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Uveal autoantigen with coiled-coil domains and ankyrin repeats (Nuclear membrane-binding protein) (Nucling)

 UACA_MOUSE              Reviewed;        1411 AA.
Q8CGB3; Q69ZG3; Q7TN77; Q8BJC8;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 2.
16-JAN-2019, entry version 133.
RecName: Full=Uveal autoantigen with coiled-coil domains and ankyrin repeats;
AltName: Full=Nuclear membrane-binding protein;
Short=Nucling;
Name=Uaca; Synonyms=Kiaa1561;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=129;
PubMed=12761289; DOI=10.1093/jb/mvg056;
Sakai T., Liu L., Shishido Y., Fukui K.;
"Identification of a novel, embryonal carcinoma cell-associated
molecule, nucling, that is up-regulated during cardiac muscle
differentiation.";
J. Biochem. 133:429-436(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryonic intestine;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary gland, and 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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-306.
STRAIN=C57BL/6J; TISSUE=Eye;
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).
[5]
FUNCTION, AND INTERACTION WITH APAF1.
PubMed=15271982; DOI=10.1074/jbc.M402902200;
Sakai T., Liu L., Teng X., Mukai-Sakai R., Shimada H., Kaji R.,
Mitani T., Matsumoto M., Toida K., Ishimura K., Shishido Y., Mak T.W.,
Fukui K.;
"Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of
stress-induced apoptosis.";
J. Biol. Chem. 279:41131-41140(2004).
[6]
FUNCTION, INTERACTION WITH LGALS3, AND DISRUPTION PHENOTYPE.
PubMed=14961764; DOI=10.1042/BJ20031300;
Liu L., Sakai T., Sano N., Fukui K.;
"Nucling mediates apoptosis by inhibiting expression of galectin-3
through interference with nuclear factor kappaB signalling.";
Biochem. J. 380:31-41(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND INTERACTION WITH RAB39A.
PubMed=23624502; DOI=10.1016/j.bbrc.2013.04.051;
Mori Y., Matsui T., Omote D., Fukuda M.;
"Small GTPase Rab39A interacts with UACA and regulates the retinoic
acid-induced neurite morphology of Neuro2A cells.";
Biochem. Biophys. Res. Commun. 435:113-119(2013).
-!- FUNCTION: Regulates APAF1 expression and plays an important role
in the regulation of stress-induced apoptosis. Promotes apoptosis
by regulating three pathways, apoptosome up-regulation,
LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation.
Regulates the redistribution of APAF1 into the nucleus after
proapoptotic stress. Down-regulates the expression of LGALS3 by
inhibiting NFKB1. {ECO:0000269|PubMed:14961764,
ECO:0000269|PubMed:15271982}.
-!- FUNCTION: Modulates isoactin dynamics to regulate the
morphological alterations required for cell growth and motility.
Interaction with ARF6 may modulate cell shape and motility after
injury (By similarity). May be involved in multiple neurite
formation (PubMed:23624502). {ECO:0000250|UniProtKB:Q8HYY4,
ECO:0000269|PubMed:23624502}.
-!- SUBUNIT: Component of the apoptosome complex, composed of APAF1,
pro-caspase-9 and UACA. In the complex, it probably interacts
directly with APAF1. Interacts with LGALS3, ARF6 and ACTB.
Interacts with RAB39A. {ECO:0000269|PubMed:14961764,
ECO:0000269|PubMed:15271982, ECO:0000269|PubMed:23624502}.
-!- INTERACTION:
Q8BHD0:Rab39a; NbExp=3; IntAct=EBI-10767725, EBI-10767908;
Q8BHC1:Rab39b; NbExp=4; IntAct=EBI-10767725, EBI-10767682;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12761289}.
Cytoplasm {ECO:0000269|PubMed:12761289}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:12761289}. Note=Expressed diffusely in
cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8CGB3-1; Sequence=Displayed;
Name=2;
IsoId=Q8CGB3-2; Sequence=VSP_017874;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8CGB3-3; Sequence=VSP_017875;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and
testis. Weakly expressed in lung and skeletal muscle. Not
expressed in brain and spleen. {ECO:0000269|PubMed:12761289}.
-!- DEVELOPMENTAL STAGE: First detected at the E9.5 stage in heart at
the edge of both sides of the common ventricular chamber and is
then progressively increased and restricted to the myocardial wall
of left common ventricular chamber of heart.
{ECO:0000269|PubMed:12761289}.
-!- INDUCTION: Up-regulated during cardiomyogenic differentiation. By
apoptotic stress in a dose-dependent manner.
{ECO:0000269|PubMed:12761289}.
-!- DISRUPTION PHENOTYPE: Mice show a high incidence of inflammatory
lesions in preputial glands. Cells around the lesions showed
resistance to apoptosis. {ECO:0000269|PubMed:14961764}.
-!- SEQUENCE CAUTION:
Sequence=BAC78213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD32481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB030647; BAC78213.1; ALT_INIT; mRNA.
EMBL; AK173203; BAD32481.1; ALT_INIT; mRNA.
EMBL; BC042415; AAH42415.1; -; mRNA.
EMBL; AK087466; BAC39886.1; -; mRNA.
CCDS; CCDS23259.1; -. [Q8CGB3-3]
RefSeq; NP_082559.1; NM_028283.2.
RefSeq; XP_017169098.1; XM_017313609.1.
UniGene; Mm.68819; -.
ProteinModelPortal; Q8CGB3; -.
SMR; Q8CGB3; -.
BioGrid; 215442; 4.
IntAct; Q8CGB3; 5.
STRING; 10090.ENSMUSP00000062047; -.
iPTMnet; Q8CGB3; -.
PhosphoSitePlus; Q8CGB3; -.
PaxDb; Q8CGB3; -.
PeptideAtlas; Q8CGB3; -.
PRIDE; Q8CGB3; -.
GeneID; 72565; -.
KEGG; mmu:72565; -.
UCSC; uc009pzi.1; mouse. [Q8CGB3-3]
UCSC; uc009pzk.1; mouse. [Q8CGB3-1]
CTD; 55075; -.
MGI; MGI:1919815; Uaca.
eggNOG; ENOG410IJC6; Eukaryota.
eggNOG; COG0666; LUCA.
HOGENOM; HOG000147885; -.
HOVERGEN; HBG066395; -.
InParanoid; Q8CGB3; -.
OrthoDB; 876605at2759; -.
PhylomeDB; Q8CGB3; -.
TreeFam; TF331274; -.
ChiTaRS; Uaca; mouse.
PRO; PR:Q8CGB3; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0043293; C:apoptosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:MGI.
GO; GO:0009411; P:response to UV; IMP:MGI.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR000727; T_SNARE_dom.
InterPro; IPR030227; UACA.
PANTHER; PTHR24173:SF23; PTHR24173:SF23; 3.
Pfam; PF12796; Ank_2; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1411 Uveal autoantigen with coiled-coil
domains and ankyrin repeats.
/FTId=PRO_0000231651.
REPEAT 69 98 ANK 1.
REPEAT 102 131 ANK 2.
REPEAT 135 164 ANK 3.
REPEAT 168 197 ANK 4.
REPEAT 201 230 ANK 5.
REPEAT 234 263 ANK 6.
COILED 299 379 {ECO:0000255}.
COILED 442 624 {ECO:0000255}.
COILED 652 1380 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9BZF9}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 398 Missing (in isoform 2).
{ECO:0000303|PubMed:15368895}.
/FTId=VSP_017874.
VAR_SEQ 264 264 G -> GGG (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017875.
CONFLICT 144 144 V -> A (in Ref. 3; AAH42415).
{ECO:0000305}.
CONFLICT 353 353 P -> L (in Ref. 3; AAH42415).
{ECO:0000305}.
CONFLICT 757 757 R -> K (in Ref. 3; AAH42415).
{ECO:0000305}.
CONFLICT 778 778 A -> T (in Ref. 3; AAH42415).
{ECO:0000305}.
SEQUENCE 1411 AA; 160813 MW; 0809D2DE9732F879 CRC64;
MKSLKSRLWK QDAPGPTSPS SPTAVASTQS AEWNKYDDRL MKAAERGDVE KVSSILAKKG
VHPGKLDVEG RSAFHVVASK GNLECLNAIL THGIDVATRD SAGRNALHLA AKYGHALCLQ
KLLQYNCPTE HVDLQGRTAL HDAVMADCPS SIQLLCDHGA SVNAKDIDGR TPLVLATQMC
RPTICQLLID RGADVNSRDK QNRTALMLGC EYGCRDAVEV LVKNGADLTL LDALGHDSSY
YARIGDNLDI LNLLKTASEN TNKGRELWRK GPPLQQRNLS HTQDEGSVKS TQREQREPHS
FQDLEIENED LREKLRKIQQ EQRILLDKVN GLQLQLNEEV MVADDLESER EKPKSLLAAK
EKQHEESLRT IEALKNRFKY FESDHPGPGS YPSNRKEDML HKQGQMYTTE PQCASPGIPP
HMHSRSMLRP LELSLPSQTS YSENEILKKE LETLRTYYDS AKQDRLKFQN ELAHKVAECK
ALALECERVK EDSDEQIKQL EDALKDVQKR MYESEGKVKQ MQTHFLALKE HLTNEAATGS
HRIIEELREQ LKDLKGKYEG ASAEVGKLRS QIKQSEMLVG EFKRDEGRLV EENKRLQKEC
GTCEVELERR GRRVVELEGQ LKELGAKLAL SVPTEKFESM KSSLSNDINE KVKRLAEVGR
DYESAQGEIR QLKRDLESVR AQHIRPEEHE QLRSRLEQKS GELGKKVSEL TLKNQTLQKD
VEKLHADNKL LNQQVHSLTV EMKTRYVPLR VSEEMKRSHD VNVEDLNKKL SEATQRYAEK
KQEAERLLAE NDKLTKNVSR LEAVFVAPEK HEKELMGLKS NIAELKKQLS ELNKKCGEGQ
EKIRALMSEN SSLKKTLSSQ YVPAKTHEEV KASLNSTVEK TNRALLEAKK RFDDTSQEVS
KLRDENEVLR RNLENVQNQM KADYVSLEEH SRRMSTVSQS LKEAQEANAA ILADHRQGQE
EIVSLHAEIK AQKKELDTIQ ECIKLKYAPL ARLEECERKF KATEKGLKEQ LSEQTHKCRQ
RDEEVKKGKQ ENERLRADLA ALQKELQDRN ALAEEAREAE RALSGKADEL SKQLKDLSQK
YSDVKSEREK LVEEKAKQAS EILAAQNLLQ KQPVPLEQVE ALKKSLNGTI EQLKEELRSK
QRCLEREQQT VSQLQQLLEN QKNSSVTLAE HLKLKEALEK EVGIMKASLR EKEEESQKKT
KEVSKLQTEV QTTKQALKNL ETREVVDMSK YKATKNDLET QISNLNDKLA SLNRKYDQAC
EEKVSAKDEK ELLHLSIEQE IRDQKERCDK SLTTIMELQQ RIQESAKQIE AKDNKITELL
NDVERLKQAL NGLSQLTYSS GSPTKRQSQL VDTLQQRVRD LQQQLADADR QHQEVIAIYR
THLLSAAQGH MDEDVQAALL QIIQMRQGLV C


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Pathways :
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1665: Limonene and pinene degradation
WP1689: Porphyrin and chlorophyll metabolism
WP1692: Protein export
WP1713: Two-component system
WP1714: Tyrosine metabolism
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1068: Nuclear Receptors
WP1099: Nuclear receptors in lipid metabolism and toxicity
WP1165: G Protein Signaling Pathways
WP1184: Nuclear Receptors
WP1326: Nuclear receptors in lipid metabolism and toxicity
WP1371: G Protein Signaling Pathways
WP1385: Nuclear Receptors
WP139: Nuclear receptors in lipid metabolism and toxicity
WP1438: Influenza A virus infection
WP1488: CFTR activity in the plasma membrane
WP1493: Carbon assimilation C4 pathway
WP1566: Citrate cycle (TCA cycle)

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[CALCOCO2 NDP52] Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)
[Calcoco1 CocoA Kiaa1536] Calcium-binding and coiled-coil domain-containing protein 1 (Coiled-coil coactivator protein)
[CALCOCO1 KIAA1536 PP13275 UNQ2436/PRO4996] Calcium-binding and coiled-coil domain-containing protein 1 (Calphoglin) (Coiled-coil coactivator protein) (Sarcoma antigen NY-SAR-3)
[XRCC6 G22P1] X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)
[MICU1 CALC CBARA1] Calcium uptake protein 1, mitochondrial (Atopy-related autoantigen CALC) (ara CALC) (Calcium-binding atopy-related autoantigen 1) (allergen Hom s 4)
[MORC3 KIAA0136 NXP2 ZCWCC3] MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)
[SHANK3 KIAA1650 PROSAP2 PSAP2] SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2)
[EXOSC9 PMSCL1] Exosome complex component RRP45 (Autoantigen PM/Scl 1) (Exosome component 9) (P75 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 1) (Polymyositis/scleroderma autoantigen 75 kDa) (PM/Scl-75)
[TNRC6A CAGH26 KIAA1460 TNRC6] Trinucleotide repeat-containing gene 6A protein (CAG repeat protein 26) (EMSY interactor protein) (GW182 autoantigen) (Protein GW1) (Glycine-tryptophan protein of 182 kDa)
[GCC2 KIAA0336 RANBP2L4] GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (CLL-associated antigen KW-11) (CTCL tumor antigen se1-1) (Ran-binding protein 2-like 4) (RanBP2L4) (Renal carcinoma antigen NY-REN-53)
[Shank3 Kiaa1650 Prosap2] SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2) (SPANK-2)
[Shank3 Prosap2] SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2) (SPANK-2)
[SP100] Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa) (Fragment)
[TMCC1 KIAA0779] Transmembrane and coiled-coil domains protein 1
[TMCC2 KIAA0481 hucep-11] Transmembrane and coiled-coil domains protein 2 (Cerebral protein 11)
[EXOSC10 PMSCL PMSCL2 RRP6] Exosome component 10 (EC 3.1.13.-) (Autoantigen PM/Scl 2) (P100 polymyositis-scleroderma overlap syndrome-associated autoantigen) (Polymyositis/scleroderma autoantigen 100 kDa) (PM/Scl-100) (Polymyositis/scleroderma autoantigen 2)
[Morc3 Nxp2 Zcwcc3] MORC family CW-type zinc finger protein 3 (Nuclear matrix protein 2) (Zinc finger CW-type coiled-coil domain protein 3)
[SP100] Nuclear autoantigen Sp-100 (Nuclear dot-associated Sp100 protein) (Speckled 100 kDa) (Fragment)
[KANK1 ANKRD15 KANK KIAA0172] KN motif and ankyrin repeat domain-containing protein 1 (Ankyrin repeat domain-containing protein 15) (Kidney ankyrin repeat-containing protein)
[TSPYL2 CDA1 DENTT TSPX HRIHFB2216] Testis-specific Y-encoded-like protein 2 (TSPY-like protein 2) (Cell division autoantigen 1) (Cutaneous T-cell lymphoma-associated antigen se20-4) (CTCL-associated antigen se20-4) (Differentially-expressed nucleolar TGF-beta1 target protein) (Nuclear protein of 79 kDa) (NP79)
[STRN3 GS2NA SG2NA] Striatin-3 (Cell cycle autoantigen SG2NA) (S/G2 antigen)
[NUMA1 NMP22 NUMA] Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)
[ANKRD1 C193 CARP HA1A2] Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Cytokine-inducible gene C-193 protein) (Cytokine-inducible nuclear protein)
[CHCHD6 CHCM1 MIC25] MICOS complex subunit MIC25 (Coiled-coil-helix cristae morphology protein 1) (Coiled-coil-helix-coiled-coil-helix domain-containing protein 6)
[Mrtfa Bsac Mal Mkl1] Myocardin-related transcription factor A (MRTF-A) (Basic SAP coiled-coil transcription activator) (MKL/myocardin-like protein 1) (Megakaryoblastic leukemia 1 protein homolog) (Megakaryocytic acute leukemia protein homolog)
[PABPN1 PAB2 PABP2] Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (Nuclear poly(A)-binding protein 1) (Poly(A)-binding protein II) (PABII) (Polyadenylate-binding nuclear protein 1)
[SYNE1 C6orf98 KIAA0796 KIAA1262 KIAA1756 MYNE1] Nesprin-1 (Enaptin) (KASH domain-containing protein 1) (KASH1) (Myocyte nuclear envelope protein 1) (Myne-1) (Nuclear envelope spectrin repeat protein 1) (Synaptic nuclear envelope protein 1) (Syne-1)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]

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