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Plasma serine protease inhibitor (Acrosomal serine protease inhibitor) (Plasminogen activator inhibitor 3) (PAI-3) (PAI3) (Protein C inhibitor) (PCI) (Serpin A5)

 IPSP_HUMAN              Reviewed;         406 AA.
P05154; Q07616; Q9UG30;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
27-SEP-2017, entry version 194.
RecName: Full=Plasma serine protease inhibitor;
AltName: Full=Acrosomal serine protease inhibitor;
AltName: Full=Plasminogen activator inhibitor 3;
Short=PAI-3;
Short=PAI3;
AltName: Full=Protein C inhibitor;
Short=PCI;
AltName: Full=Serpin A5;
Flags: Precursor;
Name=SERPINA5; Synonyms=PCI, PLANH3, PROCI;
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 VARIANT ASN-64.
PubMed=3027058;
Suzuki K., Deyashiki Y., Nishioka J., Kurachi K., Akira M.,
Yamamoto S., Hashimoto S.;
"Characterization of a cDNA for human protein C inhibitor. A new
member of the plasma serine protease inhibitor superfamily.";
J. Biol. Chem. 262:611-616(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-64.
PubMed=2173165; DOI=10.1016/0049-3848(90)90142-Y;
Meijers J.C.M., Chung D.W.;
"Evidence for a glycine residue at position 316 in human protein C
inhibitor.";
Thromb. Res. 59:389-393(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-64.
PubMed=1714450;
Meijers J.C.M., Chung D.W.;
"Organization of the gene coding for human protein C inhibitor
(plasminogen activator inhibitor-3). Assignment of the gene to
chromosome 14.";
J. Biol. Chem. 266:15028-15034(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8148499;
Hayashi T., Suzuki K.;
"Gene organization of human protein C inhibitor, a member of SERPIN
family proteins encoded in five exons.";
Int. J. Hematol. 58:213-224(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-55; ASN-64 AND GLU-105.
TISSUE=Liver;
PubMed=8713781;
Radtke K.-P., Greengard J.S., Fernandez J.A., Villoutreix B.O.,
Griffin J.H.;
"A two-allele polymorphism in protein C inhibitor with varying
frequencies in different ethnic populations.";
Thromb. Haemost. 75:62-69(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-44; VAL-55;
ASN-64; VAL-94; GLU-105; PRO-115 AND ARG-217.
SeattleSNPs variation discovery resource;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-64.
TISSUE=Skin;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-406, AND VARIANT ASN-64.
TISSUE=Testis;
PubMed=8471250; DOI=10.1002/mrd.1080340308;
Moore A., Penfold L.M., Johnson J.L., Latchman D.S., Moore H.D.;
"Human sperm-egg binding is inhibited by peptides corresponding to
core region of an acrosomal serine protease inhibitor.";
Mol. Reprod. Dev. 34:280-291(1993).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-406, AND VARIANT ASN-64.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
PROTEIN SEQUENCE OF 20-39.
PubMed=2556811;
Laurell M., Stenflo J.;
"Protein C inhibitor from human plasma: characterization of native and
cleaved inhibitor and demonstration of inhibitor complexes with plasma
kallikrein.";
Thromb. Haemost. 62:885-891(1989).
[12]
FUNCTION IN BLOOD PLASMA SERINE PROTEASE INHIBITION, AND HETERODIMER
WITH F2; F5 AND F10.
PubMed=6323392;
Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
"Mechanism of inhibition of activated protein C by protein C
inhibitor.";
J. Biochem. 95:187-195(1984).
[13]
FUNCTION IN BLOOD PLASMA PLAU INHIBITION, AND HETERODIMER WITH PLAU.
PubMed=3501295;
Stief T.W., Radtke K.P., Heimburger N.;
"Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for
identity of PCI and plasminogen activator inhibitor 3.";
Biol. Chem. Hoppe-Seyler 368:1427-1433(1987).
[14]
FUNCTION IN BLOOD PLASMA SERINE PROTEASE INHIBITION, AND HETERODIMER
WITH F5; F11 AND KLKB1.
PubMed=2844223; DOI=10.1021/bi00412a005;
Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M.,
Bouma B.N.;
"Inactivation of human plasma kallikrein and factor XIa by protein C
inhibitor.";
Biochemistry 27:4231-4237(1988).
[15]
FUNCTION IN SEMINAL PLASMA KLK3 INHIBITION, HETERODIMER WITH KLK3, AND
SUBCELLULAR LOCATION.
PubMed=1725227; DOI=10.1016/0049-3848(91)90002-E;
Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., Cabo A.;
"Functionally active protein C inhibitor/plasminogen activator
inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at
high concentrations in human seminal plasma and complexes with
prostate-specific antigen.";
Thromb. Res. 64:309-320(1991).
[16]
TISSUE SPECIFICITY.
PubMed=1372913; DOI=10.1172/JCI115689;
Laurell M., Christensson A., Abrahamsson P.A., Stenflo J., Lilja H.;
"Protein C inhibitor in human body fluids. Seminal plasma is rich in
inhibitor antigen deriving from cells throughout the male reproductive
system.";
J. Clin. Invest. 89:1094-1101(1992).
[17]
FUNCTION IN SEMINAL PLASMA ACR INHIBITION, HETERODIMER WITH ACR, AND
SUBCELLULAR LOCATION.
PubMed=7521127;
Zheng X., Geiger M., Ecke S., Bielek E., Donner P., Eberspacher U.,
Schleuning W.D., Binder B.R.;
"Inhibition of acrosin by protein C inhibitor and localization of
protein C inhibitor to spermatozoa.";
Am. J. Physiol. 267:C466-C472(1994).
[18]
FUNCTION IN SERINE PROTEASE INHIBITION, AND MUTAGENESIS OF THR-371;
PHE-372; ARG-373 AND ARG-376.
PubMed=7548057; DOI=10.1021/bi00040a009;
Cooper S.T., Whinna H.C., Jackson T.P., Boyd J.M., Church F.C.;
"Intermolecular interactions between protein C inhibitor and
coagulation proteases.";
Biochemistry 34:12991-12997(1995).
[19]
FUNCTION IN SEMINAL PLASMA AND URINE KALLIKREIN INHIBITION,
HETERODIMER WITH TISSUE KALLIKREIN, AND SUBCELLULAR LOCATION.
PubMed=8536714; DOI=10.1111/j.1432-1033.1995.641_b.x;
Espana F., Fink E., Sanchez-Cuenca J., Gilabert J., Estelles A.,
Witzgall K.;
"Complexes of tissue kallikrein with protein C inhibitor in human
semen and urine.";
Eur. J. Biochem. 234:641-649(1995).
[20]
FUNCTION IN SEMINAL PLASMA KLK3 INHIBITION, HETERODIMER WITH F5, AND
INTERACTION WITH SEMG2.
PubMed=8665956; DOI=10.1111/j.1432-1033.1996.0088q.x;
Kise H., Nishioka J., Kawamura J., Suzuki K.;
"Characterization of semenogelin II and its molecular interaction with
prostate-specific antigen and protein C inhibitor.";
Eur. J. Biochem. 238:88-96(1996).
[21]
FUNCTION IN BLOOD PLASMA F5 INHIBITION.
PubMed=9473218;
Elisen M.G., von dem Borne P.A., Bouma B.N., Meijers J.C.;
"Protein C inhibitor acts as a procoagulant by inhibiting the
thrombomodulin-induced activation of protein C in human plasma.";
Blood 91:1542-1547(1998).
[22]
FUNCTION IN FERTILIZATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=9510955; DOI=10.1095/biolreprod58.3.670;
Elisen M.G., van Kooij R.J., Nolte M.A., Marquart J.A., Lock T.M.,
Bouma B.N., Meijers J.C.;
"Protein C inhibitor may modulate human sperm-oocyte interactions.";
Biol. Reprod. 58:670-677(1998).
[23]
FUNCTION IN BLOOD PLASMA F5 INHIBITION, HETERODIMER WITH F5,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9556620; DOI=10.1074/jbc.273.18.11281;
Nishioka J., Ning M., Hayashi T., Suzuki K.;
"Protein C inhibitor secreted from activated platelets efficiently
inhibits activated protein C on phosphatidylethanolamine of platelet
membrane and microvesicles.";
J. Biol. Chem. 273:11281-11287(1998).
[24]
FUNCTION IN SEMINAL PLASMA SERINE PROTEASES INHIBITION, AND
HETERODIMER WITH PLAT AND PLAU.
PubMed=10340997; DOI=10.1093/molehr/5.6.513;
He S., Lin Y.L., Liu Y.X.;
"Functionally inactive protein C inhibitor in seminal plasma may be
associated with infertility.";
Mol. Hum. Reprod. 5:513-519(1999).
[25]
FUNCTION IN RETINOIC ACID TRANSPORT.
PubMed=11722589; DOI=10.1046/j.0014-2956.2001.02560.x;
Jerabek I., Zechmeister-Machhart M., Binder B.R., Geiger M.;
"Binding of retinoic acid by the inhibitory serpin protein C
inhibitor.";
Eur. J. Biochem. 268:5989-5996(2001).
[26]
FUNCTION AS REGULATOR OF TUMOR CELL INVASION, HETERODIMER WITH PLAU,
AND TISSUE SPECIFICITY.
PubMed=14696115; DOI=10.1002/ijc.11594;
Wakita T., Hayashi T., Nishioka J., Tamaru H., Akita N., Asanuma K.,
Kamada H., Gabazza E.C., Ido M., Kawamura J., Suzuki K.;
"Regulation of carcinoma cell invasion by protein C inhibitor whose
expression is decreased in renal cell carcinoma.";
Int. J. Cancer 108:516-523(2004).
[27]
FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS11E INHIBITION,
HETERODIMER WITH TMPRSS11E, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
THR-360 AND ARG-373.
PubMed=15328353; DOI=10.1074/jbc.M403299200;
Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C.,
Strickland D.K., Lawrence D.A., Antalis T.M., Bugge T.H.;
"Mouse DESC1 is located within a cluster of seven DESC1-like genes and
encodes a type II transmembrane serine protease that forms serpin
inhibitory complexes.";
J. Biol. Chem. 279:46981-46994(2004).
[28]
FUNCTION IN BLOOD PLASMA F5 INHIBITION, HETERODIMER WITH F5, AND
TISSUE SPECIFICITY.
PubMed=15140131; DOI=10.1111/j.1538-7836.2004.00733.x;
Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H.,
Gabazza E.C., Ido M., Suzuki K.;
"Characterization of a novel human protein C inhibitor (PCI) gene
transgenic mouse useful for studying the role of PCI in physiological
and pathological conditions.";
J. Thromb. Haemost. 2:949-961(2004).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[30]
FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND
HETERODIMER WITH TMPRSS7.
PubMed=15853774; DOI=10.1042/BJ20050299;
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
"Matriptase-3 is a novel phylogenetically preserved membrane-anchored
serine protease with broad serpin reactivity.";
Biochem. J. 390:231-242(2005).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-262 AND ASN-338.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[32]
TISSUE SPECIFICITY.
PubMed=17706750; DOI=10.1016/j.acthis.2007.04.007;
Zhang C., Li X., Lian X., Wang Y., Zeng Y., Yang K., Yu J., Gao Q.,
Yang T.;
"Immunolocalization of protein C inhibitor in differentiation of human
epidermal keratinocytes.";
Acta Histochem. 109:461-467(2007).
[33]
FUNCTION, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION AT ASN-249; ASN-262 AND
ASN-338, STRUCTURE OF CARBOHYDRATES, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18467335; DOI=10.1074/jbc.M800608200;
Sun W., Parry S., Panico M., Morris H.R., Kjellberg M., Engstrom A.,
Dell A., Schedin-Weiss S.;
"N-glycans and the N terminus of protein C inhibitor affect the
cofactor-enhanced rates of thrombin inhibition.";
J. Biol. Chem. 283:18601-18611(2008).
[34]
MUTAGENESIS OF ARG-253; GLU-272; LYS-274; LYS-285; ARG-288; LYS-289;
LYS-292 AND ARG-381.
PubMed=18362344; DOI=10.1073/pnas.0711055105;
Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.;
"Molecular basis of thrombin recognition by protein C inhibitor
revealed by the 1.6-A structure of the heparin-bridged complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008).
[35]
GLYCOSYLATION AT THR-39, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21056543; DOI=10.1016/j.bbrc.2010.11.005;
Sun W., Parry S., Ubhayasekera W., Engstrom A., Dell A.,
Schedin-Weiss S.;
"Further insight into the roles of the glycans attached to human blood
protein C inhibitor.";
Biochem. Biophys. Res. Commun. 403:198-202(2010).
[36]
GLYCOSYLATION AT THR-39, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[37]
3D-STRUCTURE MODELING.
PubMed=2172989; DOI=10.1073/pnas.87.21.8506;
Kuhn L.A., Griffin J.H., Fisher C.L., Greengard J.S., Bouma B.N.,
Espana F., Tainer J.A.;
"Elucidating the structural chemistry of glycosaminoglycan recognition
by protein C inhibitor.";
Proc. Natl. Acad. Sci. U.S.A. 87:8506-8510(1990).
[38]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 30-406, AND GLYCOSYLATION AT
ASN-262.
PubMed=12575940; DOI=10.1016/S0969-2126(02)00944-9;
Huntington J.A., Kjellberg M., Stenflo J.;
"Crystal structure of protein C inhibitor provides insights into
hormone binding and heparin activation.";
Structure 11:205-215(2003).
[39]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 36-406.
PubMed=17337440; DOI=10.1074/jbc.M701074200;
Li W., Adams T.E., Kjellberg M., Stenflo J., Huntington J.A.;
"Structure of native protein C inhibitor provides insight into its
multiple functions.";
J. Biol. Chem. 282:13759-13768(2007).
[40]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 37-406 IN COMPLEX WITH
SYNTHETIC HEPARIN, HEPARIN-BINDING SITES, AND MUTAGENESIS OF ARG-248;
LYS-285; ARG-288; LYS-289 AND LYS-292.
PubMed=18974053; DOI=10.1074/jbc.M805974200;
Li W., Huntington J.A.;
"The heparin binding site of protein C inhibitor is protease-
dependent.";
J. Biol. Chem. 283:36039-36045(2008).
[41]
VARIANTS VAL-55; ASN-64; GLU-105; ALA-121 AND ARG-217.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[42]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
-!- FUNCTION: Heparin-dependent serine protease inhibitor acting in
body fluids and secretions. Inactivates serine proteases by
binding irreversibly to their serine activation site. Involved in
the regulation of intravascular and extravascular proteolytic
activities. Plays hemostatic roles in the blood plasma. Acts as a
procoagulant and proinflammatory factor by inhibiting the
anticoagulant activated protein C factor as well as the generation
of activated protein C factor by the thrombin/thrombomodulin
complex. Acts as an anticoagulant factor by inhibiting blood
coagulation factors like prothrombin, factor XI, factor Xa, plasma
kallikrein and fibrinolytic enzymes such as tissue- and urinary-
type plasminogen activators. In seminal plasma, inactivates
several serine proteases implicated in the reproductive system.
Inhibits the serpin acrosin; indirectly protects component of the
male genital tract from being degraded by excessive released
acrosin. Inhibits tissue-and urinary-type plasminogen activator,
prostate-specific antigen and kallikrein activities; has a control
on the sperm motility and fertilization. Inhibits the activated
protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the
degradation of semenogelin during the process of transfer of
spermatozoa from the male reproductive tract into the female
tract. In urine, inhibits urinary-type plasminogen activator and
kallikrein activities. Inactivates membrane-anchored serine
proteases activities such as MPRSS7 and TMPRSS11E. Inhibits
urinary-type plasminogen activator-dependent tumor cell invasion
and metastasis. May also play a non-inhibitory role in seminal
plasma and urine as a hydrophobic hormone carrier by its binding
to retinoic acid. {ECO:0000269|PubMed:10340997,
ECO:0000269|PubMed:11722589, ECO:0000269|PubMed:14696115,
ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:15328353,
ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:1725227,
ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:2844223,
ECO:0000269|PubMed:3501295, ECO:0000269|PubMed:6323392,
ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:7548057,
ECO:0000269|PubMed:8536714, ECO:0000269|PubMed:8665956,
ECO:0000269|PubMed:9473218, ECO:0000269|PubMed:9510955,
ECO:0000269|PubMed:9556620}.
-!- ENZYME REGULATION: Its inhibitory activity is greatly enhanced in
the presence of glycosaminoglycans, heparin, thrombomodulin and
phospholipids vesicles.
-!- SUBUNIT: Forms protease inhibiting heterodimers in extracellular
body fluids with serine proteases such as activated protein
C/coagulation factor V/F5, acrosin/ACR, chymotrypsinogen B/CTRB1,
prothrombin/F2, factor Xa/F10, factor XI/F11, kallikrein/KLKB1,
tissue kallikrein, trypsin/PRSS1, prostate specific antigen/KLK3,
tissue plasminogen activator/PLAT and urinary plasminogen
activator/PLAU. Forms membrane-anchored serine proteases
inhibiting heterodimers with TMPRSS7 and TMPRSS11E. Interacts with
SEMG2. {ECO:0000269|PubMed:18974053, ECO:0000269|PubMed:8665956}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:1725227, ECO:0000269|PubMed:18467335,
ECO:0000269|PubMed:7521127, ECO:0000269|PubMed:8536714,
ECO:0000269|PubMed:9510955, ECO:0000269|PubMed:9556620}.
Note=Localized on the plasma membrane overlying the acrosomal head
of spermatozoa of ependymal spermatozoa and ejaculated sperm.
Localized at the equatorial segment of acrosome-reacted
spematozoa. Localized in alpha granules in resting platelets and
on the external plasma membrane and within the surface-connected
cannalicular system in activated platelets.
-!- TISSUE SPECIFICITY: Predominantly expressed in the epithelium of
seminal vesicles. Expressed in the proximal tubular epithelium of
the kidney. Expressed in the superficial and more differentiated
epidermal keratinocytes of the skin. Expressed in megakaryocytes
and platelets. Expressed poorly in kidney tumor cells compared to
non tumor kidney tissues. Expressed in spermatozoa. Present in
very high concentration in seminal plasma. Present in high
concentration in plasma, synovial and Graaf follicle fluids.
Present in low concentration in breast milk and in amniotic
fluids. Present in very low concentration in urine, cerebrospinal
fluids, saliva and tears (at protein level). Strongly expressed in
liver. Expressed in kidney, spleen, pancreas, skeletal muscle,
heart, testes, ovary, interstitial Leydig cells, epididymal
glands, seminal vesicles and prostate.
{ECO:0000269|PubMed:1372913, ECO:0000269|PubMed:14696115,
ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:17706750,
ECO:0000269|PubMed:18467335, ECO:0000269|PubMed:9510955,
ECO:0000269|PubMed:9556620}.
-!- DOMAIN: The reactive center loop (RCL) extends out from the body
of the protein and directs binding to the target protease. The
protease cleaves the serpin at the reactive site within the RCL,
establishing a covalent linkage between the carboxyl group of the
serpin reactive site and the serine hydroxyl of the protease. The
resulting inactive serpin-protease complex is highly stable.
-!- PTM: N- and O-glycosylated. N-glycosylation consists of a mixture
of sialylated bi- (including sialyl-Lewis X epitopes), tri- and
tetra-antennary complex-type chains; affects the maximal
heparin- and thrombomodulin-enhanced rates of thrombin inhibition.
O-glycosylated with core 1 or possibly core 8 glycans. Further
modified with 2 sialic acid residues.
{ECO:0000269|PubMed:12575940, ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18467335,
ECO:0000269|PubMed:21056543, ECO:0000269|PubMed:22171320}.
-!- PTM: Proteolytically cleaved. Inhibition of proteases is
accompanied by formation of a stable enzyme-inhibitor complex and
by degradation of the serpin to lower molecular weight
derivatives. Proteolytically cleaved at the N-terminus; inhibits
slightly the heparin- and thrombomodulin-enhanced rates of
thrombin inhibition. {ECO:0000269|PubMed:15328353,
ECO:0000269|PubMed:18467335}.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/serpina5/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J02639; AAA35688.1; -; mRNA.
EMBL; M68516; AAA02811.1; -; Genomic_DNA.
EMBL; S69366; AAB30461.1; -; Genomic_DNA.
EMBL; S69364; AAB30461.1; JOINED; Genomic_DNA.
EMBL; S69574; AAB30461.1; JOINED; Genomic_DNA.
EMBL; S69365; AAB30461.1; JOINED; Genomic_DNA.
EMBL; U35464; AAB60386.1; -; mRNA.
EMBL; AF361796; AAK27240.1; -; Genomic_DNA.
EMBL; AL049839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008915; AAH08915.1; -; mRNA.
EMBL; S58545; AAB26244.2; -; mRNA.
EMBL; AL080185; CAB45766.1; -; mRNA.
CCDS; CCDS9928.1; -.
PIR; A39339; A39339.
RefSeq; NP_000615.3; NM_000624.5.
UniGene; Hs.159628; -.
UniGene; Hs.741309; -.
PDB; 1LQ8; X-ray; 2.40 A; A/C/E/G=30-375, B/D/F/H=376-406.
PDB; 1PAI; Model; -; A=20-373, B=374-406.
PDB; 2HI9; X-ray; 2.30 A; A/B/C=44-406.
PDB; 2OL2; X-ray; 2.00 A; A/B=36-406.
PDB; 2PAI; Model; -; A=20-373, B=374-406.
PDB; 3DY0; X-ray; 1.55 A; A=37-372, B=379-406.
PDBsum; 1LQ8; -.
PDBsum; 1PAI; -.
PDBsum; 2HI9; -.
PDBsum; 2OL2; -.
PDBsum; 2PAI; -.
PDBsum; 3DY0; -.
ProteinModelPortal; P05154; -.
SMR; P05154; -.
BioGrid; 111135; 24.
CORUM; P05154; -.
DIP; DIP-29869N; -.
IntAct; P05154; 8.
MINT; MINT-1386269; -.
STRING; 9606.ENSP00000333203; -.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB05413; T-1249.
DrugBank; DB00013; Urokinase.
MEROPS; I04.004; -.
iPTMnet; P05154; -.
PhosphoSitePlus; P05154; -.
UniCarbKB; P05154; -.
BioMuta; SERPINA5; -.
DMDM; 322510122; -.
MaxQB; P05154; -.
PaxDb; P05154; -.
PeptideAtlas; P05154; -.
PRIDE; P05154; -.
DNASU; 5104; -.
Ensembl; ENST00000329597; ENSP00000333203; ENSG00000188488.
Ensembl; ENST00000553780; ENSP00000450837; ENSG00000188488.
Ensembl; ENST00000554276; ENSP00000451610; ENSG00000188488.
Ensembl; ENST00000554866; ENSP00000451126; ENSG00000188488.
GeneID; 5104; -.
KEGG; hsa:5104; -.
UCSC; uc001ydm.3; human.
CTD; 5104; -.
DisGeNET; 5104; -.
EuPathDB; HostDB:ENSG00000188488.13; -.
GeneCards; SERPINA5; -.
H-InvDB; HIX0079547; -.
HGNC; HGNC:8723; SERPINA5.
HPA; HPA056919; -.
MIM; 601841; gene.
neXtProt; NX_P05154; -.
OpenTargets; ENSG00000188488; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118839; -.
HOGENOM; HOG000238521; -.
HOVERGEN; HBG005957; -.
InParanoid; P05154; -.
KO; K03913; -.
OMA; VMVNYIF; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; P05154; -.
TreeFam; TF343201; -.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
SABIO-RK; P05154; -.
ChiTaRS; SERPINA5; human.
EvolutionaryTrace; P05154; -.
GeneWiki; Protein_C_inhibitor; -.
GenomeRNAi; 5104; -.
PMAP-CutDB; P05154; -.
PRO; PR:P05154; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000188488; -.
CleanEx; HS_SERPINA5; -.
ExpressionAtlas; P05154; baseline and differential.
Genevisible; P05154; HS.
GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
GO; GO:0031094; C:platelet dense tubular network; IDA:UniProtKB.
GO; GO:0097181; C:protein C inhibitor-coagulation factor V complex; IDA:UniProtKB.
GO; GO:0097182; C:protein C inhibitor-coagulation factor Xa complex; IDA:UniProtKB.
GO; GO:0097183; C:protein C inhibitor-coagulation factor XI complex; IDA:UniProtKB.
GO; GO:0036029; C:protein C inhibitor-KLK3 complex; IDA:UniProtKB.
GO; GO:0036030; C:protein C inhibitor-plasma kallikrein complex; IDA:UniProtKB.
GO; GO:0036026; C:protein C inhibitor-PLAT complex; IDA:UniProtKB.
GO; GO:0036027; C:protein C inhibitor-PLAU complex; IDA:UniProtKB.
GO; GO:0036028; C:protein C inhibitor-thrombin complex; IDA:UniProtKB.
GO; GO:0036025; C:protein C inhibitor-TMPRSS11E complex; IDA:UniProtKB.
GO; GO:0036024; C:protein C inhibitor-TMPRSS7 complex; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0032190; F:acrosin binding; IPI:UniProtKB.
GO; GO:0005539; F:glycosaminoglycan binding; TAS:UniProtKB.
GO; GO:0008201; F:heparin binding; TAS:UniProtKB.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane; NAS:UniProtKB.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:UniProtKB.
GO; GO:0061107; P:seminal vesicle development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Fertilization; Glycoprotein; Heparin-binding; Lipid transport;
Polymorphism; Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:2556811}.
PROPEP 20 25 Removed in mature form.
/FTId=PRO_0000414091.
CHAIN 26 406 Plasma serine protease inhibitor.
/FTId=PRO_0000032427.
SITE 373 374 Reactive bond.
CARBOHYD 39 39 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:21056543,
ECO:0000269|PubMed:22171320}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:18467335}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12575940,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18467335}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18467335}.
VARIANT 44 44 S -> G (in dbSNP:rs2069975).
{ECO:0000269|Ref.6}.
/FTId=VAR_013080.
VARIANT 55 55 A -> V (in allele PCI*B; dbSNP:rs6118).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:8713781,
ECO:0000269|Ref.6}.
/FTId=VAR_007100.
VARIANT 64 64 S -> N (in dbSNP:rs6115).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1714450,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:2173165,
ECO:0000269|PubMed:3027058,
ECO:0000269|PubMed:8471250,
ECO:0000269|PubMed:8713781,
ECO:0000269|Ref.6}.
/FTId=VAR_013081.
VARIANT 94 94 G -> V (in dbSNP:rs2069976).
{ECO:0000269|Ref.6}.
/FTId=VAR_013082.
VARIANT 105 105 K -> E (in allele PCI*B; dbSNP:rs6119).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:8713781,
ECO:0000269|Ref.6}.
/FTId=VAR_007101.
VARIANT 115 115 L -> P (in dbSNP:rs2069999).
{ECO:0000269|Ref.6}.
/FTId=VAR_013083.
VARIANT 121 121 P -> A (in dbSNP:rs6120).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013900.
VARIANT 217 217 G -> R (in dbSNP:rs6114).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.6}.
/FTId=VAR_013084.
MUTAGEN 248 248 R->E: Does not change the rate of
thrombin or activated protein C/F5
inhibition in the presence or absence of
heparin. Strongly reduces the rate of
thrombin inhibition in the presence of
heparin. {ECO:0000269|PubMed:18974053}.
MUTAGEN 253 253 R->E: Inhibits strongly thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344}.
MUTAGEN 272 272 E->K: Does not inhibit thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344}.
MUTAGEN 274 274 K->E: Does not inhibit thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344}.
MUTAGEN 285 285 K->E: Does not change the rate of
thrombin or activated protein C/F5
inhibition in the presence or absence of
heparin. Slightly reduces the rate of
thrombin inhibition in the presence of
heparin. Does not inhibit thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344,
ECO:0000269|PubMed:18974053}.
MUTAGEN 288 288 R->E: Does not change the rate of
thrombin or activated protein C/F5
inhibition in the presence or absence of
heparin. Slightly reduces the rate of
thrombin inhibition in the presence of
heparin. Does not inhibit thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344,
ECO:0000269|PubMed:18974053}.
MUTAGEN 289 289 K->E: Does not change the rate of
thrombin or activated protein C/F5
inhibition in the presence or absence of
heparin. Slightly reduces the rate of
thrombin inhibition in the presence of
heparin. Inhibits weakly thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344,
ECO:0000269|PubMed:18974053}.
MUTAGEN 292 292 K->E: Does not change the rate of
thrombin or activated protein C/F5
inhibition in the presence or absence of
heparin. Slightly reduces the rate of
thrombin inhibition in the presence of
heparin. Does not inhibit thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344,
ECO:0000269|PubMed:18974053}.
MUTAGEN 360 360 T->R: Inhibits heterodimer formation with
TMPRSS11E. {ECO:0000269|PubMed:15328353}.
MUTAGEN 371 371 T->R: Increases inhibition of activated
protein C/F5 and factor XI/F11
activities. Decreases inhibition of
thrombin activity.
{ECO:0000269|PubMed:7548057}.
MUTAGEN 372 372 F->P,G: Increases inhibition of thrombin
activity. {ECO:0000269|PubMed:7548057}.
MUTAGEN 373 373 R->P: Increases inhibition of thrombin
activity. Inhibits heterodimer formation
with TMPRSS11E.
{ECO:0000269|PubMed:15328353,
ECO:0000269|PubMed:7548057}.
MUTAGEN 376 376 R->P: Does not change inhibition of
thrombin, activated protein C/F5 and
factor XI/F11 activities.
{ECO:0000269|PubMed:7548057}.
MUTAGEN 381 381 R->E: Does not inhibit thrombomodulin-
enhanced rate of thrombin inhibition in
presence of heparin.
{ECO:0000269|PubMed:18362344}.
CONFLICT 28 28 K -> E (in Ref. 10; CAB45766).
{ECO:0000305}.
CONFLICT 221 221 Q -> L (in Ref. 9; AAB26244).
{ECO:0000305}.
CONFLICT 335 335 G -> R (in Ref. 1; AAA35688 and 9;
AAB26244). {ECO:0000305}.
CONFLICT 384 384 F -> S (in Ref. 9; AAB26244).
{ECO:0000305}.
HELIX 48 59 {ECO:0000244|PDB:3DY0}.
STRAND 65 67 {ECO:0000244|PDB:3DY0}.
HELIX 69 81 {ECO:0000244|PDB:3DY0}.
HELIX 85 94 {ECO:0000244|PDB:3DY0}.
HELIX 101 117 {ECO:0000244|PDB:3DY0}.
STRAND 123 135 {ECO:0000244|PDB:3DY0}.
HELIX 143 153 {ECO:0000244|PDB:3DY0}.
STRAND 156 159 {ECO:0000244|PDB:3DY0}.
HELIX 165 179 {ECO:0000244|PDB:3DY0}.
TURN 180 182 {ECO:0000244|PDB:3DY0}.
STRAND 195 211 {ECO:0000244|PDB:3DY0}.
HELIX 215 217 {ECO:0000244|PDB:3DY0}.
STRAND 219 228 {ECO:0000244|PDB:3DY0}.
STRAND 230 247 {ECO:0000244|PDB:3DY0}.
TURN 248 251 {ECO:0000244|PDB:3DY0}.
STRAND 252 262 {ECO:0000244|PDB:3DY0}.
STRAND 264 270 {ECO:0000244|PDB:3DY0}.
HELIX 275 281 {ECO:0000244|PDB:3DY0}.
HELIX 284 293 {ECO:0000244|PDB:3DY0}.
STRAND 295 304 {ECO:0000244|PDB:3DY0}.
STRAND 306 313 {ECO:0000244|PDB:3DY0}.
HELIX 314 316 {ECO:0000244|PDB:3DY0}.
HELIX 318 321 {ECO:0000244|PDB:3DY0}.
HELIX 325 327 {ECO:0000244|PDB:3DY0}.
TURN 334 336 {ECO:0000244|PDB:3DY0}.
STRAND 337 339 {ECO:0000244|PDB:1LQ8}.
STRAND 343 355 {ECO:0000244|PDB:3DY0}.
STRAND 357 371 {ECO:0000244|PDB:3DY0}.
STRAND 372 375 {ECO:0000244|PDB:2OL2}.
STRAND 380 383 {ECO:0000244|PDB:3DY0}.
STRAND 388 404 {ECO:0000244|PDB:3DY0}.
SEQUENCE 406 AA; 45675 MW; 2A8FF3DC33C77E04 CRC64;
MQLFLLLCLV LLSPQGASLH RHHPREMKKR VEDLHVGATV APSSRRDFTF DLYRALASAA
PSQSIFFSPV SISMSLAMLS LGAGSSTKMQ ILEGLGLNLQ KSSEKELHRG FQQLLQELNQ
PRDGFQLSLG NALFTDLVVD LQDTFVSAMK TLYLADTFPT NFRDSAGAMK QINDYVAKQT
KGKIVDLLKN LDSNAVVIMV NYIFFKAKWE TSFNHKGTQE QDFYVTSETV VRVPMMSRED
QYHYLLDRNL SCRVVGVPYQ GNATALFILP SEGKMQQVEN GLSEKTLRKW LKMFKKRQLE
LYLPKFSIEG SYQLEKVLPS LGISNVFTSH ADLSGISNHS NIQVSEMVHK AVVEVDESGT
RAAAATGTIF TFRSARLNSQ RLVFNRPFLM FIVDNNILFL GKVNRP


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