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Integrin alpha-PS1 (Position-specific antigen subunit alpha-1) (Protein multiple edematous wings) [Cleaved into: Integrin alpha-PS1 heavy chain; Integrin alpha-PS1 light chain]

 ITA1_DROME              Reviewed;        1146 AA.
Q24247; M9PEG3; M9PHG7; M9PJL8; Q8SY51; Q9VYF6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
22-NOV-2017, entry version 171.
RecName: Full=Integrin alpha-PS1;
AltName: Full=Position-specific antigen subunit alpha-1;
AltName: Full=Protein multiple edematous wings;
Contains:
RecName: Full=Integrin alpha-PS1 heavy chain;
Contains:
RecName: Full=Integrin alpha-PS1 light chain;
Flags: Precursor;
Name=mew; ORFNames=CG1771;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PARTIAL PROTEIN SEQUENCE,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Oregon-R; TISSUE=Embryo, and Larva;
PubMed=8240969; DOI=10.1016/0925-4773(93)90020-X;
Wehrli M., Diantonio A., Fearnley I.M., Smith R.J., Wilcox M.;
"Cloning and characterization of alpha PS1, a novel Drosophila
melanogaster integrin.";
Mech. Dev. 43:21-36(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION.
PubMed=7972082; DOI=10.1073/pnas.91.24.11447;
Gotwals P.J., Fessler L.I., Wehrli M., Hynes R.O.;
"Drosophila PS1 integrin is a laminin receptor and differs in ligand
specificity from PS2.";
Proc. Natl. Acad. Sci. U.S.A. 91:11447-11451(1994).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657 AND ASN-1027, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=19035354; DOI=10.1002/dvdy.21802;
Dinkins M.B., Fratto V.M., Lemosy E.K.;
"Integrin alpha chains exhibit distinct temporal and spatial
localization patterns in epithelial cells of the Drosophila ovary.";
Dev. Dyn. 237:3927-3939(2008).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-711; ASN-718 AND ASN-761,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
-!- FUNCTION: Integrin alpha-PS1/beta-PS is a receptor for laminin.
{ECO:0000269|PubMed:7972082}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit is composed of a heavy and a light chain linked by a
disulfide bond. Alpha-PS1 associates with beta-PS.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Lateral cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Basal cell membrane
{ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein
{ECO:0000269|PubMed:19035354}. Note=During mid-oogenesis,
localizes to the apical, to the lateral and to the basal membranes
of follicle cells. Apical membrane localization peaks at oogenesis
stages 9 and 10A in columnar follicle cells overlying the oocyte
while decreases in the most posterior follicle cells. Localization
to lateral and basal membranes persists during dorsal appendage
morphogenesis, although diminished and often absent.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=B;
IsoId=Q24247-1; Sequence=Displayed;
Name=A;
IsoId=Q24247-2; Sequence=VSP_009270;
Note=No experimental confirmation available.;
Name=C;
IsoId=Q24247-3; Sequence=VSP_053396;
Note=No experimental confirmation available.;
Name=D;
IsoId=Q24247-4; Sequence=VSP_009270, VSP_053396;
Note=No experimental confirmation available.;
Name=E;
IsoId=Q24247-5; Sequence=VSP_009270, VSP_053397;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in follicle cells (at protein
level). At syncytial blastoderm stage, expressed in the ectoderm
but not in the mesodermal precursors. At embryonic stage 7,
expressed in dorsal and ventrolateral ectoderm and in some yolk
nuclei. At late stage 10, expression is homogeneous in the
ectoderm and is particularly abundant in the anterior and
posterior midgut primordia. At stage 11, strongly expressed in a
metameric pattern in the ectoderm, in the proctodeum and in the
posterior midgut primordium. At stage 12, accumulates at the
segment boundaries that start to become morphologically visible,
similar expression pattern is observed in the central nervous
system. In third larval instar wing imaginal disk, strongly
expressed in the dorsal compartment, in the adepithelial cells and
in patches on the peripodial membrane covering the imaginal disk
to the outside. {ECO:0000269|PubMed:19035354,
ECO:0000269|PubMed:8240969}.
-!- DEVELOPMENTAL STAGE: Expressed during mid- and late-oogenesis (at
protein level). Expressed throughout embryonic and larval
development with peaks of expression during mid-embryogenesis and
at third larval instar. {ECO:0000269|PubMed:19035354,
ECO:0000269|PubMed:8240969}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X73975; CAA52155.1; -; mRNA.
EMBL; AE014298; AAF48242.2; -; Genomic_DNA.
EMBL; AE014298; AAN09652.1; -; Genomic_DNA.
EMBL; AE014298; AGB95345.1; -; Genomic_DNA.
EMBL; AE014298; AGB95346.1; -; Genomic_DNA.
EMBL; AE014298; AGB95347.1; -; Genomic_DNA.
EMBL; AY075338; AAL68203.1; -; mRNA.
PIR; S40311; S40311.
RefSeq; NP_001259503.1; NM_001272574.1. [Q24247-5]
RefSeq; NP_001259504.1; NM_001272575.2. [Q24247-3]
RefSeq; NP_001259505.1; NM_001272576.2. [Q24247-4]
RefSeq; NP_511145.2; NM_078590.3. [Q24247-1]
RefSeq; NP_727679.1; NM_167354.2. [Q24247-2]
UniGene; Dm.152; -.
ProteinModelPortal; Q24247; -.
BioGrid; 58660; 11.
IntAct; Q24247; 15.
STRING; 7227.FBpp0302767; -.
iPTMnet; Q24247; -.
PaxDb; Q24247; -.
PRIDE; Q24247; -.
EnsemblMetazoa; FBtr0073731; FBpp0073562; FBgn0004456. [Q24247-2]
EnsemblMetazoa; FBtr0073732; FBpp0073563; FBgn0004456. [Q24247-1]
EnsemblMetazoa; FBtr0310647; FBpp0302767; FBgn0004456. [Q24247-3]
EnsemblMetazoa; FBtr0310648; FBpp0302768; FBgn0004456. [Q24247-4]
EnsemblMetazoa; FBtr0330398; FBpp0303424; FBgn0004456. [Q24247-5]
GeneID; 32275; -.
KEGG; dme:Dmel_CG1771; -.
CTD; 32275; -.
FlyBase; FBgn0004456; mew.
eggNOG; ENOG410IPBB; Eukaryota.
eggNOG; ENOG410XVGZ; LUCA.
GeneTree; ENSGT00760000118782; -.
InParanoid; Q24247; -.
OrthoDB; EOG091G02JI; -.
PhylomeDB; Q24247; -.
Reactome; R-DME-3000157; Laminin interactions.
Reactome; R-DME-446107; Type I hemidesmosome assembly.
GenomeRNAi; 32275; -.
PRO; PR:Q24247; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004456; -.
ExpressionAtlas; Q24247; differential.
Genevisible; Q24247; DM.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
GO; GO:0008305; C:integrin complex; IDA:FlyBase.
GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IMP:FlyBase.
GO; GO:0050840; F:extracellular matrix binding; IDA:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
GO; GO:0004872; F:receptor activity; IMP:FlyBase.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0007475; P:apposition of dorsal and ventral imaginal disc-derived wing surfaces; NAS:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007414; P:axonal defasciculation; IMP:FlyBase.
GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
GO; GO:0030154; P:cell differentiation; TAS:FlyBase.
GO; GO:0016477; P:cell migration; TAS:FlyBase.
GO; GO:0098609; P:cell-cell adhesion; TAS:FlyBase.
GO; GO:0007160; P:cell-matrix adhesion; ISS:FlyBase.
GO; GO:0048567; P:ectodermal digestive tract morphogenesis; TAS:FlyBase.
GO; GO:0007427; P:epithelial cell migration, open tracheal system; TAS:FlyBase.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:FlyBase.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IGI:FlyBase.
GO; GO:0007494; P:midgut development; TAS:FlyBase.
GO; GO:0016203; P:muscle attachment; IGI:FlyBase.
GO; GO:0007424; P:open tracheal system development; NAS:FlyBase.
GO; GO:0007432; P:salivary gland boundary specification; IMP:FlyBase.
GO; GO:0007431; P:salivary gland development; TAS:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IGI:FlyBase.
GO; GO:0007608; P:sensory perception of smell; IGI:FlyBase.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
GO; GO:0007426; P:tracheal outgrowth, open tracheal system; TAS:FlyBase.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 4.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1146 Integrin alpha-PS1.
/FTId=PRO_0000016320.
CHAIN 31 ?960 Integrin alpha-PS1 heavy chain.
{ECO:0000255}.
/FTId=PRO_0000016321.
CHAIN ?961 1146 Integrin alpha-PS1 light chain.
{ECO:0000255}.
/FTId=PRO_0000016322.
TOPO_DOM 31 1085 Extracellular. {ECO:0000255}.
TRANSMEM 1086 1106 Helical. {ECO:0000255}.
TOPO_DOM 1107 1146 Cytoplasmic. {ECO:0000255}.
REPEAT 38 105 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 121 186 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 193 245 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 254 303 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 304 366 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 367 422 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 432 494 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 470 470 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 511 511 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
CARBOHYD 680 680 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 711 711 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 718 718 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 761 761 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 928 928 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1027 1027 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
VAR_SEQ 1 97 Missing (in isoform A, isoform D and
isoform E).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_009270.
VAR_SEQ 114 115 RN -> RTNGAYEINKH (in isoform C and
isoform D). {ECO:0000305}.
/FTId=VSP_053396.
VAR_SEQ 1146 1146 F -> FXQEGTVGWDLVRRRRRRRRLKLRLPVTAQPRHGWR
KTTDKSINNNNNNNHNNNSSNSRNDSDVDVLSLTPPPPPLS
IFSWGNDGYYQASAAWWGHHM (in isoform E).
{ECO:0000305}.
/FTId=VSP_053397.
CONFLICT 730 731 ML -> IV (in Ref. 1; CAA52155).
{ECO:0000305}.
CONFLICT 815 815 D -> E (in Ref. 1; CAA52155).
{ECO:0000305}.
SEQUENCE 1146 AA; 127973 MW; E8AB75BC8DE6854E CRC64;
MLELPFTTIR PNCRLRQNLG ILIILQCVLT CYNFNLEQRL PIVKYGHPHS HFGYSVATHT
IGEANGPNKT NCVLVGAPLD QNRQPNTTHS GALWRCPMTQ RFDDCEQVIT DGRRNFDSEI
LSPPGNDEIK EDQWMGVTVR SNPLQANGSG GKVIVCAHRY MYIVRENRYG QGLCYLLTND
LQFEEVHEPC KGRPVQRQHE DYGLCQAGTS AALLDDDTMV LGSPGPYTWR GSIWVTQVGG
EYLQRDKTTY YSDHSDLNSP VDKYSYLGMS VTGGRFFGHM SYAAGAPRSE GHGQVVIFDK
STDNPIPVHS ILDGEQFGSS FGYELATADI NGDHRPDLIV AAPLYFTKTE GGAVYVYQNI
QDTLPMKYTL KLTGPLESRF GLALANIGDL NKDNCEDLAV GAPYEGNGVV YIYLGSSQGL
NSKPAQKIQA SELGGTIPNG QPIRTFGISI SGNTDLDDNS YPDVVIGAFN SSAAVILLAR
PIISIQTSVQ RKELHNMDPN TPGCLDDPAS NLTCFTFRAC CSIEPYDEKN KELRLAYSVE
AETFDHLKKF SRVFFFDREN KRTNVLSRVV RVHTNGRTEC QAVTGYIKAN TRDIQTPVRF
RLKYSLVEPP LADSALVRLN PILDQTQAHV DFEGTFQKDC GDDDLCESNL IIRVEPNITE
SSGNEYTLIL DETELEVRIN VSNLADSAYE AQLFIAHQAG VSYVATKKPT NATCNSYNTT
LVACSLGNPM LRDTTTFVTI RFQPKGLEPS EKIMLFHIFA NTTSKLVGPE RPERDLRVNV
VRRAKLNFRG WAIPEQSFYS GSSVANSVAN TAATDIEGHG PMGMDDVGSQ VHHMFTIFNE
GPSTAPKVQM VIHWPYSLYS DPQSGRPVQY LLYLEQVPTV EVSQGECHVA KEYVNPLNLA
SGSRENPAYL SAPAQMRMFP SQSRHSFNKS LIHSQRSYYS SSHRDDHSDD TQSNRNRVRR
SFLERVTRLE RLMYDPESSN AANGKKQDIV ELDCNKGATN CVRIECDILN MPALSEAQVV
VKARLWNSTL VSEYPRVERV RIFSTATAQI PESYGVEVMD HNNIEVETRA YPELRNQQRD
TSIPWLIIIL GIVGGLLLLA LVTYVLWKVG FFKRIRPTDP TLSGNLEKMN EEKPFLAPSK
NTHHVF


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U1685h CLIA CD11 antigen-like family member B,CD11B,Cell surface glycoprotein MAC-1 subunit alpha,CR-3 alpha chain,CR3A,Homo sapiens,Human,Integrin alpha-M,ITGAM,Leukocyte adhesion receptor MO1,Neutrophil ad 96T
E1685h ELISA kit CD11 antigen-like family member B,CD11B,Cell surface glycoprotein MAC-1 subunit alpha,CR-3 alpha chain,CR3A,Homo sapiens,Human,Integrin alpha-M,ITGAM,Leukocyte adhesion receptor MO1,Neutrop 96T
E1685h ELISA CD11 antigen-like family member B,CD11B,Cell surface glycoprotein MAC-1 subunit alpha,CR-3 alpha chain,CR3A,Homo sapiens,Human,Integrin alpha-M,ITGAM,Leukocyte adhesion receptor MO1,Neutrophil a 96T
E1572m ELISA kit CD11 antigen-like family member A,Integrin alpha-L,Itgal,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,Lfa-1,LFA-1A,Ly-15,Ly-15,Lymp 96T
U1572m CLIA CD11 antigen-like family member A,Integrin alpha-L,Itgal,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,Lfa-1,LFA-1A,Ly-15,Ly-15,Lymphocyte 96T
E1572m ELISA CD11 antigen-like family member A,Integrin alpha-L,Itgal,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,Lfa-1,LFA-1A,Ly-15,Ly-15,Lymphocyt 96T
20-783-72304 MOUSE ANTI HUMAN CD11b Azide Free - INTEGRIN ALPHA M CHAIN. MAC-1; Cell surface glycoprotein MAC-1 subunit alpha; CR-3 alpha chain; Leukocyte adhesion receptor MO1; Neutrophil adherence receptor; CD11 1 mg
U1572b CLIA Bos taurus,Bovine,CD11 antigen-like family member A,Integrin alpha-L,ITGAL,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,LFA-1A 96T
E1572b ELISA kit Bos taurus,Bovine,CD11 antigen-like family member A,Integrin alpha-L,ITGAL,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,LFA-1A 96T
E1572b ELISA Bos taurus,Bovine,CD11 antigen-like family member A,Integrin alpha-L,ITGAL,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,LFA-1A 96T
E1572h ELISA CD11 antigen-like family member A,CD11A,Homo sapiens,Human,Integrin alpha-L,ITGAL,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,LFA-1A 96T
E1572h ELISA kit CD11 antigen-like family member A,CD11A,Homo sapiens,Human,Integrin alpha-L,ITGAL,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,LFA- 96T
U1572h CLIA CD11 antigen-like family member A,CD11A,Homo sapiens,Human,Integrin alpha-L,ITGAL,Leukocyte adhesion glycoprotein LFA-1 alpha chain,Leukocyte function-associated molecule 1 alpha chain,LFA-1A 96T
20-783-72302 MOUSE ANTI HUMAN CD11b RPE - INTEGRIN ALPHA M CHAIN. MAC-1; Cell surface glycoprotein MAC-1 subunit alpha; CR-3 alpha chain; Leukocyte adhesion receptor MO1; Neutrophil adherence receptor; CD11b antig 100 TESTS
20-783-72299 MOUSE ANTI HUMAN CD11b Biotin - INTEGRIN ALPHA M CHAIN. MAC-1; Cell surface glycoprotein MAC-1 subunit alpha; CR-3 alpha chain; Leukocyte adhesion receptor MO1; Neutrophil adherence receptor; CD11b an 0.1 mg
15-288-21339 Integrin alpha-3 - Galactoprotein B3; GAPB3; VLA-3 alpha chain; FRP-2; CD49c antigen Polyclonal 0.05 mg
15-288-21339 Integrin alpha-3 - Galactoprotein B3; GAPB3; VLA-3 alpha chain; FRP-2; CD49c antigen Polyclonal 0.1 mg


 

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