GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

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

Leucine-rich repeat-containing protein 4 (Brain tumor-associated protein BAG) (Nasopharyngeal carcinoma-associated gene 14 protein) (Netrin-G2 ligand) (NGL-2)

 LRRC4_HUMAN             Reviewed;         653 AA.
Q9HBW1; A4D0Y9; Q14DU9; Q6ZMI8; Q96A85;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
13-FEB-2019, entry version 161.
RecName: Full=Leucine-rich repeat-containing protein 4;
AltName: Full=Brain tumor-associated protein BAG;
AltName: Full=Nasopharyngeal carcinoma-associated gene 14 protein;
AltName: Full=Netrin-G2 ligand;
Short=NGL-2;
Flags: Precursor;
Name=LRRC4; Synonyms=BAG; ORFNames=NAG14, UNQ554/PRO1111;
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 TISSUE SPECIFICITY.
PubMed=15967442; DOI=10.1016/j.febslet.2005.05.058;
Zhang Q., Wang J., Fan S., Wang L., Cao L., Tang K., Peng C., Li Z.,
Li W., Gan K., Liu Z., Li X., Shen S., Li G.;
"Expression and functional characterization of LRRC4, a novel brain-
specific member of the LRR superfamily.";
FEBS Lett. 579:3674-3682(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Wang J.;
Thesis (2000), Zhongshan Medical University / Guangzhou, China.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
STRUCTURE BY NMR OF 351-442.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the Ig-like domain of human leucine-rich
repeat-containing protein 4.";
Submitted (OCT-2006) to the PDB data bank.
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-444 IN COMPLEX WITH NTNG2,
AND DISULFIDE BONDS.
PubMed=21946559; DOI=10.1038/emboj.2011.346;
Seiradake E., Coles C.H., Perestenko P.V., Harlos K., McIlhinney R.A.,
Aricescu A.R., Jones E.Y.;
"Structural basis for cell surface patterning through NetrinG-NGL
interactions.";
EMBO J. 30:4479-4488(2011).
[9]
VARIANT [LARGE SCALE ANALYSIS] ALA-579.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
exitatory synapses through the recruitment of pre-and-postsynaptic
proteins. Organize the lamina/pathway-specific differentiation of
dendrites. Plays a important role for auditory synaptic responses.
Involved in the suppression of glioma (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with DLG4 (By similarity). Interacts (via LRR
repeats) with NTNG2. Forms a complex with DLG4 and with NMDA
receptors. {ECO:0000250, ECO:0000269|PubMed:21946559}.
-!- INTERACTION:
Q9Y2I2:NTNG1; NbExp=2; IntAct=EBI-7444327, EBI-7444396;
Q96CW9:NTNG2; NbExp=4; IntAct=EBI-7444327, EBI-750795;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250}. Note=LRRC4 and DLG4 are interdependent for synaptic
localization. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Specifically expressed in brain.
{ECO:0000269|PubMed:15967442}.
-!- DOMAIN: The last 4 C-terminal residues bind to the first 2 PDZ
domains of DLG4. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF196976; AAG28019.2; -; mRNA.
EMBL; AJ297858; CAC82651.1; -; mRNA.
EMBL; AY358307; AAQ88674.1; -; mRNA.
EMBL; AK172751; BAD18737.1; -; mRNA.
EMBL; AK314047; BAG36756.1; -; mRNA.
EMBL; CH236947; EAL24316.1; -; Genomic_DNA.
EMBL; BC111561; AAI11562.1; -; mRNA.
EMBL; BC111745; AAI11746.1; -; mRNA.
CCDS; CCDS5799.1; -.
RefSeq; NP_071426.1; NM_022143.4.
RefSeq; XP_011514763.1; XM_011516461.2.
RefSeq; XP_016867994.1; XM_017012505.1.
UniGene; Hs.655003; -.
PDB; 2DL9; NMR; -; A=353-442.
PDB; 3ZYI; X-ray; 2.60 A; A=1-444.
PDBsum; 2DL9; -.
PDBsum; 3ZYI; -.
ProteinModelPortal; Q9HBW1; -.
SMR; Q9HBW1; -.
BioGrid; 122061; 13.
IntAct; Q9HBW1; 3.
MINT; Q9HBW1; -.
STRING; 9606.ENSP00000249363; -.
GlyConnect; 1453; -.
iPTMnet; Q9HBW1; -.
PhosphoSitePlus; Q9HBW1; -.
BioMuta; LRRC4; -.
DMDM; 51701696; -.
EPD; Q9HBW1; -.
PaxDb; Q9HBW1; -.
PeptideAtlas; Q9HBW1; -.
PRIDE; Q9HBW1; -.
ProteomicsDB; 81601; -.
Ensembl; ENST00000249363; ENSP00000249363; ENSG00000128594.
GeneID; 64101; -.
KEGG; hsa:64101; -.
UCSC; uc003vmk.4; human.
CTD; 64101; -.
DisGeNET; 64101; -.
EuPathDB; HostDB:ENSG00000128594.7; -.
GeneCards; LRRC4; -.
HGNC; HGNC:15586; LRRC4.
HPA; HPA051100; -.
MIM; 610486; gene.
neXtProt; NX_Q9HBW1; -.
OpenTargets; ENSG00000128594; -.
PharmGKB; PA30463; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000159260; -.
HOGENOM; HOG000252924; -.
HOVERGEN; HBG052359; -.
InParanoid; Q9HBW1; -.
KO; K16351; -.
OMA; SWWLREY; -.
OrthoDB; 282791at2759; -.
PhylomeDB; Q9HBW1; -.
TreeFam; TF324303; -.
EvolutionaryTrace; Q9HBW1; -.
GeneWiki; LRRC4; -.
GenomeRNAi; 64101; -.
PRO; PR:Q9HBW1; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000128594; Expressed in 140 organ(s), highest expression level in cerebellum.
ExpressionAtlas; Q9HBW1; baseline and differential.
Genevisible; Q9HBW1; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0097119; P:postsynaptic density protein 95 clustering; IEA:Ensembl.
GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR026882; Lrrc4.
InterPro; IPR000372; LRRNT.
PANTHER; PTHR24369:SF9; PTHR24369:SF9; 1.
Pfam; PF07679; I-set; 1.
Pfam; PF13855; LRR_8; 3.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51450; LRR; 7.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Leucine-rich repeat; Membrane; Polymorphism;
Postsynaptic cell membrane; Reference proteome; Repeat; Signal;
Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 38 {ECO:0000255}.
CHAIN 39 653 Leucine-rich repeat-containing protein 4.
/FTId=PRO_0000014833.
TOPO_DOM 39 527 Extracellular. {ECO:0000255}.
TRANSMEM 528 548 Helical. {ECO:0000255}.
TOPO_DOM 549 653 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 75 LRRNT.
REPEAT 76 97 LRR 1.
REPEAT 100 121 LRR 2.
REPEAT 124 145 LRR 3.
REPEAT 148 169 LRR 4.
REPEAT 172 194 LRR 5.
REPEAT 197 218 LRR 6.
REPEAT 219 240 LRR 7.
REPEAT 243 264 LRR 8.
REPEAT 267 288 LRR 9.
DOMAIN 300 352 LRRCT.
DOMAIN 353 442 Ig-like.
COMPBIAS 455 526 Thr-rich.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 447 447 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 52 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 50 61 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 304 329 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 306 350 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
DISULFID 374 424 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21946559}.
VARIANT 579 579 T -> A (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035519.
CONFLICT 4 4 L -> S (in Ref. 4; BAD18737).
{ECO:0000305}.
CONFLICT 253 257 QVSLI -> H (in Ref. 2; CAC82651).
{ECO:0000305}.
CONFLICT 300 300 N -> D (in Ref. 4; BAD18737).
{ECO:0000305}.
CONFLICT 315 315 L -> F (in Ref. 4; BAD18737).
{ECO:0000305}.
STRAND 50 52 {ECO:0000244|PDB:3ZYI}.
STRAND 54 56 {ECO:0000244|PDB:3ZYI}.
STRAND 58 60 {ECO:0000244|PDB:3ZYI}.
STRAND 78 81 {ECO:0000244|PDB:3ZYI}.
TURN 92 97 {ECO:0000244|PDB:3ZYI}.
STRAND 103 105 {ECO:0000244|PDB:3ZYI}.
TURN 116 121 {ECO:0000244|PDB:3ZYI}.
STRAND 127 129 {ECO:0000244|PDB:3ZYI}.
TURN 140 142 {ECO:0000244|PDB:3ZYI}.
STRAND 143 145 {ECO:0000244|PDB:3ZYI}.
STRAND 151 153 {ECO:0000244|PDB:3ZYI}.
TURN 164 169 {ECO:0000244|PDB:3ZYI}.
STRAND 175 177 {ECO:0000244|PDB:3ZYI}.
TURN 189 194 {ECO:0000244|PDB:3ZYI}.
STRAND 200 202 {ECO:0000244|PDB:3ZYI}.
STRAND 222 224 {ECO:0000244|PDB:3ZYI}.
STRAND 231 233 {ECO:0000244|PDB:3ZYI}.
HELIX 235 238 {ECO:0000244|PDB:3ZYI}.
STRAND 246 248 {ECO:0000244|PDB:3ZYI}.
TURN 259 264 {ECO:0000244|PDB:3ZYI}.
STRAND 270 272 {ECO:0000244|PDB:3ZYI}.
STRAND 294 296 {ECO:0000244|PDB:3ZYI}.
TURN 306 308 {ECO:0000244|PDB:3ZYI}.
HELIX 309 318 {ECO:0000244|PDB:3ZYI}.
STRAND 328 332 {ECO:0000244|PDB:3ZYI}.
TURN 333 337 {ECO:0000244|PDB:3ZYI}.
HELIX 345 347 {ECO:0000244|PDB:3ZYI}.
STRAND 362 365 {ECO:0000244|PDB:2DL9}.
STRAND 370 372 {ECO:0000244|PDB:2DL9}.
STRAND 380 385 {ECO:0000244|PDB:3ZYI}.
TURN 387 389 {ECO:0000244|PDB:2DL9}.
STRAND 390 393 {ECO:0000244|PDB:2DL9}.
STRAND 399 403 {ECO:0000244|PDB:2DL9}.
STRAND 405 407 {ECO:0000244|PDB:2DL9}.
STRAND 409 413 {ECO:0000244|PDB:2DL9}.
TURN 416 418 {ECO:0000244|PDB:2DL9}.
STRAND 420 427 {ECO:0000244|PDB:3ZYI}.
STRAND 432 440 {ECO:0000244|PDB:3ZYI}.
SEQUENCE 653 AA; 72717 MW; 38159C81F6850E37 CRC64;
MKLLWQVTVH HHTWNAILLP FVYLTAQVWI LCAAIAAAAS AGPQNCPSVC SCSNQFSKVV
CTRRGLSEVP QGIPSNTRYL NLMENNIQMI QADTFRHLHH LEVLQLGRNS IRQIEVGAFN
GLASLNTLEL FDNWLTVIPS GAFEYLSKLR ELWLRNNPIE SIPSYAFNRV PSLMRLDLGE
LKKLEYISEG AFEGLFNLKY LNLGMCNIKD MPNLTPLVGL EELEMSGNHF PEIRPGSFHG
LSSLKKLWVM NSQVSLIERN AFDGLASLVE LNLAHNNLSS LPHDLFTPLR YLVELHLHHN
PWNCDCDILW LAWWLREYIP TNSTCCGRCH APMHMRGRYL VEVDQASFQC SAPFIMDAPR
DLNISEGRMA ELKCRTPPMS SVKWLLPNGT VLSHASRHPR ISVLNDGTLN FSHVLLSDTG
VYTCMVTNVA GNSNASAYLN VSTAELNTSN YSFFTTVTVE TTEISPEDTT RKYKPVPTTS
TGYQPAYTTS TTVLIQTTRV PKQVAVPATD TTDKMQTSLD EVMKTTKIII GCFVAVTLLA
AAMLIVFYKL RKRHQQRSTV TAARTVEIIQ VDEDIPAATS AAATAAPSGV SGEGAVVLPT
IHDHINYNTY KPAHGAHWTE NSLGNSLHPT VTTISEPYII QTHTKDKVQE TQI


Related products :

Catalog number Product name Quantity
EIAAB07019 Brain and nasopharyngeal carcinoma susceptibility protein NSG-x,C7orf54,Homo sapiens,Human,NAG8,Nasopharyngeal carcinoma-associated gene 8 protein,Uncharacterized protein C7orf54
EIAAB27645 Homo sapiens,Human,Nasopharyngeal carcinoma down-regulated gene protein 1,Nasopharyngeal carcinoma-related gene protein,NPCDR1,NPCDRG,NPCR
EIAAB32455 Homo sapiens,Human,Lacrimal proline-rich protein,LPRP,Nasopharyngeal carcinoma-associated proline-rich protein 4,PROL4,Proline-rich protein 4,PRR4
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
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
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
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
EIAAB14613 FBL2,FBL3,F-box and leucine-rich repeat protein 2,F-box protein FBL2_FBL3,F-box_LRR-repeat protein 2,FBXL2,Homo sapiens,Human
EIAAB14617 FBL4,FBL5,F-box and leucine-rich repeat protein 4,F-box protein FBL4_FBL5,F-box_LRR-repeat protein 4,FBXL4,Homo sapiens,Human
EIAAB14626 FBL6,FBL7,F-box and leucine-rich repeat protein 7,F-box protein FBL6_FBL7,F-box_LRR-repeat protein 7,FBXL7,Homo sapiens,Human,KIAA0840
PREPL PRELP Gene proline_arginine-rich end leucine-rich repeat protein
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
LRWD1_MOUSE ELISA Kit FOR Leucine-rich repeat and WD repeat-containing protein 1; organism: Mouse; gene name: LRWD1 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
18-003-43413 JmjC domain-containing histone demethylation protein 1A - EC 1.14.11.27; [Histone-H3]-lysine-36 demethylase 1A; F-box_LRR-repeat protein 11; F-box and leucine-rich repeat protein 11; F-box protein FBL 0.05 mg Aff Pur
EIAAB44217 E2IG4,E2-induced gene 4 protein,Homo sapiens,Human,Leucine-rich repeat-containing protein 54,LRRC54,TSK,TSKU,Tsukushi,Tsukushin,UNQ850_PRO1788
EIAAB43191 C9orf127,Homo sapiens,Human,Nasopharyngeal carcinoma-associated gene 6 protein,NGX6,Protein NAG-5,Protein NGX6,TMEM8B,Transmembrane protein 8B
FBXL19 FBXL17 Gene F-box and leucine-rich repeat protein 17
FBXL22 FBXL20 Gene F-box and leucine-rich repeat protein 20
FBXL8 FBXL6 Gene F-box and leucine-rich repeat protein 6
FBXL16 FBXL14 Gene F-box and leucine-rich repeat protein 14
FBXL15 FBXL13 Gene F-box and leucine-rich repeat protein 13
FBXL18 FBXL16 Gene F-box and leucine-rich repeat protein 16
FBXL2 FBXL18 Gene F-box and leucine-rich repeat protein 18
FBXL20 FBXL19 Gene F-box and leucine-rich repeat protein 19

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[LRRC4C KIAA1580 NGL1 UNQ292/PRO331] Leucine-rich repeat-containing protein 4C (Netrin-G1 ligand) (NGL-1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env gp160] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[STRN3 GS2NA SG2NA] Striatin-3 (Cell cycle autoantigen SG2NA) (S/G2 antigen)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :
?>