Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lipopolysaccharide-binding protein (LBP)

 LBP_HUMAN               Reviewed;         481 AA.
P18428; B2R938; O43438; Q92672; Q9H403; Q9UD66;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
12-SEP-2018, entry version 164.
RecName: Full=Lipopolysaccharide-binding protein;
Short=LBP;
Flags: Precursor;
Name=LBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-40, VARIANT
LEU-436, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=2402637; DOI=10.1126/science.2402637;
Schumann R.R., Leong S.R., Flaggs G.W., Gray P.W., Wright S.D.,
Mathison J.C., Tobias P.S., Ulevitch R.J.;
"Structure and function of lipopolysaccharide binding protein.";
Science 249:1429-1431(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=7517398;
Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L.,
Lane J.C., Leong S.R., Thornton M.B., Miller K.L., Scott R.W.;
"Bactericidal/permeability-increasing protein and lipopolysaccharide
(LPS)-binding protein. LPS binding properties and effects on LPS-
mediated cell activation.";
J. Biol. Chem. 269:17411-17416(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-436.
PubMed=9240454; DOI=10.1006/bbrc.1997.6970;
Hubacek J.A., Buchler C., Aslanidis C., Schmitz G.;
"The genomic organization of the genes for human lipopolysaccharide
binding protein (LBP) and bactericidal permeability increasing protein
(BPI) is highly conserved.";
Biochem. Biophys. Res. Commun. 236:427-430(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9441745; DOI=10.1006/geno.1997.5030;
Kirschning C.J., Au-Young J., Lamping N., Reuter D., Pfeil D.,
Seilhamer J.J., Schumann R.R.;
"Similar organization of the lipopolysaccharide-binding protein (LBP)
and phospholipid transfer protein (PLTP) genes suggests a common gene
family of lipid-binding proteins.";
Genomics 46:416-425(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-436.
TISSUE=Liver;
Long J.Y., Liu J.Q., Xue Y.N., Wang H.X.;
"Cloning and sequencing of human lipopolysaccharide-binding protein
gene.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:469-471(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[7]
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).
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
Sutton C.L., Smith R.I.F., Centola M.B., Theofan G.;
"Cloning and characterization of the human LBP upstream sequence.";
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, AND INTERACTION WITH CD14 AND LIPOPOLYSACCHARIDE.
PubMed=1698311; DOI=10.1126/science.1698311;
Wright S.D., Ramos R.A., Tobias P.S., Ulevitch R.J., Mathison J.C.;
"CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS
binding protein.";
Science 249:1431-1433(1990).
[11]
REVIEW.
PubMed=17481951; DOI=10.1016/j.ijmm.2007.04.001;
Jerala R.;
"Structural biology of the LPS recognition.";
Int. J. Med. Microbiol. 297:353-363(2007).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
FUNCTION.
PubMed=20133493; DOI=10.1093/intimm/dxq005;
Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.;
"Lipopolysaccharide-binding protein-mediated Toll-like receptor 4
dimerization enables rapid signal transduction against
lipopolysaccharide stimulation on membrane-associated CD14-expressing
cells.";
Int. Immunol. 22:271-280(2010).
[14]
FUNCTION, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, GLYCOSYLATION, VARIANT LEU-333, AND CHARACTERIZATION OF
VARIANT LEU-333.
PubMed=24120359; DOI=10.1016/j.immuni.2013.09.005;
Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S.,
Lundvall L., Hamann L., van der Ploeg A., Pickkers P.,
Giamarellos-Bourboulis E., Kubarenko A.V., Weber A.N., Kabesch M.,
Kumpf O., An H.J., Lee J.O., Schumann R.R.;
"The crystal structure of lipopolysaccharide binding protein reveals
the location of a frequent mutation that impairs innate immunity.";
Immunity 39:647-660(2013).
-!- FUNCTION: Plays a role in the innate immune response. Binds to the
lipid A moiety of bacterial lipopolysaccharides (LPS), a
glycolipid present in the outer membrane of all Gram-negative
bacteria (PubMed:7517398, PubMed:24120359). Acts as an affinity
enhancer for CD14, facilitating its association with LPS. Promotes
the release of cytokines in response to bacterial
lipopolysaccharide (PubMed:7517398, PubMed:24120359).
{ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:20133493,
ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398,
ECO:0000305|PubMed:17481951}.
-!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with
soluble and membrane-bound CD14. {ECO:0000269|PubMed:1698311,
ECO:0000305|PubMed:17481951}.
-!- INTERACTION:
Q13162:PRDX4; NbExp=4; IntAct=EBI-3927059, EBI-2211957;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402637,
ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398}.
Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}.
Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
granules. {ECO:0000250|UniProtKB:P17213}.
-!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
{ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:24120359}.
-!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M35533; AAA59493.1; -; mRNA.
EMBL; X98657; CAA67226.1; -; Genomic_DNA.
EMBL; X98658; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98659; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98660; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98661; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98662; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98663; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98664; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98665; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98666; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98667; CAA67226.1; JOINED; Genomic_DNA.
EMBL; X98668; CAA67226.1; JOINED; Genomic_DNA.
EMBL; AF013512; AAC39547.1; -; Genomic_DNA.
EMBL; AF013500; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013501; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013502; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013503; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013504; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013505; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013506; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013507; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013508; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013509; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013510; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF013511; AAC39547.1; JOINED; Genomic_DNA.
EMBL; AF105067; AAD21962.1; -; mRNA.
EMBL; AK313625; BAG36385.1; -; mRNA.
EMBL; AL080249; CAC10462.1; -; Genomic_DNA.
EMBL; CH471077; EAW76034.1; -; Genomic_DNA.
EMBL; L42172; AAA66446.1; -; Genomic_DNA.
CCDS; CCDS13304.1; -.
PIR; A35843; A35843.
PIR; A54136; A54136.
RefSeq; NP_004130.2; NM_004139.4.
UniGene; Hs.154078; -.
ProteinModelPortal; P18428; -.
SMR; P18428; -.
BioGrid; 110121; 16.
DIP; DIP-90N; -.
IntAct; P18428; 14.
STRING; 9606.ENSP00000217407; -.
TCDB; 1.C.40.1.2; the bactericidal permeability increasing protein (bpip) family.
iPTMnet; P18428; -.
PhosphoSitePlus; P18428; -.
BioMuta; LBP; -.
DMDM; 116242615; -.
EPD; P18428; -.
MaxQB; P18428; -.
PaxDb; P18428; -.
PeptideAtlas; P18428; -.
PRIDE; P18428; -.
ProteomicsDB; 53558; -.
TopDownProteomics; P18428; -.
Ensembl; ENST00000217407; ENSP00000217407; ENSG00000129988.
GeneID; 3929; -.
KEGG; hsa:3929; -.
UCSC; uc002xic.3; human.
CTD; 3929; -.
DisGeNET; 3929; -.
EuPathDB; HostDB:ENSG00000129988.5; -.
GeneCards; LBP; -.
HGNC; HGNC:6517; LBP.
HPA; CAB025905; -.
HPA; HPA001508; -.
MIM; 151990; gene.
neXtProt; NX_P18428; -.
OpenTargets; ENSG00000129988; -.
PharmGKB; PA30303; -.
eggNOG; KOG4160; Eukaryota.
eggNOG; ENOG410Z88E; LUCA.
GeneTree; ENSGT00730000110583; -.
HOGENOM; HOG000231250; -.
HOVERGEN; HBG002797; -.
InParanoid; P18428; -.
KO; K05399; -.
OMA; GHYEFHS; -.
OrthoDB; EOG091G08NV; -.
PhylomeDB; P18428; -.
TreeFam; TF315617; -.
Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-HSA-166020; Transfer of LPS from LBP carrier to CD14.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
SignaLink; P18428; -.
GeneWiki; Lipopolysaccharide-binding_protein; -.
GenomeRNAi; 3929; -.
PRO; PR:P18428; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000129988; Expressed in 94 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_LBP; -.
Genevisible; P18428; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
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:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0071723; F:lipopeptide binding; IDA:AgBase.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
GO; GO:0070891; F:lipoteichoic acid binding; IDA:MGI.
GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEP:BHF-UCL.
GO; GO:0006968; P:cellular defense response; ISS:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:BHF-UCL.
GO; GO:0032490; P:detection of molecule of bacterial origin; IDA:BHF-UCL.
GO; GO:0045087; P:innate immune response; ISS:BHF-UCL.
GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IEA:Ensembl.
GO; GO:0015920; P:lipopolysaccharide transport; IDA:BHF-UCL.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0033036; P:macromolecule localization; IDA:AgBase.
GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0008228; P:opsonization; ISS:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
GO; GO:0045919; P:positive regulation of cytolysis; IDA:AgBase.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; ISS:BHF-UCL.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IDA:BHF-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
InterPro; IPR030675; BPI/LBP.
InterPro; IPR032942; BPI/LBP/Plunc.
InterPro; IPR030180; LBP.
InterPro; IPR001124; Lipid-bd_serum_glycop_C.
InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
InterPro; IPR017942; Lipid-bd_serum_glycop_N.
PANTHER; PTHR10504; PTHR10504; 1.
PANTHER; PTHR10504:SF66; PTHR10504:SF66; 1.
Pfam; PF01273; LBP_BPI_CETP; 1.
Pfam; PF02886; LBP_BPI_CETP_C; 1.
PIRSF; PIRSF002417; Lipid_binding_protein; 1.
SMART; SM00328; BPI1; 1.
SMART; SM00329; BPI2; 1.
SUPFAM; SSF55394; SSF55394; 2.
PROSITE; PS00400; LBP_BPI_CETP; 1.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Innate immunity; Lipid transport; Membrane; Polymorphism;
Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 25 {ECO:0000269|PubMed:2402637}.
CHAIN 26 481 Lipopolysaccharide-binding protein.
/FTId=PRO_0000017158.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 159 198 {ECO:0000250|UniProtKB:Q61805}.
VARIANT 9 9 P -> L (in dbSNP:rs2232580).
/FTId=VAR_028243.
VARIANT 111 111 R -> Q (in dbSNP:rs2232583).
/FTId=VAR_049737.
VARIANT 125 125 L -> I (in dbSNP:rs2232585).
/FTId=VAR_028244.
VARIANT 147 147 E -> K (in dbSNP:rs36015492).
/FTId=VAR_049738.
VARIANT 157 157 S -> C (in dbSNP:rs2232586).
/FTId=VAR_061293.
VARIANT 166 166 V -> M (in dbSNP:rs5744204).
/FTId=VAR_028245.
VARIANT 242 242 M -> I (in dbSNP:rs2232601).
/FTId=VAR_028246.
VARIANT 283 283 D -> G (in dbSNP:rs2232607).
/FTId=VAR_028247.
VARIANT 294 294 H -> R (in dbSNP:rs2232608).
/FTId=VAR_028248.
VARIANT 333 333 P -> L (abolishes lipopolysaccharide
binding and causes increased proteolytic
degradation of the protein;
dbSNP:rs2232613).
{ECO:0000269|PubMed:24120359}.
/FTId=VAR_028249.
VARIANT 339 339 L -> F (in dbSNP:rs5744212).
/FTId=VAR_028250.
VARIANT 364 364 I -> T (in dbSNP:rs2232615).
/FTId=VAR_049739.
VARIANT 436 436 F -> L (in dbSNP:rs2232618).
{ECO:0000269|PubMed:2402637,
ECO:0000269|PubMed:9240454,
ECO:0000269|Ref.5}.
/FTId=VAR_028251.
VARIANT 445 445 A -> T (in dbSNP:rs2232619).
/FTId=VAR_028252.
CONFLICT 6 6 R -> H (in Ref. 2). {ECO:0000305}.
CONFLICT 22 22 E -> C (in Ref. 2). {ECO:0000305}.
CONFLICT 82 82 N -> K (in Ref. 4; AAC39547).
{ECO:0000305}.
CONFLICT 128 128 S -> F (in Ref. 4; AAC39547).
{ECO:0000305}.
CONFLICT 154 157 VTAS -> GYCL (in Ref. 1; AAA59493).
{ECO:0000305}.
CONFLICT 174 174 L -> S (in Ref. 1; AAA59493).
{ECO:0000305}.
CONFLICT 257 257 R -> S (in Ref. 4; AAC39547).
{ECO:0000305}.
CONFLICT 266 270 VMSLP -> A (in Ref. 1; AAA59493).
{ECO:0000305}.
CONFLICT 369 369 L -> H (in Ref. 4; AAC39547).
{ECO:0000305}.
SEQUENCE 481 AA; 53384 MW; 5A0E4B9E5E604C72 CRC64;
MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL QSELLRITLP
DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG LSLSISDSSI RVQGRWKVRK
SFFKLQGSFD VSVKGISISV NLLLGSESSG RPTVTASSCS SDIADVEVDM SGDLGWLLNL
FHNQIESKFQ KVLESRICEM IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA
QMLEVMFKGE IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN
FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN FSPGNLSVDP
YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG FLKPGKVKVE LKESKVGLFN
AELLEALLNY YILNTFYPKF NDKLAEGFPL PLLKRVQLYD LGLQIHKDFL FLGANVQYMR
V


Related products :

Catalog number Product name Quantity
20-321-175032 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) - MONOCLONAL ANTIBODY TO MOUSE LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) Monoclonal 0.1 mg
20-321-175033 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) - MONOCLONAL ANTIBODY TO MOUSE LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) Monoclonal 0.1 mg
20-321-175034 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) - MONOCLONAL ANTIBODY TO MOUSE LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) Monoclonal 0.1 mg
20-321-175126 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) - MONOCLONAL ANTIBODY TO HUMAN LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP); LBP Monoclonal 0.1 mg
20-321-175127 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP) - MONOCLONAL ANTIBODY TO HUMAN LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP); LBP Monoclonal 0.1 mg
C370 Lipopolysaccharide-Binding Protein LBP 500
C370 Lipopolysaccharide-Binding Protein LBP lmg
DL-LBP-Ra Rat Lipopolysaccharide Binding Protein (LBP) ELISA Kit 96T
EIAAB44625 CXorf15,ELRG,Environmental lipopolysaccharide-responding gene protein,Factor inhibiting ATF4-mediated transcription,FIAT,Gamma-taxilin,Homo sapiens,Human,Lipopolysaccharide-specific response protein 5
GWB-CFAEB0 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP), Antibody
EH1560 Lipopolysaccharide-binding protein Elisa Kit 96T
C201 Human Lipopolysaccharide-Binding Protein LBP 50
E91406Hu ELISA Kit for Lipopolysaccharide Binding Protein (LBP) 96T/Kit
C116 Human Lipopolysaccharide-Binding Protein LBP l0
201-20-3065 LBP{lipopolysaccharide binding protein}rabbit.pAb 0.2ml
GWB-FAAF48 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP), Antibody
E1381067 Lipopolysaccharide Binding Protein (LBP) ELISA Kit 1
DL-LBP-Hu Human Lipopolysaccharide Binding Protein (LBP) ELISA Kit 96T
E12411266 Rat Lipopolysaccharide Binding Protein(LBP) ELISA Kit 1
LBX1 LBP Gene lipopolysaccharide binding protein
10526-H08H LBP _ Lipopolysaccharide Binding Protein (His Tag) 50
DL-LBP-b Bovine Lipopolysaccharide Binding Protein (LBP) ELISA Kit 96T
E91406Bo ELISA Kit for Lipopolysaccharide Binding Protein (LBP) 96T/Kit
DL-LBP-Mu Mouse Lipopolysaccharide Binding Protein (LBP) ELISA Kit 96T
GWB-C0D8A2 LIPOPOLYSACCHARIDE BINDING PROTEIN (LBP), Antibody


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur