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

Negative regulator of reactive oxygen species (Leucine-rich repeat-containing protein 33)

 LRC33_MOUSE             Reviewed;         693 AA.
Q8BMT4; Q3TIA8; Q8BTT4; Q8BUI7; Q8BY16; Q8R063;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
05-DEC-2018, entry version 145.
RecName: Full=Transforming growth factor beta activator LRRC33 {ECO:0000305};
AltName: Full=Leucine-rich repeat-containing protein 33 {ECO:0000305};
AltName: Full=Negative regulator of reactive oxygen species {ECO:0000303|PubMed:24739962};
Flags: Precursor;
Name=Nrros {ECO:0000303|PubMed:24739962, ECO:0000312|MGI:MGI:2445095};
Synonyms=Lrrc33 {ECO:0000303|PubMed:29909984,
ECO:0000312|MGI:MGI:2445095};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Salivary gland;
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).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24550525; DOI=10.1189/jlb.0813457;
Su X., Mei S., Liang X., Wang S., Liu J., Zhang Y., Bao Y., Chen Y.,
Che Y., Chunhua Zhao R., Zhang Z., Yang R.;
"Epigenetically modulated LRRC33 acts as a negative physiological
regulator for multiple Toll-like receptors.";
J. Leukoc. Biol. 96:17-26(2014).
[4]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH
CYBB, AND DISRUPTION PHENOTYPE.
PubMed=24739962; DOI=10.1038/nature13152;
Noubade R., Wong K., Ota N., Rutz S., Eidenschenk C., Valdez P.A.,
Ding J., Peng I., Sebrell A., Caplazi P., Devoss J., Soriano R.H.,
Sai T., Lu R., Modrusan Z., Hackney J., Ouyang W.;
"NRROS negatively regulates reactive oxygen species during host
defence and autoimmunity.";
Nature 509:235-239(2014).
[5]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=28459434; DOI=10.1038/ni.3743;
Wong K., Noubade R., Manzanillo P., Ota N., Foreman O., Hackney J.A.,
Friedman B.A., Pappu R., Scearce-Levie K., Ouyang W.;
"Mice deficient in NRROS show abnormal microglial development and
neurological disorders.";
Nat. Immunol. 18:633-641(2017).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGFB1, DISRUPTION
PHENOTYPE, TISSUE SPECIFICITY, DISULFIDE BONDS, GLYCOSYLATION, AND
MUTAGENESIS OF CYS-219 AND CYS-363.
PubMed=29909984; DOI=10.1016/j.cell.2018.05.027;
Qin Y., Garrison B.S., Ma W., Wang R., Jiang A., Li J., Mistry M.,
Bronson R.T., Santoro D., Franco C., Robinton D.A., Stevens B.,
Rossi D.J., Lu C., Springer T.A.;
"A milieu molecule for TGF-beta required for microglia function in the
nervous system.";
Cell 174:156-171(2018).
-!- FUNCTION: Key regulator of transforming growth factor beta-1
(TGFB1) specifically required for microglia function in the
nervous system (PubMed:29909984). Required for activation of
latent TGF-beta-1 in macrophages and microglia: associates
specifically via disulfide bonds with the Latency-associated
peptide (LAP), which is the regulatory chain of TGFB1, and
regulates integrin-dependent activation of TGF-beta-1
(PubMed:29909984). TGF-beta-1 activation mediated by LRRC33/NRROS
is highly localized: there is little spreading of TGF-beta-1
activated from one microglial cell to neighboring microglia,
suggesting the existence of localized and selective activation of
TGF-beta-1 by LRRC33/NRROS (PubMed:29909984). Indirectly plays a
role in Toll-like receptor (TLR) signaling: ability to inhibit
TLR-mediated NF-kappa-B activation and cytokine production is
probably a consequence of its role in TGF-beta-1 signaling
(Probable). {ECO:0000269|PubMed:29909984,
ECO:0000305|PubMed:24550525, ECO:0000305|PubMed:29909984}.
-!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with
the Latency-associated peptide chain (LAP) regulatory chain of
TGFB1, leading to regulate activation of TGF-beta-1
(PubMed:29909984). Interacts (via LRR repeats) with TLR2, TLR3,
TLR4, TLR9 and probably other Toll-like receptors (By similarity).
Interacts with CYBB/NOX2; the interaction is direct
(PubMed:24739962). {ECO:0000250|UniProtKB:Q86YC3,
ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:29909984}.
-!- INTERACTION:
Q61093:Cybb; NbExp=4; IntAct=EBI-16102695, EBI-6654585;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24739962,
ECO:0000269|PubMed:29909984}; Single-pass type I membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:24739962}; Single-pass type I membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8BMT4-1; Sequence=Displayed;
Name=2;
IsoId=Q8BMT4-2; Sequence=VSP_016019;
Name=3;
IsoId=Q8BMT4-3; Sequence=VSP_016020;
-!- TISSUE SPECIFICITY: Mainly expressed in cells of hematopoietic
origin, such as in immune organs such as lymph nodes, thymus and
spleen (PubMed:24739962, PubMed:29909984). Among leukocytes,
expressed at higher level in myeloid cell such as macrophages,
neutrophils and dendritic cells (PubMed:24739962). Highly
expressed in central nervous system-resident macrophages,
including microglia and perivascular macrophages (PubMed:28459434,
PubMed:29909984). {ECO:0000269|PubMed:24739962,
ECO:0000269|PubMed:28459434, ECO:0000269|PubMed:29909984}.
-!- INDUCTION: Down-regulated by IFN-gamma (IFNG), LPS or TNF-alpha in
bone marrow-derived macrophages (BMDMs).
{ECO:0000269|PubMed:24739962}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:29909984}.
-!- DISRUPTION PHENOTYPE: Mice develop paraparesis and
neurodegeneration and display reactive microglia caused by defects
in TGF-beta-1 signaling (PubMed:29909984). Mice are viable at six-
weeks of age and immune organs and leukocyte subsets are not
affected (PubMed:24739962). However, significantly increased
reactive oxygen species (ROS) production is observed in primary
bone marrow-derived macrophages (BMDMs) upon zymosan stimulation
(PubMed:24739962). Mice are more susceptible to Toll-like receptor
(TLR) ligand challenges: the macrophages and dendritic cells
produce more proinflammatory cytokines through increased
activation of MAPK and NF-kappa-B (PubMed:24550525). By two months
of age, mice begin to display neurological symptoms including
defects in motor control and strength and die before six months of
age (PubMed:28459434, PubMed:29909984). Mice show microglial
development defects (PubMed:28459434, PubMed:29909984). Mice
develop progressive paraparesis associated with loss of myelin and
axons in the spinal cord and brainstem (PubMed:29909984).
{ECO:0000269|PubMed:24550525, ECO:0000269|PubMed:24739962,
ECO:0000269|PubMed:28459434, ECO:0000269|PubMed:29909984}.
-!- SIMILARITY: Belongs to the LRRC32/LRRC33 family. {ECO:0000305}.
-!- CAUTION: Was initially thought to act as a negative regulator of
reactive oxygen species (ROS) that limits ROS production by
phagocytes during inflammatory response, thereby playing a role
during host defense (PubMed:24739962). However, these results were
based on indirect evidences and could not be confirmed by another
group (PubMed:29909984). It was later shown to act as a key
regulator of transforming growth factor beta-1 (TGFB1)
(PubMed:29909984). {ECO:0000269|PubMed:24739962,
ECO:0000269|PubMed:29909984}.
-!- SEQUENCE CAUTION:
Sequence=AAH27411.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC25907.1; Type=Frameshift; Positions=660; Evidence={ECO:0000305};
Sequence=BAC31275.1; Type=Frameshift; Positions=5; Evidence={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; AK028367; BAC25907.1; ALT_FRAME; mRNA.
EMBL; AK042502; BAC31275.1; ALT_FRAME; mRNA.
EMBL; AK084858; BAC39294.1; -; mRNA.
EMBL; AK088770; BAC40561.1; -; mRNA.
EMBL; AK167934; BAE39938.1; -; mRNA.
EMBL; BC027411; AAH27411.1; ALT_INIT; mRNA.
CCDS; CCDS28115.1; -. [Q8BMT4-1]
CCDS; CCDS84220.1; -. [Q8BMT4-1]
CCDS; CCDS84221.1; -. [Q8BMT4-2]
RefSeq; NP_001334110.1; NM_001347181.1. [Q8BMT4-1]
RefSeq; NP_001334111.1; NM_001347182.1. [Q8BMT4-2]
RefSeq; NP_666181.2; NM_146069.4. [Q8BMT4-1]
RefSeq; XP_006522137.1; XM_006522074.3. [Q8BMT4-1]
RefSeq; XP_006522138.1; XM_006522075.1. [Q8BMT4-1]
RefSeq; XP_006522139.1; XM_006522076.2. [Q8BMT4-1]
RefSeq; XP_006522140.1; XM_006522077.3. [Q8BMT4-1]
RefSeq; XP_017172451.1; XM_017316962.1. [Q8BMT4-1]
UniGene; Mm.33498; -.
ProteinModelPortal; Q8BMT4; -.
DIP; DIP-60840N; -.
IntAct; Q8BMT4; 1.
STRING; 10090.ENSMUSP00000110817; -.
iPTMnet; Q8BMT4; -.
PhosphoSitePlus; Q8BMT4; -.
PaxDb; Q8BMT4; -.
PeptideAtlas; Q8BMT4; -.
PRIDE; Q8BMT4; -.
Ensembl; ENSMUST00000099991; ENSMUSP00000097571; ENSMUSG00000052384. [Q8BMT4-1]
Ensembl; ENSMUST00000115163; ENSMUSP00000110817; ENSMUSG00000052384. [Q8BMT4-3]
Ensembl; ENSMUST00000115165; ENSMUSP00000110819; ENSMUSG00000052384. [Q8BMT4-2]
Ensembl; ENSMUST00000126869; ENSMUSP00000116388; ENSMUSG00000052384. [Q8BMT4-1]
Ensembl; ENSMUST00000143682; ENSMUSP00000119349; ENSMUSG00000052384. [Q8BMT4-1]
GeneID; 224109; -.
KEGG; mmu:224109; -.
UCSC; uc007yyg.1; mouse. [Q8BMT4-1]
UCSC; uc007yyh.1; mouse. [Q8BMT4-3]
UCSC; uc007yyi.1; mouse. [Q8BMT4-2]
CTD; 375387; -.
MGI; MGI:2445095; Nrros.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000157975; -.
HOGENOM; HOG000113368; -.
HOVERGEN; HBG081928; -.
InParanoid; Q8BMT4; -.
OMA; NVLEWFL; -.
OrthoDB; EOG091G03PI; -.
PhylomeDB; Q8BMT4; -.
TreeFam; TF317167; -.
ChiTaRS; Nrros; mouse.
PRO; PR:Q8BMT4; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000052384; Expressed in 121 organ(s), highest expression level in thymus.
CleanEx; MM_LRRC33; -.
ExpressionAtlas; Q8BMT4; baseline and differential.
Genevisible; Q8BMT4; MM.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
GO; GO:0006955; P:immune response; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0014005; P:microglia development; IMP:UniProtKB.
GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; IDA:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; IMP:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0036364; P:transforming growth factor beta1 activation; IDA:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; TAS:UniProtKB.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13855; LRR_8; 2.
SMART; SM00369; LRR_TYP; 11.
PROSITE; PS51450; LRR; 17.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Growth factor binding; Leucine-rich repeat; Membrane;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 693 Transforming growth factor beta activator
LRRC33. {ECO:0000255}.
/FTId=PRO_0000042661.
TOPO_DOM 20 651 Extracellular. {ECO:0000305}.
TRANSMEM 652 672 Helical. {ECO:0000255}.
TOPO_DOM 673 693 Cytoplasmic. {ECO:0000305}.
DOMAIN 29 56 LRRNT. {ECO:0000255}.
REPEAT 58 79 LRR 1. {ECO:0000255}.
REPEAT 82 103 LRR 2. {ECO:0000255}.
REPEAT 106 127 LRR 3. {ECO:0000255}.
REPEAT 133 155 LRR 4. {ECO:0000255}.
REPEAT 158 179 LRR 5. {ECO:0000255}.
REPEAT 182 203 LRR 6. {ECO:0000255}.
REPEAT 206 227 LRR 7. {ECO:0000255}.
REPEAT 228 239 LRR 8. {ECO:0000255}.
REPEAT 251 272 LRR 9. {ECO:0000255}.
REPEAT 273 294 LRR 10. {ECO:0000255}.
REPEAT 329 350 LRR 11. {ECO:0000255}.
REPEAT 353 374 LRR 12. {ECO:0000255}.
REPEAT 377 398 LRR 13. {ECO:0000255}.
REPEAT 403 424 LRR 14. {ECO:0000255}.
REPEAT 427 448 LRR 15. {ECO:0000255}.
REPEAT 463 484 LRR 16. {ECO:0000255}.
REPEAT 486 507 LRR 17. {ECO:0000255}.
REPEAT 512 533 LRR 18. {ECO:0000255}.
REPEAT 537 558 LRR 19. {ECO:0000255}.
REPEAT 559 580 LRR 20. {ECO:0000255}.
REPEAT 585 605 LRR 21. {ECO:0000255}.
DOMAIN 606 644 LRRCT. {ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 500 500 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 219 219 Interchain (with C-? in TGFB1); in linked
form. {ECO:0000269|PubMed:29909984}.
DISULFID 363 363 Interchain (with C-? in TGFB1); in linked
form. {ECO:0000269|PubMed:29909984}.
VAR_SEQ 1 36 MEFPPLWLCLGFHFLIVEWRSGPGTATAASQGGCKV -> M
RPAEPPGPAGA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016019.
VAR_SEQ 1 1 M -> MQEPLETGSIESSGTGNVVVSHQRAVPEM (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016020.
MUTAGEN 219 219 C->A: Abolishes formation of disulfide
bonds and ability to interact with TGFB1;
when associated with A-363.
{ECO:0000269|PubMed:29909984}.
MUTAGEN 363 363 C->A: Abolishes formation of disulfide
bonds and ability to interact with TGFB1;
when associated with A-219.
{ECO:0000269|PubMed:29909984}.
CONFLICT 520 520 D -> E (in Ref. 2; BAC25907).
{ECO:0000305}.
CONFLICT 566 566 R -> H (in Ref. 2; BAC25907).
{ECO:0000305}.
SEQUENCE 693 AA; 77140 MW; 6B4520019DF98BD2 CRC64;
MEFPPLWLCL GFHFLIVEWR SGPGTATAAS QGGCKVVDGV ADCRGLNLAS VPSSLPPHSR
MLILDANPLK DLWNHSLQAY PRLENLSLHS CHLDRISHYA FREQGHLRNL VLADNRLSEN
YKESAAALHT LLGLRRLDLS GNSLTEDMAA LMLQNLSSLE VVSLARNTLM RLDDSIFEGL
EHLVELDLQR NYIFEIEGGA FDGLTELRRL NLAYNNLPCI VDFSLTQLRF LNVSYNILEW
FLAAREEVAF ELEILDLSHN QLLFFPLLPQ CGKLHTLLLQ DNNMGFYREL YNTSSPQEMV
AQFLLVDGNV TNITTVNLWE EFSSSDLSAL RFLDMSQNQF RHLPDGFLKK TPSLSHLNLN
QNCLKMLHIR EHEPPGALTE LDLSHNQLAE LHLAPGLTGS LRNLRVFNLS SNQLLGVPTG
LFDNASSITT IDMSHNQISL CPQMVPVDWE GPPSCVDFRN MGSLRSLSLD GCGLKALQDC
PFQGTSLTHL DLSSNWGVLN GSISPLWAVA PTLQVLSLRD VGLGSGAAEM DFSAFGNLRA
LDLSGNSLTS FPKFKGSLAL RTLDLRRNSL TALPQRVVSE QPLRGLQTIY LSQNPYDCCG
VEGWGALQQH FKTVADLSMV TCNLSSKIVR VVELPEGLPQ GCKWEQVDTG LFYLVLILPS
CLTLLVACTV VFLTFKKPLL QVIKSRCHWS SIY


Related products :

Catalog number Product name Quantity
EIAAB30918 Homo sapiens,Human,KIAA0931,PH domain leucine-rich repeat-containing protein phosphatase 2,PH domain leucine-rich repeat-containing protein phosphatase-like,PHLPP2,PHLPPL,PHLPP-like
CSB-EL018663RA Rat proline_arginine-rich end leucine-rich repeat protein (PRELP) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB43981 Leucine-rich repeat-containing protein KIAA0644 homolog,Rat,Rattus norvegicus,TLR4 interactor with leucine rich repeats,Tril
20-372-60235 F-box and leucine-rich repeat protein 4 (FBXL4) - Mouse monoclonal anti-human FBXL4 antibody; F-box and leucine-rich repeat protein 4; F-box protein FBL4_FBL5 Monoclonal 0.1 mg
EIAAB30919 Mouse,Mus musculus,PH domain leucine-rich repeat-containing protein phosphatase 2,PH domain leucine-rich repeat-containing protein phosphatase-like,Phlpp2,Phlppl,PHLPP-like
EIAAB43980 Homo sapiens,Human,KIAA0644,Leucine-rich repeat-containing protein KIAA0644,TLR4 interactor with leucine rich repeats,TRIL
30-556 LRRC8 is a multi-pass membrane protein. It contains 13 LRR (leucine-rich) repeats. LRRC8 involved in B cell development belongs to a novel family of leucine-rich repeat proteins 0.05 mg
EIAAB43982 Kiaa0644,Leucine-rich repeat-containing protein KIAA0644,Mouse,Mus musculus,TLR4 interactor with leucine rich repeats,Tril
CSB-EL018663HU Human proline_arginine-rich end leucine-rich repeat protein (PRELP) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL018663MO Mouse proline_arginine-rich end leucine-rich repeat protein (PRELP) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL018663BO Bovine proline_arginine-rich end leucine-rich repeat protein (PRELP) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
LF-PA40670 anti-Leucine Rich Repeat Containing 1, Rabbit polyclonal to Leucine Rich Repeat Containing 1, Isotype IgG, Host Rabbit 50 ug
EIAAB14615 Afh,Fbl3a,F-box and leucine-rich repeat protein 3A,F-box_LRR-repeat protein 3,F-box_LRR-repeat protein 3A,Fbxl3,Fbxl3a,Mouse,Mus musculus,Ovtm,Protein after-hours,Protein overtime
PREPL PRELP Gene proline_arginine-rich end leucine-rich repeat protein
EH3648 Proline Arginine Rich End Leucine Rich Repeat Protein Elisa Kit 96T
CSB-EL008472RA Rat F-box and leucine-rich repeat protein 20 (FBXL20) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL008467RA Rat F-box and leucine-rich repeat protein 16 (FBXL16) ELISA kit, Species Rat, Sample Type serum, plasma 96T
Lgr-601AP Leucine Rich repeat containing G-protein Coupled Receptor , Host species: Rabbit, Polyclonal antibody 200ul
CSB-EL008466DO Dog F-box and leucine-rich repeat protein 15 (FBXL15) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL008466RA Rat F-box and leucine-rich repeat protein 15 (FBXL15) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB14616 FBL3A,F-box and leucine-rich repeat protein 3A,F-box_LRR-repeat protein 3,F-box_LRR-repeat protein 3A,FBXL3,FBXL3A,Homo sapiens,Human
E97319Hu ELISA Kit for Proline Arginine Rich End Leucine Rich Repeat Protein (PRELP) 96T/Kit
EIAAB14621 FBL4,FBL5,F-box and leucine-rich repeat protein 5,F-box protein FBL4_FBL5,F-box_LRR-repeat protein 5,FBXL5,FLR1,Homo sapiens,Human,p45SKP2-like protein
QY-E03544 Human Proline Arginine Rich End Leucine Rich Repeat Protein(PRELP)ELISA Kit 96T
201-12-4627 Human Proline Arginine Rich End Leucine Rich Repeat Protein(PRELP)ELISA Kit 96T


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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