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Leukocyte elastase inhibitor (LEI) (Monocyte/neutrophil elastase inhibitor) (EI) (M/NEI) (Peptidase inhibitor 2) (PI-2) (Serpin B1)

 ILEU_HUMAN              Reviewed;         379 AA.
P30740; A8K5L2; B4DNT0; Q53FB9; Q5W0E1; Q9UDF8;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
12-SEP-2018, entry version 178.
RecName: Full=Leukocyte elastase inhibitor;
Short=LEI;
AltName: Full=Monocyte/neutrophil elastase inhibitor;
Short=EI;
Short=M/NEI;
AltName: Full=Peptidase inhibitor 2;
Short=PI-2;
AltName: Full=Serpin B1;
Name=SERPINB1; Synonyms=ELANH2, MNEI, PI2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1376927; DOI=10.1073/pnas.89.12.5635;
Remold-O'Donnell E., Chin J., Alberts M.;
"Sequence and molecular characterization of human monocyte/neutrophil
elastase inhibitor.";
Proc. Natl. Acad. Sci. U.S.A. 89:5635-5639(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9630619; DOI=10.1016/S0378-1119(98)00189-9;
Zeng W., Silverman G.A., Remold-O'Donnell E.;
"Structure and sequence of human M/NEI (monocyte/neutrophil elastase
inhibitor), an Ov-serpin family gene.";
Gene 213:179-187(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and 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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Small intestine;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
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 1-10, AND ACETYLATION AT MET-1.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
PROTEIN SEQUENCE OF 111-129; 216-244 AND 255-274.
PubMed=7578269; DOI=10.1016/0167-4889(95)00113-7;
Packard B.Z., Lee S.S., Remold-O'Donnell E., Komoriya A.;
"A serpin from human tumor cells with direct lymphoid immunomodulatory
activity: mitogenic stimulation of human tumor-infiltrating
lymphocytes.";
Biochim. Biophys. Acta 1269:41-50(1995).
[10]
PROTEIN SEQUENCE OF 178-185; 204-210 AND 364-371.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[11]
FUNCTION, REACTIVE SITES, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11747453; DOI=10.1021/bi0113925;
Cooley J., Takayama T.K., Shapiro S.D., Schechter N.M.,
Remold-O'Donnell E.;
"The serpin MNEI inhibits elastase-like and chymotrypsin-like serine
proteases through efficient reactions at two active sites.";
Biochemistry 40:15762-15770(2001).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GZMH,
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=23269243; DOI=10.4049/jimmunol.1202542;
Wang L., Li Q., Wu L., Liu S., Zhang Y., Yang X., Zhu P., Zhang H.,
Zhang K., Lou J., Liu P., Tong L., Sun F., Fan Z.;
"Identification of SERPINB1 as a physiological inhibitor of human
granzyme H.";
J. Immunol. 190:1319-1330(2013).
-!- FUNCTION: Regulates the activity of the neutrophil proteases
elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and
kallikrein-3. Also functions as a potent intracellular inhibitor
of granzyme H. {ECO:0000269|PubMed:11747453}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23269243}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic granule
{ECO:0000269|PubMed:23269243}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P30740-1; Sequence=Displayed;
Name=2;
IsoId=P30740-2; Sequence=VSP_056511;
Note=No experimental confirmation available.;
-!- DOMAIN: Reactive bond 1 is specific for reaction with
chymotrypsin-like protease such as cathepsin G, chymotrypsin,
chymase or granzyme H, while reactive bond 2 is specific for
reaction with elastase-like protease such as neutrophil elastase,
proteinase-3, pancreatic elastase or PSA.
-!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD97090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M93056; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF053630; AAC31394.1; -; Genomic_DNA.
EMBL; AK291327; BAF84016.1; -; mRNA.
EMBL; AK298044; BAG60342.1; -; mRNA.
EMBL; BT006928; AAP35574.1; -; mRNA.
EMBL; AK223370; BAD97090.1; ALT_INIT; mRNA.
EMBL; AL139092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009015; AAH09015.1; -; mRNA.
CCDS; CCDS4477.1; -. [P30740-1]
PIR; S27383; S27383.
RefSeq; NP_109591.1; NM_030666.3. [P30740-1]
RefSeq; XP_011512635.1; XM_011514333.1. [P30740-1]
RefSeq; XP_011512636.1; XM_011514334.2. [P30740-1]
UniGene; Hs.381167; -.
PDB; 4GA7; X-ray; 2.90 A; A/B=1-379.
PDBsum; 4GA7; -.
ProteinModelPortal; P30740; -.
SMR; P30740; -.
BioGrid; 108307; 23.
IntAct; P30740; 3.
STRING; 9606.ENSP00000370115; -.
MEROPS; I04.006; -.
iPTMnet; P30740; -.
PhosphoSitePlus; P30740; -.
DMDM; 266344; -.
OGP; P30740; -.
REPRODUCTION-2DPAGE; IPI00027444; -.
EPD; P30740; -.
PaxDb; P30740; -.
PeptideAtlas; P30740; -.
PRIDE; P30740; -.
ProteomicsDB; 54734; -.
DNASU; 1992; -.
Ensembl; ENST00000380739; ENSP00000370115; ENSG00000021355. [P30740-1]
GeneID; 1992; -.
KEGG; hsa:1992; -.
CTD; 1992; -.
DisGeNET; 1992; -.
EuPathDB; HostDB:ENSG00000021355.12; -.
GeneCards; SERPINB1; -.
HGNC; HGNC:3311; SERPINB1.
HPA; HPA018871; -.
HPA; HPA018882; -.
HPA; HPA052642; -.
MIM; 130135; gene.
neXtProt; NX_P30740; -.
OpenTargets; ENSG00000021355; -.
PharmGKB; PA35046; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118789; -.
HOGENOM; HOG000238519; -.
HOVERGEN; HBG005957; -.
InParanoid; P30740; -.
KO; K13963; -.
OMA; AESFHQV; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; P30740; -.
TreeFam; TF352619; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; SERPINB1; human.
GeneWiki; SERPINB1; -.
GenomeRNAi; 1992; -.
PMAP-CutDB; P30740; -.
PRO; PR:P30740; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000021355; Expressed in 220 organ(s), highest expression level in esophagus squamous epithelium.
CleanEx; HS_SERPINB1; -.
ExpressionAtlas; P30740; baseline and differential.
Genevisible; P30740; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
InterPro; IPR015557; Serpin_B1.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
PANTHER; PTHR11461:SF180; PTHR11461:SF180; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism;
Protease inhibitor; Reference proteome; Serine protease inhibitor.
CHAIN 1 379 Leukocyte elastase inhibitor.
/FTId=PRO_0000094101.
SITE 343 344 Reactive bond 1.
SITE 344 345 Reactive bond 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
MOD_RES 137 137 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 151 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056511.
VARIANT 82 82 A -> V (in dbSNP:rs34825616).
/FTId=VAR_051945.
CONFLICT 137 137 K -> R (in Ref. 4; AAP35574).
{ECO:0000305}.
CONFLICT 149 149 A -> V (in Ref. 3; BAF84016).
{ECO:0000305}.
CONFLICT 264 264 L -> F (in Ref. 3; BAF84016).
{ECO:0000305}.
CONFLICT 272 272 Missing (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 329 329 E -> K (in Ref. 3; BAF84016).
{ECO:0000305}.
HELIX 3 22 {ECO:0000244|PDB:4GA7}.
STRAND 24 26 {ECO:0000244|PDB:4GA7}.
STRAND 28 30 {ECO:0000244|PDB:4GA7}.
HELIX 32 43 {ECO:0000244|PDB:4GA7}.
HELIX 48 57 {ECO:0000244|PDB:4GA7}.
HELIX 60 62 {ECO:0000244|PDB:4GA7}.
HELIX 66 77 {ECO:0000244|PDB:4GA7}.
STRAND 83 95 {ECO:0000244|PDB:4GA7}.
HELIX 102 111 {ECO:0000244|PDB:4GA7}.
STRAND 116 119 {ECO:0000244|PDB:4GA7}.
HELIX 121 139 {ECO:0000244|PDB:4GA7}.
TURN 140 142 {ECO:0000244|PDB:4GA7}.
STRAND 159 168 {ECO:0000244|PDB:4GA7}.
STRAND 171 173 {ECO:0000244|PDB:4GA7}.
TURN 177 179 {ECO:0000244|PDB:4GA7}.
STRAND 181 188 {ECO:0000244|PDB:4GA7}.
STRAND 191 209 {ECO:0000244|PDB:4GA7}.
TURN 210 213 {ECO:0000244|PDB:4GA7}.
STRAND 214 221 {ECO:0000244|PDB:4GA7}.
STRAND 224 235 {ECO:0000244|PDB:4GA7}.
STRAND 238 242 {ECO:0000244|PDB:4GA7}.
HELIX 244 249 {ECO:0000244|PDB:4GA7}.
HELIX 252 259 {ECO:0000244|PDB:4GA7}.
HELIX 261 263 {ECO:0000244|PDB:4GA7}.
STRAND 265 274 {ECO:0000244|PDB:4GA7}.
STRAND 276 283 {ECO:0000244|PDB:4GA7}.
HELIX 285 290 {ECO:0000244|PDB:4GA7}.
HELIX 295 297 {ECO:0000244|PDB:4GA7}.
TURN 299 301 {ECO:0000244|PDB:4GA7}.
TURN 305 307 {ECO:0000244|PDB:4GA7}.
STRAND 315 326 {ECO:0000244|PDB:4GA7}.
STRAND 345 347 {ECO:0000244|PDB:4GA7}.
STRAND 349 353 {ECO:0000244|PDB:4GA7}.
STRAND 358 364 {ECO:0000244|PDB:4GA7}.
TURN 365 368 {ECO:0000244|PDB:4GA7}.
STRAND 369 376 {ECO:0000244|PDB:4GA7}.
SEQUENCE 379 AA; 42742 MW; BAAE08DFCBCD8CD3 CRC64;
MEQLSSANTR FALDLFLALS ENNPAGNIFI SPFSISSAMA MVFLGTRGNT AAQLSKTFHF
NTVEEVHSRF QSLNADINKR GASYILKLAN RLYGEKTYNF LPEFLVSTQK TYGADLASVD
FQHASEDARK TINQWVKGQT EGKIPELLAS GMVDNMTKLV LVNAIYFKGN WKDKFMKEAT
TNAPFRLNKK DRKTVKMMYQ KKKFAYGYIE DLKCRVLELP YQGEELSMVI LLPDDIEDES
TGLKKIEEQL TLEKLHEWTK PENLDFIEVN VSLPRFKLEE SYTLNSDLAR LGVQDLFNSS
KADLSGMSGA RDIFISKIVH KSFVEVNEEG TEAAAATAGI ATFCMLMPEE NFTADHPFLF
FIRHNSSGSI LFLGRFSSP


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U0181m CLIA Ela2,Elane,Elastase-2,Leukocyte elastase,Mouse,Mus musculus,Neutrophil elastase 96T
201-11-1042 Rat Leukocyte Elastase Inhibitor(LEI)ELISA kit 96T
QY-E10603 Rat Leukocyte Elastase Inhibitor(LEI)ELISA kit 96T
DL-LEI-Hu Human Leukocyte Elastase Inhibitor (LEI) ELISA Kit 96T
DL-LEI-Mu Mouse Leukocyte Elastase Inhibitor (LEI) ELISA Kit 96T
EH2499 Leukocyte elastase inhibitor Elisa Kit 96T
UB-E10603 Rat Leukocyte Elastase Inhibitor(LEI)ELISA kit 96T
201-11-1042 Rat Leukocyte Elastase Inhibitor (LEI)ELISA kit 96T
K782-100 Neutrophil Elastase Inhibitor Screening Kit 100 assays
HPAI-AVI PAI - 1 Human PAI-1 (Neutrophil Elastase inhibitor) 0.5 mg
HPAI-AVI Human PAI-1 (Neutrophil Elastase inhibitor) 1.0 mg
GWB-AXR357 Neutrophil Elastase Inhibitor Screening Kit
HPAI-AVI Human PAI-1 (Neutrophil Elastase inhibitor) 0.5 mg
HPAI-AVI PAI - 1 Human PAI-1 (Neutrophil Elastase inhibitor) 1.0 mg
E0757Mo Mouse Leukocyte Elastase Inhibitor (LEI)ELISA kit 96T


 

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