECO:0000269|PubMed:24121345, ECO:0000269|PubMed:24352879,
ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3533531,
ECO:0000305}.
-!- INTERACTION:
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-355293, EBI-10175124;
O43765:SGTA; NbExp=3; IntAct=EBI-355293, EBI-347996;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2039600,
ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719,
ECO:0000269|PubMed:3485543}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:24352879).
Detected in bone marrow myeloid cells (PubMed:24352879). Detected
in airway sputum (PubMed:2039600). Detected in parotid gland
secretions (PubMed:3462719). Detected in seminal plasma (at
protein level) (PubMed:3485543). Detected in uterus cervix
(PubMed:3533531). {ECO:0000269|PubMed:2039600,
ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719,
ECO:0000269|PubMed:3485543, ECO:0000269|PubMed:3533531}.
-!- INDUCTION: Down-regulated in response to low ELANE activity. Up-
regulated by ELANE treatment in bone marrow cells.
{ECO:0000269|PubMed:24352879}.
-!- MISCELLANEOUS: The pathologies of several chronic and acute
diseases of the respiratory tract involve an imbalance between the
proteases of cells involved in inflammatory responses and the
inhibitors of these proteases. The inflammation-mediated release
of neutrophil elastase in the lungs of patients whose levels of
active alpha-1-antiprotease are compromised by genetic background,
cigarette smoking, air pollutants, or a combination of all three
can result in severe lung damage and a decreased lifespan. The
relatively small size of this protein, its lack of glycosylation
and its stability make this protein a candidate for use as a
therapeutic agent in diseases mediated by leukocyte elastase-
antielastase imbalances. {ECO:0000305}.
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EMBL; X04470; CAA28158.1; -; mRNA.
EMBL; X04502; CAA28187.1; -; Genomic_DNA.
EMBL; X04503; CAA28188.1; -; mRNA.
EMBL; AF114471; AAD19661.1; -; mRNA.
EMBL; AK312192; BAG35125.1; -; mRNA.
EMBL; AL035660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75869.1; -; Genomic_DNA.
EMBL; BC020708; AAH20708.1; -; mRNA.
CCDS; CCDS13347.1; -.
PIR; A25541; TIHUSP.
RefSeq; NP_003055.1; NM_003064.3.
UniGene; Hs.517070; -.
PDB; 2Z7F; X-ray; 1.70 A; I=83-132.
PDB; 4DOQ; X-ray; 2.00 A; B/D=85-131.
PDBsum; 2Z7F; -.
PDBsum; 4DOQ; -.
ProteinModelPortal; P03973; -.
SMR; P03973; -.
BioGrid; 112475; 6.
IntAct; P03973; 20.
MINT; P03973; -.
STRING; 9606.ENSP00000342082; -.
MEROPS; I17.001; -.
iPTMnet; P03973; -.
PhosphoSitePlus; P03973; -.
DMDM; 113636; -.
EPD; P03973; -.
MaxQB; P03973; -.
PaxDb; P03973; -.
PeptideAtlas; P03973; -.
PRIDE; P03973; -.
ProteomicsDB; 51625; -.
DNASU; 6590; -.
Ensembl; ENST00000338380; ENSP00000342082; ENSG00000124107.
GeneID; 6590; -.
KEGG; hsa:6590; -.
UCSC; uc002xnm.2; human.
CTD; 6590; -.
DisGeNET; 6590; -.
EuPathDB; HostDB:ENSG00000124107.5; -.
GeneCards; SLPI; -.
HGNC; HGNC:11092; SLPI.
HPA; CAB002303; -.
HPA; HPA027774; -.
MIM; 107285; gene.
neXtProt; NX_P03973; -.
OpenTargets; ENSG00000124107; -.
PharmGKB; PA35944; -.
eggNOG; ENOG410J417; Eukaryota.
eggNOG; ENOG41116TS; LUCA.
GeneTree; ENSGT00730000111217; -.
HOGENOM; HOG000115819; -.
HOVERGEN; HBG018073; -.
InParanoid; P03973; -.
OMA; SDWQCPG; -.
OrthoDB; EOG091G0S8U; -.
PhylomeDB; P03973; -.
TreeFam; TF338375; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; SLPI; human.
EvolutionaryTrace; P03973; -.
GeneWiki; SLPI; -.
GenomeRNAi; 6590; -.
PMAP-CutDB; P03973; -.
PRO; PR:P03973; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124107; -.
CleanEx; HS_SLPI; -.
Genevisible; P03973; HS.
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:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0006955; P:immune response; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0035821; P:modification of morphology or physiology of other organism; IDA:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
Gene3D; 4.10.75.10; -; 2.
InterPro; IPR036645; Elafin-like_sf.
InterPro; IPR008197; WAP_dom.
Pfam; PF00095; WAP; 2.
PRINTS; PR00003; 4DISULPHCORE.
SMART; SM00217; WAP; 2.
SUPFAM; SSF57256; SSF57256; 2.
PROSITE; PS51390; WAP; 2.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
Protease inhibitor; Reference proteome; Repeat; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 25 {ECO:0000269|PubMed:2039600,
ECO:0000269|PubMed:25946035,
ECO:0000269|PubMed:3462719,
ECO:0000269|PubMed:3485543}.
CHAIN 26 132 Antileukoproteinase.
/FTId=PRO_0000041355.
DOMAIN 28 76 WAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00722}.
DOMAIN 82 130 WAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00722}.
REGION 84 132 Elastase inhibitory domain.
SITE 97 98 Reactive bond for chymotrypsin, trypsin
and elastase.
{ECO:0000305|PubMed:18421166,
ECO:0000305|PubMed:24121345,
ECO:0000305|PubMed:3366116}.
DISULFID 35 64 {ECO:0000269|PubMed:3366116}.
DISULFID 43 68 {ECO:0000269|PubMed:3366116}.
DISULFID 51 63 {ECO:0000269|PubMed:3366116}.
DISULFID 57 72 {ECO:0000269|PubMed:3366116}.
DISULFID 89 118 {ECO:0000244|PDB:2Z7F,
ECO:0000244|PDB:4DOQ,
ECO:0000269|PubMed:3366116}.
DISULFID 96 122 {ECO:0000244|PDB:2Z7F,
ECO:0000244|PDB:4DOQ,
ECO:0000269|PubMed:3366116}.
DISULFID 105 117 {ECO:0000244|PDB:2Z7F,
ECO:0000244|PDB:4DOQ,
ECO:0000269|PubMed:3366116}.
DISULFID 111 126 {ECO:0000244|PDB:2Z7F,
ECO:0000244|PDB:4DOQ,
ECO:0000269|PubMed:3366116}.
MUTAGEN 45 45 R->G: No significant effect on inhibition
of elastase, trypsin and chymotrypsin.
{ECO:0000269|PubMed:10702419,
ECO:0000269|PubMed:2110563}.
MUTAGEN 45 45 R->M,V: No significant effect on
inhibition of elastase, trypsin and
chymotrypsin.
{ECO:0000269|PubMed:2110563}.
MUTAGEN 97 97 L->F: Increases inhibition of
chymotrypsin.
{ECO:0000269|PubMed:10702419,
ECO:0000269|PubMed:2110563}.
MUTAGEN 97 97 L->G: Reduced inhibition of elastase.
Strongly reduced inhibition of
chymotrypsin and trypsin.
{ECO:0000269|PubMed:10702419,
ECO:0000269|PubMed:2110563}.
MUTAGEN 97 97 L->K,R: Strongly reduced inhibition of
elastase. Abolishes inhibition of
trypsin. {ECO:0000269|PubMed:10702419,
ECO:0000269|PubMed:2110563}.
MUTAGEN 98 98 M->G: No significant effect on inhibition
of elastase, trypsin and chymotrypsin.
{ECO:0000269|PubMed:2110563}.
MUTAGEN 99 99 L->G: No significant effect on inhibition
of elastase, trypsin and chymotrypsin.
{ECO:0000269|PubMed:2110563}.
STRAND 86 88 {ECO:0000244|PDB:2Z7F}.
STRAND 95 97 {ECO:0000244|PDB:2Z7F}.
HELIX 108 110 {ECO:0000244|PDB:2Z7F}.
STRAND 116 120 {ECO:0000244|PDB:2Z7F}.
STRAND 123 127 {ECO:0000244|PDB:2Z7F}.
SEQUENCE 132 AA; 14326 MW; B62F3221E0903D90 CRC64;
MKSSGLFPFL VLLALGTLAP WAVEGSGKSF KAGVCPPKKS AQCLRYKKPE CQSDWQCPGK
KRCCPDTCGI KCLDPVDTPN PTRRKPGKCP VTYGQCLMLN PPNFCEMDGQ CKRDLKCCMG
MCGKSCVSPV KA


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Catalog number Product name Quantity
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
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
18-321-177029 SECRETORY LEUCOCYTE PROTEASE INHIBITOR (SLPI) - POLYCLONAL ANTIBODY TO HUMAN SECRETORY LEUCOCYTE PROTEASE INHIBITOR (SLPI); ALP; Secretory leukocyte protease inhibitor; HUSI-1; Seminal proteinase inhi 0.1 mg
20-321-175120 SECRETORY LEUCOCYTE PROTEASE INHIBITOR (SLPI) - MONOCLONAL ANTIBODY TO HUMAN SECRETORY LEUCOCYTE PROTEASE INHIBITOR (SLPI); ALP; Secretory leukocyte protease inhibitor; HUSI-1; Seminal proteinase inhi 0.1 mg
20-321-175121 SECRETORY LEUCOCYTE PROTEASE INHIBITOR (SLPI) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN SECRETORY LEUCOCYTE PROTEASE INHIBITOR (SLPI); ALP; Secretory leukocyte protease inhibitor; HUSI-1; Seminal pr 0.05 mg
EIAAB12765 Elafin,Elastase-specific inhibitor,ESI,Homo sapiens,Human,Peptidase inhibitor 3,PI3,PI-3,Protease inhibitor WAP3,SKALP,Skin-derived antileukoproteinase,WAP four-disulfide core domain protein 14,WAP3,W
EIAAB39365 Contrapsin-like protease inhibitor 1,CPI-21,GHR-P63,Growth hormone-regulated proteinase inhibitor,Kallikrein-binding protein,KBP,Rat,Rattus norvegicus,Serine protease inhibitor 2,Serine protease inhib
EIAAB13139 Cancer_testis antigen 71,CT71,Epididymal protease inhibitor,Eppin,Homo sapiens,Human,Protease inhibitor WAP7,Serine protease inhibitor-like with Kunitz and WAP domains 1,SPINLW1,WAP four-disulfide cor
U1312p CLIA ALP,ALP,Antileukoproteinase,Pig,Secretory leukocyte protease inhibitor,SLPI,Sus scrofa 96T
E1312p ELISA ALP,ALP,Antileukoproteinase,Pig,Secretory leukocyte protease inhibitor,SLPI,Sus scrofa 96T
E1312p ELISA kit ALP,ALP,Antileukoproteinase,Pig,Secretory leukocyte protease inhibitor,SLPI,Sus scrofa 96T
U1312m CLIA ALP,Antileukoproteinase,Mouse,Mus musculus,Secretory leukocyte protease inhibitor,Slpi 96T
E1312m ELISA kit ALP,Antileukoproteinase,Mouse,Mus musculus,Secretory leukocyte protease inhibitor,Slpi 96T
E1312m ELISA ALP,Antileukoproteinase,Mouse,Mus musculus,Secretory leukocyte protease inhibitor,Slpi 96T
EIAAB39366 Contrapsin-like protease inhibitor 3,CPI-23,Rat,Rattus norvegicus,Serine protease inhibitor 1,Serine protease inhibitor A3L,Serpin A3L,Serpina3l,SPI-1,Spin2a
EIAAB39369 Contrapsin-like protease inhibitor 6,CPI-26,Rat,Rattus norvegicus,Serine protease inhibitor 3,Serine protease inhibitor A3N,Serpin A3N,Serpina3n,SPI-2.2,SPI-3,Spin2c
EIAAB46317 Epididymal secretory protein E4,HE4,Homo sapiens,Human,Major epididymis-specific protein E4,Putative protease inhibitor WAP5,WAP four-disulfide core domain protein 2,WAP5,WFDC2
EIAAB39439 Bos taurus,Bovine,Proteinase inhibitor 6,Serine proteinase inhibitor B-43,Serpin B6,SERPINB6
EIAAB46325 Gm706,Mouse,Mus musculus,Putative protease inhibitor WAP8C,WAP four-disulfide core domain protein 8,Wfdc8
EIAAB46302 C20orf146,Homo sapiens,Human,Putative protease inhibitor WAP10A,WAP four-disulfide core domain protein 10A,WAP10,WFDC10A
4249 Secretory leukocyte protease inhibitor 0.1 mg
4249 Secretory leukocyte protease inhibitor 0.5 mg
EIAAB13140 Epididymal protease inhibitor,Eppin,Mouse,Mus musculus,Serine protease inhibitor-like with Kunitz and WAP domains 1,Spinlw1
E1312r Rat secretory leukocyte protease inhibitor ELISA K 96T


 

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