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

GM14014p (Spoonbill, isoform A) (Spoonbill, isoform D) (Spoonbill, isoform E)

 Q9W4C4_DROME            Unreviewed;       585 AA.
Q9W4C4; Q961E4;
01-MAY-2000, integrated into UniProtKB/TrEMBL.
01-OCT-2002, sequence version 2.
03-JUL-2019, entry version 158.
SubName: Full=GM14014p {ECO:0000313|EMBL:AAK93065.1};
SubName: Full=Spoonbill, isoform A {ECO:0000313|EMBL:AAF46032.2};
SubName: Full=Spoonbill, isoform D {ECO:0000313|EMBL:AAN09138.1};
SubName: Full=Spoonbill, isoform E {ECO:0000313|EMBL:AFH07246.1};
Name=spoon {ECO:0000313|EMBL:AAF46032.2,
ECO:0000313|FlyBase:FBgn0263987};
Synonyms=AKAP Yu {ECO:0000313|EMBL:AAF46032.2},
BcDNA:GM04319 {ECO:0000313|EMBL:AAF46032.2},
Dmel\CG3249 {ECO:0000313|EMBL:AAF46032.2},
mdi {ECO:0000313|EMBL:AAF46032.2},
PKAAP {ECO:0000313|EMBL:AAF46032.2},
Spoon {ECO:0000313|EMBL:AAF46032.2}, yu {ECO:0000313|EMBL:AAF46032.2,
ECO:0000313|FlyBase:FBgn0263987};
ORFNames=CG3249 {ECO:0000313|EMBL:AAK93065.1,
ECO:0000313|FlyBase:FBgn0263987},
Dmel_CG3249 {ECO:0000313|EMBL:AAF46032.2};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000313|EMBL:AAK93065.1}
NUCLEOTIDE SEQUENCE.
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R.,
Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J.,
Nunoo J., Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K.,
Yu C., Lewis S.E., Rubin G.M., Celniker S.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[4] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002).
[6] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[7] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[8] {ECO:0000313|EMBL:AAF46032.2}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:AAF46032.2}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[11] {ECO:0000313|EMBL:AAF46032.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[12] {ECO:0000313|EMBL:AAF46032.2}
NUCLEOTIDE SEQUENCE.
PubMed=26109357; DOI=.1534/g3.115.018929;
FlyBase Consortium;
Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B.,
St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K.,
Strelets V., Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: Impact of High-
Throughput Data.";
G3 (Bethesda) 5:1721-1736(2015).
[13] {ECO:0000313|EMBL:AAF46032.2}
NUCLEOTIDE SEQUENCE.
PubMed=26109356; DOI=.1534/g3.115.018937;
FlyBase Consortium;
Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B.,
St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B.,
Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: The Rule-
Benders.";
G3 (Bethesda) 5:1737-1749(2015).
[14] {ECO:0000313|EMBL:AAF46032.2}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE014298; AAF46032.2; -; Genomic_DNA.
EMBL; AY051641; AAK93065.1; -; mRNA.
EMBL; AE014298; AAN09138.1; -; Genomic_DNA.
EMBL; AE014298; AFH07246.1; -; Genomic_DNA.
RefSeq; NP_001245532.1; NM_001258603.2.
RefSeq; NP_572221.1; NM_131993.4.
RefSeq; NP_726991.1; NM_167033.3.
EnsemblMetazoa; FBtr0070794; FBpp0070760; FBgn0263987.
EnsemblMetazoa; FBtr0308688; FBpp0300894; FBgn0263987.
EnsemblMetazoa; FBtr0308689; FBpp0300895; FBgn0263987.
GeneID; 31459; -.
KEGG; dme:Dmel_CG3249; -.
UCSC; CG3249-RA; d. melanogaster.
CTD; 31459; -.
FlyBase; FBgn0263987; spoon.
eggNOG; KOG2279; Eukaryota.
eggNOG; ENOG410Z0DP; LUCA.
GeneTree; ENSGT00390000001360; -.
KO; K16518; -.
OMA; NSHNIPE; -.
ChiTaRS; spoon; fly.
GenomeRNAi; 31459; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0263987; Expressed in 43 organ(s), highest expression level in embryo.
GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:FlyBase.
GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0060269; P:centripetally migrating follicle cell migration; IMP:FlyBase.
GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IMP:FlyBase.
GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0008070; P:maternal determination of dorsal/ventral axis, ovarian follicular epithelium, germ-line encoded; IMP:FlyBase.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:FlyBase.
GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:InterPro.
GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
Gene3D; 2.40.50.90; -; 1.
Gene3D; 3.30.1370.10; -; 1.
InterPro; IPR033104; Akap1.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR035437; SNase_OB-fold_sf.
InterPro; IPR002999; Tudor.
PANTHER; PTHR22948:SF48; PTHR22948:SF48; 2.
Pfam; PF00013; KH_1; 1.
Pfam; PF00567; TUDOR; 1.
SMART; SM00322; KH; 1.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF54791; SSF54791; 1.
PROSITE; PS50304; TUDOR; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Membrane {ECO:0000256|SAM:Phobius};
Proteomics identification {ECO:0000213|PeptideAtlas:Q9W4C4};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 444 503 Tudor. {ECO:0000259|PROSITE:PS50304}.
REGION 60 103 Disordered. {ECO:0000256|MobiDB-
lite:Q9W4C4}.
REGION 193 259 Disordered. {ECO:0000256|MobiDB-
lite:Q9W4C4}.
COMPBIAS 60 100 Polar. {ECO:0000256|MobiDB-lite:Q9W4C4}.
COMPBIAS 193 211 Polar. {ECO:0000256|MobiDB-lite:Q9W4C4}.
COMPBIAS 212 249 Polyampholyte. {ECO:0000256|MobiDB-
lite:Q9W4C4}.
SEQUENCE 585 AA; 64907 MW; B377F9A975F9F05A CRC64;
MVSGRPLLYL SLPGVAFILG VFWFRRRYKN CLDKPDDEDS SAINDSSIEP TVQARKANGV
LQNGKLPQQS ASKSMNINGT LVNGSGSGSG SSSDEKDSPT TMLYGKSAPI KIQSNGRTSN
GKHQQQIDSE ILKSKIQDAE HKTLCSIDED FENLSSPRDL PDSVNTRVSF YNRKATQKTV
EPVVIKATRT PKISPENSFL DTNYTNKECE QNNNCEPKEE PSKKEADQEE LEQDQEQTVL
KEEVVDSNGN QKRNVDAASP SLSICSVQSG DSGKGSSLPR SEATRVKTTY EFLFPISLIG
HLYGRKRAFI NQIKAKTLAS VSVGKNPYSG KVRICTIEGT ESEIDAALAM IRQRLPAKRY
PNFTMQRIHF ALPQTIVPLS TESLYNLQLK LIEGINNDVV VSAVLSGSHI FIQHPLHPSH
PSLPLLQKQL YDSYSTMEAP LLPSLELSAV CVIPINDVWY RVQIVDTDPE DEERCVIKFL
DFGGYMNVGF NTLRQIRTDF MNVPFQSTEC ILSNIEPIGG TWSIEAAEIL NKLTKGIVLQ
AQVAGYNSHN LPEIFLFASL GPNNVIFINK ELVGRKLAKW VEMSD


Related products :

Catalog number Product name Quantity
46-229 Prostaglandin E Receptor 3 Antibody. This antibody is expected to recognize isoform 1 (NP_000948.2), isoform 2 (NP_942005.1), isoform 3 (NP_942006.1), isoform 4 (NP_942007.1, NP_942012.1 and NP_942013 0.1 mg
E1250h ELISA kit Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
U1250h CLIA Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
E1250h ELISA Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
45-625 FOXP2 Antibody. This antibody is expected to recognize isoform I (NP_055306.1), isoform II (NP_683696.1) and isoform III (NP_683697.1 and NP_683698.1). 0.1 mg
45-080 LAT Antibody. This antibody is expected to recognize isoform a (NP_055202.1), isoform b (NP_001014987.1 and NP_001014989.1) and isoform c (NP_001014988.1). 0.1 mg
H-9105.0500 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 0.5 mg
H-9105.1000 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 1.0 mg
H-9105.1000 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 1.0 mg
H-9105.0500 pTH_Related Protein Splice Isoform 3 (140_173) (human) Salt Trifluoroacetate Binding _ Synonym Hypercalcemia of Malignancy Factor Splice Isoform 3 (140_173) (human), pTH_rP Splice Isoform 3 (140_17 0.5 mg
45-911 MTMR1 Antibody. Please note this will only recognize Human isoform 1 (NP_003819.1), not isoform 2 (NP_789746). 0.1 mg
EIAAB45911 ATP6N1B,ATP6V0A2,Bos taurus,Bovine,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 kDa subunit a isoform 2
'AP55093SU-N Myoglobin isoform 2 Isoform 2 antibody Ab host: Rabbit 0.2 ml
'AP09453PU-N COX IV isoform 2 (+ Isoform 1) antibody Isotype Host Goat 0.1 mg
26-516 PHF19 contains 2 PHD-type zinc fingers. It acts as a transcritpional repressor. Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter. 0.05 mg
26-517 PHF19 contains 2 PHD-type zinc fingers. It acts as a transcritpional repressor. Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter. 0.05 mg
'AP16992PU-N COX IV isoform 1 (+ isoform 2) antibody Host Goat 0.1 mg
AP16992PU-N COX IV isoform 1 (+ isoform 2) Goat antibody Ab Aff - Purified 0.1 mg
'AP09453PU-N COX IV isoform 2 (+ Isoform 1) antibody Ab host: Goat 0.1 mg
AP09453PU-N COX IV isoform 2 (+ Isoform 1) Goat antibody Ab Aff - Purified 0.1 mg
'AP16992PU-N COX IV isoform 1 (+ isoform 2) antibody Ab host: Goat 0.1 mg
29-369 RBM14 contains 2 RRM (RNA recognition motif) domains. Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, 0.05 mg
EIAAB45905 ATP6V0A1,Chicken,Gallus gallus,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1,V-ATPase 116 kDa isoform a1,V-type proton ATPase 116 kDa subunit a isoform 1
EIAAB38501 Homo sapiens,Human,Signal-regulatory protein beta-1 isoform 3,SIRPB1,SIRP-beta-1 isoform 3
45-064 GIPC1 Antibody. This antibody is expected to recognize both isoform 1 (NP_005707.1, NP_974197.1 and NP_974199.1) and isoform 2 (NP_974196.1, NP_974198.1 and NP_974223.1). 0.1 mg
Pathways :
No related Items

Related Genes :
[PPP2R5E] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon)
[PPP2R5D] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A B subunit isoform B'-delta) (PP2A B subunit isoform B56-delta) (PP2A B subunit isoform PR61-delta) (PP2A B subunit isoform R5-delta)
[] Sarafotoxin [Cleaved into: Sarafotoxin-A, Ser-isoform (SRTX-A) (Sarafotoxin-A) (S6A); Sarafotoxin-C (SRTX-C) (S6C); Sarafotoxin-B (SRTX-B) (S6B); Sarafotoxin-E (SRTX-E) (S6E); Sarafotoxin-A, Thr-isoform]
[RTS1 SCS1 YOR014W OR26.04] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) (Protein SCS1)
[Ppp2r2b] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform BRB) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PPP2R2B] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PPP2R5C KIAA0044] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29)
[CRYBA1 CRYB1] Beta-crystallin A3 [Cleaved into: Beta-crystallin A3, isoform A1, Delta4 form; Beta-crystallin A3, isoform A1, Delta7 form; Beta-crystallin A3, isoform A1, Delta8 form]
[PPP2R2A] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)
[Ppp2r2b] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
[PPP2R5B] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta)
[TCIRG1 ATP6N1C ATP6V0A3] V-type proton ATPase 116 kDa subunit a isoform 3 (V-ATPase 116 kDa isoform a3) (Osteoclastic proton pump 116 kDa subunit) (OC-116 kDa) (OC116) (T-cell immune regulator 1) (T-cell immune response cDNA7 protein) (TIRC7) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 3)
[PPP2R5A] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha)
[PPP2R1B] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta)
[Atp6v0a2 Atp6n1b Tj6] V-type proton ATPase 116 kDa subunit a isoform 2 (V-ATPase 116 kDa isoform a2) (Immune suppressor factor J6B7) (ISF) (Lysosomal H(+)-transporting ATPase V0 subunit a2) (ShIF) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2)
[CACNA1D CACH3 CACN4 CACNL1A2 CCHL1A2] Voltage-dependent L-type calcium channel subunit alpha-1D (Calcium channel, L type, alpha-1 polypeptide, isoform 2) (Voltage-gated calcium channel subunit alpha Cav1.3)
[Cryba1] Beta-crystallin A3 [Cleaved into: Beta-crystallin A3, isoform A1, Delta4 form; Beta-crystallin A3, isoform A1, Delta7 form; Beta-crystallin A3, isoform A1, Delta8 form]
[ATP6V0A1 ATP6N1 ATP6N1A VPP1] V-type proton ATPase 116 kDa subunit a isoform 1 (V-ATPase 116 kDa isoform a1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)
[Cacna1d Cach3 Cacn4 Cacnl1a2 Cchl1a2] Voltage-dependent L-type calcium channel subunit alpha-1D (Calcium channel, L type, alpha-1 polypeptide isoform 2) (Voltage-gated calcium channel subunit alpha Cav1.3)
[Cacna1d Cach3 Cacn4 Cacnl1a2 Cchl1a2] Voltage-dependent L-type calcium channel subunit alpha-1D (Calcium channel, L type, alpha-1 polypeptide, isoform 2) (Rat brain class D) (RBD) (Voltage-gated calcium channel subunit alpha Cav1.3)
[CACNA1E CACH6 CACNL1A6] Voltage-dependent R-type calcium channel subunit alpha-1E (Brain calcium channel II) (BII) (Calcium channel, L type, alpha-1 polypeptide, isoform 6) (Voltage-gated calcium channel subunit alpha Cav2.3)
[Atp6v0a1 Atp6n1] V-type proton ATPase 116 kDa subunit a isoform 1 (V-ATPase 116 kDa isoform a1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)
[Atp6v0a4 Atp6n1b] V-type proton ATPase 116 kDa subunit a isoform 4 (V-ATPase 116 kDa isoform a4) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4) (Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform)
[PPP3CA CALNA CNA] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)
[VPH1 YOR270C] V-type proton ATPase subunit a, vacuolar isoform (V-ATPase a 1 subunit) (V-ATPase 95 kDa subunit) (Vacuolar pH protein 1) (Vacuolar proton pump a subunit) (Vacuolar proton translocating ATPase subunit a 1)
[STV1 YMR054W YM9796.07] V-type proton ATPase subunit a, Golgi isoform (V-ATPase a 2 subunit) (Similar to VPH1 protein 1) (V-ATPase 101 kDa subunit) (V-ATPase subunit AC115) (Vacuolar proton translocating ATPase subunit a 2)
[CPT1A CPT1] Carnitine O-palmitoyltransferase 1, liver isoform (CPT1-L) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, liver isoform) (CPT I) (CPTI-L) (Carnitine palmitoyltransferase 1A)
[PPP3CA] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)
[PPP3CB CALNA2 CALNB CNA2] Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta)
[Cacna1e Cach6 Cacnl1a6 Cchra1] Voltage-dependent R-type calcium channel subunit alpha-1E (Brain calcium channel II) (BII) (Calcium channel, L type, alpha-1 polypeptide, isoform 6) (Voltage-gated calcium channel subunit alpha Cav2.3)

Bibliography :
No related Items