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Capping protein, Arp2/3 and myosin-I linker protein 2 (Capping protein regulator and myosin 1 linker 2) (F-actin-uncapping protein RLTPR) (Leucine-rich repeat-containing protein 16C) (RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein)

 CARL2_HUMAN             Reviewed;        1435 AA.
Q6F5E8; B8X2Z3;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
20-JUN-2018, entry version 107.
RecName: Full=Capping protein, Arp2/3 and myosin-I linker protein 2 {ECO:0000303|PubMed:19846667};
AltName: Full=Capping protein regulator and myosin 1 linker 2 {ECO:0000312|HGNC:HGNC:27089};
AltName: Full=F-actin-uncapping protein RLTPR {ECO:0000305};
AltName: Full=Leucine-rich repeat-containing protein 16C;
AltName: Full=RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein {ECO:0000303|PubMed:15588584};
Name=CARMIL2 {ECO:0000312|HGNC:HGNC:27089};
Synonyms=LRRC16C, RLTPR {ECO:0000303|PubMed:15588584};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Keratinocyte;
PubMed=15588584; DOI=10.1016/j.gene.2004.09.004;
Matsuzaka Y., Okamoto K., Mabuchi T., Iizuka M., Ozawa A., Oka A.,
Tamiya G., Kulski J.K., Inoko H.;
"Identification, expression analysis and polymorphism of a novel RLTPR
gene encoding a RGD motif, tropomodulin domain and proline/leucine-
rich regions.";
Gene 343:291-304(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR
LOCATION (ISOFORM 2).
PubMed=19846667; DOI=10.1091/mbc.E08-10-1071;
Liang Y., Niederstrasser H., Edwards M., Jackson C.E., Cooper J.A.;
"Distinct roles for CARMIL isoforms in cell migration.";
Mol. Biol. Cell 20:5290-5305(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-993 AND SER-1246, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
FUNCTION, INTERACTION WITH F-ACTIN-CAPPING PROTEIN (ISOFORM 2),
SUBCELLULAR LOCATION (ISOFORM 2), DOMAIN (ISOFORM 2), AND MUTAGENESIS
OF ARG-1021 AND ARG-1023.
PubMed=26466680; DOI=10.1091/mbc.E15-08-0552;
Lanier M.H., Kim T., Cooper J.A.;
"CARMIL2 is a novel molecular connection between vimentin and actin
essential for cell migration and invadopodia formation.";
Mol. Biol. Cell 26:4577-4588(2015).
[11]
FUNCTION, SUBCELLULAR LOCATION (ISOFORM 2), DOMAIN (ISOFORM 2), AND
MUTAGENESIS OF 1096-LYS--LYS-1106.
PubMed=26578515; DOI=10.1074/jbc.M115.676882;
Lanier M.H., McConnell P., Cooper J.A.;
"Cell migration and invadopodia formation require a membrane-binding
domain of CARMIL2.";
J. Biol. Chem. 291:1076-1091(2016).
-!- FUNCTION: Cell membrane-cytoskeleton-associated protein that plays
a role in the regulation of actin polymerization at the barbed end
of actin filaments. Prevents F-actin heterodimeric capping protein
(CP) activity at the leading edges of migrating cells, and hence
generates uncapped barbed ends and enhances actin polymerization
(PubMed:26466680). Plays a role in cell protrusion formations;
involved in cell polarity, lamellipodial assembly, membrane
ruffling and macropinosome formations (PubMed:19846667,
PubMed:26578515, PubMed:26466680). Involved as well in cell
migration and invadopodia formation during wound healing
(PubMed:19846667, PubMed:26578515, PubMed:26466680).
{ECO:0000269|PubMed:19846667, ECO:0000269|PubMed:26466680,
ECO:0000269|PubMed:26578515}.
-!- SUBUNIT: Isoform 2: Interacts (via C-terminus) with heterodimeric
capping protein (CP); the interaction inhibits CP activity and
hence promotes actin polymerization at the barbed end of actin
filaments (PubMed:26466680). {ECO:0000269|PubMed:26466680}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:19846667, ECO:0000269|PubMed:26466680}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19846667,
ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}. Cell
membrane {ECO:0000269|PubMed:26466680,
ECO:0000269|PubMed:26578515}; Peripheral membrane protein
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection,
lamellipodium {ECO:0000269|PubMed:26578515}. Cell projection,
ruffle {ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}.
Note=Colocalizes to dynamic vimentin filaments both in the central
cytoplasm and at leading edges of migrating cells
(PubMed:26578515, PubMed:26466680, PubMed:19846667). Colocalizes
with F-actin, Arp2/3 complex and cortactin to leading edge
lamellipodia, ruffles and macropinosomes of migrating cells
(PubMed:26578515). {ECO:0000269|PubMed:19846667,
ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=CARMIL2a {ECO:0000303|PubMed:19846667};
IsoId=Q6F5E8-1; Sequence=Displayed;
Name=2; Synonyms=CARMIL2b {ECO:0000303|PubMed:19846667};
IsoId=Q6F5E8-2; Sequence=VSP_047857, VSP_047858;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
thymus, spleen, colon, leukocytes, peripheral blood, skin, skin
keratinocytes and skin fibroblasts. {ECO:0000269|PubMed:15588584}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal skin.
{ECO:0000269|PubMed:15588584}.
-!- DOMAIN: The N-terminal leucine-rich repeat (LRR) domain is
necessary for localization to vimentin filaments
(PubMed:26466680). The C-terminus is necessary for localization to
the cell membrane (PubMed:26578515). {ECO:0000269|PubMed:26466680,
ECO:0000269|PubMed:26578515}.
-!- SIMILARITY: Belongs to the CARMIL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD26751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB113647; BAD26751.1; ALT_INIT; mRNA.
EMBL; FJ026014; ACI49710.1; -; mRNA.
EMBL; AC009095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS45513.1; -. [Q6F5E8-1]
CCDS; CCDS81998.1; -. [Q6F5E8-2]
RefSeq; NP_001013860.1; NM_001013838.1. [Q6F5E8-1]
RefSeq; NP_001303955.1; NM_001317026.1. [Q6F5E8-2]
UniGene; Hs.611432; -.
ProteinModelPortal; Q6F5E8; -.
SMR; Q6F5E8; -.
BioGrid; 126970; 5.
IntAct; Q6F5E8; 3.
MINT; Q6F5E8; -.
STRING; 9606.ENSP00000334958; -.
iPTMnet; Q6F5E8; -.
PhosphoSitePlus; Q6F5E8; -.
BioMuta; RLTPR; -.
DMDM; 172045901; -.
EPD; Q6F5E8; -.
MaxQB; Q6F5E8; -.
PaxDb; Q6F5E8; -.
PeptideAtlas; Q6F5E8; -.
PRIDE; Q6F5E8; -.
ProteomicsDB; 66290; -.
DNASU; 146206; -.
Ensembl; ENST00000334583; ENSP00000334958; ENSG00000159753. [Q6F5E8-1]
Ensembl; ENST00000545661; ENSP00000441481; ENSG00000159753. [Q6F5E8-2]
GeneID; 146206; -.
KEGG; hsa:146206; -.
UCSC; uc002etn.4; human. [Q6F5E8-1]
CTD; 146206; -.
EuPathDB; HostDB:ENSG00000159753.13; -.
GeneCards; CARMIL2; -.
HGNC; HGNC:27089; CARMIL2.
HPA; HPA041402; -.
MIM; 610859; gene.
neXtProt; NX_Q6F5E8; -.
OpenTargets; ENSG00000159753; -.
PharmGKB; PA162401371; -.
eggNOG; KOG4242; Eukaryota.
eggNOG; ENOG410YEE1; LUCA.
GeneTree; ENSGT00390000014487; -.
HOGENOM; HOG000230565; -.
HOVERGEN; HBG108095; -.
InParanoid; Q6F5E8; -.
KO; K20493; -.
OMA; KKVFPRS; -.
OrthoDB; EOG091G01FI; -.
PhylomeDB; Q6F5E8; -.
TreeFam; TF316381; -.
GenomeRNAi; 146206; -.
PRO; PR:Q6F5E8; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000159753; -.
CleanEx; HS_RLTPR; -.
ExpressionAtlas; Q6F5E8; baseline and differential.
Genevisible; Q6F5E8; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; NAS:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0044354; C:macropinosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0051639; P:actin filament network formation; IDA:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IDA:UniProtKB.
GO; GO:0061339; P:establishment or maintenance of monopolar cell polarity; IDA:UniProtKB.
GO; GO:0030011; P:maintenance of cell polarity; IEA:InterPro.
GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IDA:UniProtKB.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:UniProtKB.
GO; GO:1902745; P:positive regulation of lamellipodium organization; IDA:UniProtKB.
GO; GO:1900029; P:positive regulation of ruffle assembly; IDA:UniProtKB.
GO; GO:0044319; P:wound healing, spreading of cells; IDA:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR029763; CARMIL2.
InterPro; IPR031943; CARMIL_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR011993; PH-like_dom_sf.
PANTHER; PTHR24112:SF32; PTHR24112:SF32; 1.
Pfam; PF16000; CARMIL_C; 1.
Pfam; PF13516; LRR_6; 2.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
Membrane; Methylation; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 1435 Capping protein, Arp2/3 and myosin-I
linker protein 2.
/FTId=PRO_0000325817.
REPEAT 64 88 LRR 1.
REPEAT 89 111 LRR 2.
REPEAT 249 272 LRR 3.
REPEAT 274 297 LRR 4.
REPEAT 303 326 LRR 5.
REPEAT 335 362 LRR 6.
REPEAT 393 423 LRR 7.
REPEAT 429 452 LRR 8.
REPEAT 461 481 LRR 9.
REPEAT 492 514 LRR 10.
REPEAT 519 543 LRR 11.
REPEAT 546 572 LRR 12.
REPEAT 581 604 LRR 13.
REPEAT 608 631 LRR 14.
REPEAT 636 660 LRR 15.
REPEAT 664 687 LRR 16.
REGION 573 667 Tropomodulin-like.
REGION 1087 1114 Necessary for localization at the cell
membrane. {ECO:0000269|PubMed:26578515}.
COMPBIAS 905 1046 Pro-rich.
COMPBIAS 1311 1435 Pro-rich.
MOD_RES 991 991 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 993 993 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1120 1120 Phosphoserine.
{ECO:0000250|UniProtKB:Q3V3V9}.
MOD_RES 1246 1246 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1303 1303 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q3V3V9}.
MOD_RES 1315 1315 Phosphoserine.
{ECO:0000250|UniProtKB:Q3V3V9}.
MOD_RES 1420 1420 Phosphoserine.
{ECO:0000250|UniProtKB:Q3V3V9}.
VAR_SEQ 384 419 Missing (in isoform 2).
{ECO:0000303|PubMed:19846667}.
/FTId=VSP_047857.
VAR_SEQ 1346 1372 Missing (in isoform 2).
{ECO:0000303|PubMed:19846667}.
/FTId=VSP_047858.
MUTAGEN 1021 1021 R->A: Loss of ability to bind
heterodimeric capping protein (CP),
unable to inhibit the actin-capping
activity of CP and to rescue the loss of
lamellipodial ruffling, macropinocytosis,
cell polarity, and invadopodia-mediated
matrix degradation; when associated with
A-1023. {ECO:0000269|PubMed:26466680}.
MUTAGEN 1023 1023 R->A: Loss of ability to bind
heterodimeric capping protein (CP),
unable to inhibit the actin-capping
activity of CP and to rescue the loss of
lamellipodial ruffling, macropinocytosis,
cell polarity, and invadopodia-mediated
matrix degradation; when associated with
A-1021. {ECO:0000269|PubMed:26466680}.
MUTAGEN 1096 1106 KKLGTLFAFKK->EEEEEEEEEEE: Loss of
accumulation at the cell membrane. Does
not alter colocalization at vimentin
filaments. Alters monopolar cell
polarity, increasing the number of
leading edges lacking lamellipodia and
ruffles. Inhibits cell migration during
wound healing.
{ECO:0000269|PubMed:26578515}.
MUTAGEN 1096 1106 KKLGTLFAFKK->GGGGGGGGGGG: Loss of
accumulation at the cell membrane. Does
not alter colocalization at vimentin
filaments. Alters monopolar cell
polarity, increasing the number of
leading edges lacking lamellipodia and
ruffles. Inhibits cell migration during
wound healing.
{ECO:0000269|PubMed:26578515}.
MUTAGEN 1096 1106 Missing: Loss of accumulation at the cell
membrane. Does not alter colocalization
at vimentin filaments. Alters monopolar
cell polarity, increasing the number of
leading edges lacking lamellipodia and
ruffles. Inhibits cell migration during
wound healing.
{ECO:0000269|PubMed:26578515}.
SEQUENCE 1435 AA; 154689 MW; B0D452CE375436A5 CRC64;
MAQTPDGISC ELRGEITRFL WPKEVELLLK TWLPGEGAVQ NHVLALLRWR AYLLHTTCLP
LRVDCTFSYL EVQAMALQET PPQVTFELES LRELVLEFPG VAALEQLAQH VAAAIKKVFP
RSTLGKLFRR PTPASMLARL ERSSPSESTD PCSPCGGFLE TYEALCDYNG FPFREEIQWD
VDTIYHRQGC RHFSLGDFSH LGSRDLALSV AALSYNLWFR CLSCVDMKLS LEVSEQILHM
MSQSSHLEEL VLETCSLRGD FVRRLAQALA GHSSSGLREL SLAGNLLDDR GMTALSRHLE
RCPGALRRLS LAQTGLTPRG MRALGRALAT NAAFDSTLTH LDLSGNPGAL GASEDSGGLY
SFLSRPNVLS FLNLAGTDTA LDTVRGCSVG GWMTGRADWR AGRGGLGPPA GVANSLPPQL
FAAVSRGCCT SLTHLDASRN VFSRTKSRAA PAALQLFLSR ARTLRHLGLA GCKLPPDALR
ALLDGLALNT HLRDLHLDLS ACELRSAGAQ VIQDLVCDAG AVSSLDLADN GFGSDMVTLV
LAIGRSRSLR HVALGRNFNV RCKETLDDVL HRIVQLMQDD DCPLQSLSVA ESRLKLGASV
LLRALATNPN LTALDISGNA MGDAGAKLLA KALRVNSRLR SVVWDRNHTS ALGLLDVAQA
LEQNHSLKAM PLPLNDVAQA QRSRPELTAR AVHQIQACLL RNNRADPASS DHTTRLQPLG
LVSDPSEQEV NELCQSVQEH VELLGCGAGP QGEAAVRQAE DAIQNANFSL SILPILYEAG
SSPSHHWQLG QKLEGLLRQV GEVCRQDIQD FTQATLDTAR SLCPQMLQGS SWREQLEGVL
AGSRGLPELL PEQLLQDAFT RLRDMRLSIT GTLAESIVAQ ALAGLSAARD QLVESLAQQA
TVTMPPALPA PDGGEPSLLE PGELEGLFFP EEKEEEKEKD DSPPQKWPEL SHGLHLVPFI
HSAAEEAEPE PELAAPGEDA EPQAGPSARG SPSPAAPGPP AGPLPRMDLP LAGQPLRHPT
RARPRPRRQH HHRPPPGGPQ VPPALPQEGN GLSARVDEGV EEFFSKRLIQ QDRLWAPEED
PATEGGATPV PRTLRKKLGT LFAFKKPRST RGPRTDLETS PGAAPRTRKT TFGDLLRPPT
RPSRGEELGG AEGDTSSPDP AGRSRPRYTR DSKAYSMILL PAEEEATLGA RPDKRRPLER
GETELAPSFE QRVQVMLQRI GVSRGSGGAE GKRKQSKDGE IKKAGSDGDI MDSSTEAPPI
SIKSRTHSVS ADPSCRPGPG SQGPESATWK TLGQQLNAEL RSRGWGQQDG PGPPSPGQSP
SPCRTSPSPD SLGLPEDPCL GPRNEDGQLR PRPLSAGRRA VSVHEDQLQA PAERPLRLQR
SPVLKRRPKL EAPPSPSLGS GLGTEPLPPQ PTEPSSPERS PPSPATDQRG GGPNP


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EIAAB32333 Prelp,Prolargin,Proline-arginine-rich end leucine-rich repeat protein,Rat,Rattus norvegicus
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
SEH319Hu ELISA Kit for Proline Arginine Rich End Leucine Rich Repeat Protein (PRELP) Homo sapiens (Human) 96T
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
EIAAB32334 Homo sapiens,Human,PRELP,Prolargin,Proline-arginine-rich end leucine-rich repeat protein,SLRR2A
E97319Hu ELISA Kit for Proline Arginine Rich End Leucine Rich Repeat Protein (PRELP) Organism: Homo sapiens (Human) 96T
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
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
RLTPR RLTPR Gene RGD motif, leucine rich repeats, tropomodulin domain and proline-rich containing
CSB-EL019752MO Mouse Leucine-rich repeat-containing protein 16C(RLTPR) ELISA kit 96T
CSB-EL019752HU Human Leucine-rich repeat-containing protein 16C(RLTPR) ELISA kit 96T
CSB-EL019752HU Human Leucine-rich repeat-containing protein 16C(RLTPR) ELISA kit SpeciesHuman 96T


 

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