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Protein bowel (Brother of odd with entrails limited)

 BOWEL_DROME             Reviewed;         744 AA.
Q9VQU9; Q24219;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
16-JAN-2019, entry version 143.
RecName: Full=Protein bowel;
AltName: Full=Brother of odd with entrails limited;
Name=bowl {ECO:0000312|FlyBase:FBgn0004893}; ORFNames=CG10021;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB17949.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF THR-261; ASP-279; HIS-284; THR-343; THR-345 AND
LEU-609.
STRAIN=Canton-S {ECO:0000269|PubMed:8670819};
TISSUE=Embryo {ECO:0000269|PubMed:8670819};
PubMed=8670819;
Wang L., Coulter D.E.;
"Bowel, an odd-skipped homolog, functions in the terminal pathway
during Drosophila embryogenesis.";
EMBO J. 15:3182-3196(1996).
[2] {ECO:0000312|EMBL:AAF51065.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
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.A., 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.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., 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.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
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., Woodage T., 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.C., 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).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF51065.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
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., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., 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).
[4] {ECO:0000312|EMBL:AAQ23612.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAQ23612.1}; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:AAB17949.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 233-372, AND TISSUE SPECIFICITY.
STRAIN=Canton-S {ECO:0000269|PubMed:8878683};
TISSUE=Embryo {ECO:0000269|PubMed:8878683};
PubMed=8878683;
Hart M.C., Wang L., Coulter D.E.;
"Comparison of the structure and expression of odd-skipped and two
related genes that encode a new family of zinc finger proteins in
Drosophila.";
Genetics 144:171-182(1996).
[6] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11784087; DOI=10.1006/dbio.2001.0483;
Iwaki D.D., Johansen K.A., Singer J.B., Lengyel J.A.;
"Drumstick, bowl, and lines are required for patterning and cell
rearrangement in the Drosophila embryonic hindgut.";
Dev. Biol. 240:611-626(2001).
[7] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-284.
PubMed=14573519; DOI=10.1242/dev.00833;
de Celis Ibeas J.M., Bray S.J.;
"Bowl is required downstream of Notch for elaboration of distal limb
patterning.";
Development 130:5943-5952(2003).
[8] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14597202; DOI=10.1016/j.ydbio.2003.07.011;
Hao I., Green R.B., Dunaevsky O., Lengyel J.A., Rauskolb C.;
"The odd-skipped family of zinc finger genes promotes Drosophila leg
segmentation.";
Dev. Biol. 263:282-295(2003).
[9] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14568103; DOI=10.1016/j.mod.2003.08.001;
Johansen K.A., Green R.B., Iwaki D.D., Hernandez J.B., Lengyel J.A.;
"The Drm-Bowl-Lin relief-of-repression hierarchy controls fore- and
hindgut patterning and morphogenesis.";
Mech. Dev. 120:1139-1151(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-407, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Putative transcription factor. Required for leg joint
formation, acting downstream of Notch to pattern the leg tarsal
segments. Functions in the terminal pathway during embryogenesis,
acting downstream of tll in the posterior of the embryo. Acts in a
hierarchy downstream of drm and lin during foregut and hindgut
patterning and morphogenesis. Involved in cell rearrangement
during elongation of the embryonic hindgut. Regulates expression
of hindgut patterning genes to establish the small intestine
region of the embryonic hindgut. Required in the foregut for
spatially localized gene expression and morphogenesis of the
proventriculus. {ECO:0000269|PubMed:11784087,
ECO:0000269|PubMed:14568103, ECO:0000269|PubMed:14573519,
ECO:0000269|PubMed:14597202, ECO:0000269|PubMed:8670819}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed at the termini of the blastoderm
embryo in three domains; strongly expressed at the posterior pole,
relatively weakly expressed at the anterior pole and expressed in
a broad transverse stripe just anterior to the presumptive
cephalic furrow. Subsequent to the blastoderm stage, the
expression pattern reflects the morphological rearrangements
associated with gastrulation. Additionally, at early gastrulation,
terminal expression is supplemented by weak expression in seven
stripes. These primary stripes are rapidly supplemented by seven
secondary stripes. Relatively uniformly expressed throughout the
anlagen, primordia and epithelia of the embryonic foregut and
hindgut. By stage 13, hindgut expression is greatly reduced but
foregut expression remains high until stage 17. Segmentally
expressed in the developing leg; present at a subset of segmental
boundaries including all proximal joints (coxa/femur, femur/tibia,
tibia/t1) and the distal t5/pretarsal boundary.
{ECO:0000269|PubMed:11784087, ECO:0000269|PubMed:14568103,
ECO:0000269|PubMed:14573519, ECO:0000269|PubMed:14597202,
ECO:0000269|PubMed:8670819, ECO:0000269|PubMed:8878683}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U58282; AAB17949.1; -; mRNA.
EMBL; AE014134; AAF51065.1; -; Genomic_DNA.
EMBL; BT010294; AAQ23612.1; -; mRNA.
PIR; S70619; S70619.
RefSeq; NP_001245861.1; NM_001258932.2.
RefSeq; NP_001245862.1; NM_001258933.2.
RefSeq; NP_001245863.1; NM_001258934.1.
RefSeq; NP_476883.1; NM_057535.4.
RefSeq; NP_722939.1; NM_164556.2.
RefSeq; NP_722940.1; NM_164557.3.
RefSeq; NP_722941.1; NM_164558.2.
UniGene; Dm.4025; -.
ProteinModelPortal; Q9VQU9; -.
SMR; Q9VQU9; -.
BioGrid; 59806; 13.
ELM; Q9VQU9; -.
IntAct; Q9VQU9; 15.
STRING; 7227.FBpp0297869; -.
iPTMnet; Q9VQU9; -.
PaxDb; Q9VQU9; -.
PRIDE; Q9VQU9; -.
EnsemblMetazoa; FBtr0077490; FBpp0077179; FBgn0004893.
EnsemblMetazoa; FBtr0077491; FBpp0077180; FBgn0004893.
EnsemblMetazoa; FBtr0077492; FBpp0077181; FBgn0004893.
EnsemblMetazoa; FBtr0077493; FBpp0077182; FBgn0004893.
EnsemblMetazoa; FBtr0307027; FBpp0297870; FBgn0004893.
EnsemblMetazoa; FBtr0307028; FBpp0297871; FBgn0004893.
EnsemblMetazoa; FBtr0307029; FBpp0297872; FBgn0004893.
GeneID; 33602; -.
KEGG; dme:Dmel_CG10021; -.
CTD; 33602; -.
FlyBase; FBgn0004893; bowl.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00940000168461; -.
InParanoid; Q9VQU9; -.
KO; K09215; -.
OMA; HREISAF; -.
OrthoDB; 1318335at2759; -.
GenomeRNAi; 33602; -.
PRO; PR:Q9VQU9; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0004893; Expressed in 67 organ(s), highest expression level in wing disc (Drosophila).
ExpressionAtlas; Q9VQU9; baseline and differential.
Genevisible; Q9VQU9; DM.
GO; GO:0005634; C:nucleus; ISS:FlyBase.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:UniProtKB.
GO; GO:0048619; P:embryonic hindgut morphogenesis; IMP:UniProtKB.
GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
GO; GO:0016348; P:imaginal disc-derived leg joint morphogenesis; IMP:FlyBase.
GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0007366; P:periodic partitioning by pair rule gene; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0007362; P:terminal region determination; IMP:UniProtKB.
GO; GO:0035220; P:wing disc development; IMP:FlyBase.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 5.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
1: Evidence at protein level;
Complete proteome; Developmental protein; Metal-binding; Nucleus;
Pair-rule protein; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 744 Protein bowel.
/FTId=PRO_0000046909.
ZN_FING 238 260 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 266 288 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 294 316 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 322 344 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 350 372 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 157 219 Gly/Pro-rich. {ECO:0000255}.
COMPBIAS 547 731 Pro-rich. {ECO:0000255}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 261 261 T->M: In bowl3; embryonic lethal.
{ECO:0000269|PubMed:8670819}.
MUTAGEN 279 279 D->N: In bowl4; embryonic lethal with 50%
larval/pupal escapers.
{ECO:0000269|PubMed:8670819}.
MUTAGEN 284 284 H->Y: In bowl2; embryonic lethal. Legs
containing clones show fusion and
truncation of tarsomeres and disrupted
expression of the leg patterning genes
bab2, dac and B-H1.
{ECO:0000269|PubMed:14573519,
ECO:0000269|PubMed:8670819}.
MUTAGEN 343 343 T->I: In bowl5; embryonic lethal; when
associated with K-345 and P-609.
{ECO:0000269|PubMed:8670819}.
MUTAGEN 345 345 T->K: In bowl5; embryonic lethal; when
associated with I-343 and P-609.
{ECO:0000269|PubMed:8670819}.
MUTAGEN 609 609 L->P: In bowl5; embryonic lethal; when
associated with I-343 and K-345.
{ECO:0000269|PubMed:8670819}.
CONFLICT 196 196 F -> S (in Ref. 1; AAB17949).
{ECO:0000305}.
CONFLICT 634 634 P -> L (in Ref. 1; AAB17949).
{ECO:0000305}.
CONFLICT 720 720 A -> P (in Ref. 1; AAB17949).
{ECO:0000305}.
SEQUENCE 744 AA; 79831 MW; 403653CE7F57672D CRC64;
MPTESSSSEI SGGGGGAIPM LRPSRMDQFM NSMAAAAAAV GGGGLPGAAD RNGGSGGSDG
GSQNGNGDSR NSSASRISAY ETQLAYQQHL AGLHGPPPPP PPSHHREISA FVPVLPTGKV
RPGSNSNYEI IAMMADKRKE LALREAAAAA AMLGRGPGGP GGPGVPPPGV LYGPAGVPPP
PYLTGPGPSP TGAGSFPFPP GAAAAALFPP GLGPGMHAGL DRRLLRAPGR ASRPKKQFIC
KFCNRQFTKS YNLLIHERTH TDERPYSCDI CGKAFRRQDH LRDHRYIHSK EKPFKCTECG
KGFCQSRTLA VHKILHMEES PHKCPVCSRS FNQRSNLKTH LLTHTDHKPY ECSSCGKVFR
RNCDLRRHAL THAVGEVNSG DYVDVGEEDE ARNLSGDEED SLLEVDSPRQ SPVHNLGESG
GSGEKSESER MRLKRKAAID HEESEEEFDD FDEEEELQDL PRVHDLPREE DDDFDPEDEE
QAEVALVARF QASKAAATSQ SSSSVGTKPE RQGVTHCHHE GGETYTMRPH GEKHQEEPGN
SGIASLPVPP SFVRYSVPPG AAGPPPAPPG APPPTHQHPG HPHLLPPNGD PYLPILHVRR
DLHHKSLNLS KAGVPPPPHT PPTIITQPES GKPPNQPLHS PHEAMPSFLG SIPMRKRILP
APTLDLMDPH HHPGLGQRTF VDSPSIYALN MSRHPPRQLL GKPPSTETSG ATTEKGPPVA
APPIAPPPAP PRRTGFSIED IMRR


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Kits Elisa; taq POLYMERASE

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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 :
[NOD2 CARD15 IBD1] Nucleotide-binding oligomerization domain-containing protein 2 (Caspase recruitment domain-containing protein 15) (Inflammatory bowel disease protein 1)
[Osr2] Protein odd-skipped-related 2
[osr1 si:dkey-199e17.1 zgc:101674] Protein odd-skipped-related 1 (zOsr1)
[tenm4 odz4 tnm4] Teneurin-4 (Ten-4) (Protein Odd Oz/ten-m homolog 4) (Tenascin-M4) (Ten-m4) (Teneurin transmembrane protein 4)
[Tenm3 Kiaa1455 Odz3 Tnm3] Teneurin-3 (Ten-3) (Protein Odd Oz/ten-m homolog 3) (Tenascin-M3) (Ten-m3) (Teneurin transmembrane protein 3)
[Tenm1 Odz1 Tnm1] Teneurin-1 (Ten-1) (Protein Odd Oz/ten-m homolog 1) (Tenascin-M1) (Ten-m1) (Teneurin transmembrane protein 1) [Cleaved into: Ten-1 intracellular domain (IDten-1) (Ten-1 ICD); Teneurin C-terminal-associated peptide (TCPA-1) (Ten-1 extracellular domain) (Ten-1 ECD)]
[TENM4 KIAA1302 ODZ4 TNM4] Teneurin-4 (Ten-4) (Protein Odd Oz/ten-m homolog 4) (Tenascin-M4) (Ten-m4) (Teneurin transmembrane protein 4)
[Tenm4 Doc4 Kiaa1302 Odz4 Tnm4] Teneurin-4 (Ten-4) (Downstream of CHOP4) (Protein Odd Oz/ten-m homolog 4) (Tenascin-M4) (Ten-m4) (Teneurin transmembrane protein 4)
[Tmub1 Hops] Transmembrane and ubiquitin-like domain-containing protein 1 (Hepatocyte odd protein shuttling protein) [Cleaved into: iHOPS]
[TENM3 KIAA1455 ODZ3 TNM3] Teneurin-3 (Ten-3) (Protein Odd Oz/ten-m homolog 3) (Tenascin-M3) (Ten-m3) (Teneurin transmembrane protein 3)
[OSR2] Protein odd-skipped-related 2
[TENM1 ODZ1 TNM1] Teneurin-1 (Ten-1) (Protein Odd Oz/ten-m homolog 1) (Tenascin-M1) (Ten-m1) (Teneurin transmembrane protein 1) [Cleaved into: Ten-1 intracellular domain (IDten-1) (Ten-1 ICD); Teneurin C-terminal-associated peptide (TCPA-1) (Ten-1 extracellular domain) (Ten-1 ECD)]
[Tenm2 Odz2 Tnm2] Teneurin-2 (Ten-2) (Neurestin) (Protein Odd Oz/ten-m homolog 2) (Tenascin-M2) (Ten-m2) (Teneurin transmembrane protein 2) [Cleaved into: Ten-2, soluble form; Ten-2 intracellular domain (Ten-2 ICD)]
[Tenm2 Kiaa1127 Odz2 Tnm2] Teneurin-2 (Ten-2) (Protein Odd Oz/ten-m homolog 2) (Tenascin-M2) (Ten-m2) (Teneurin transmembrane protein 2) [Cleaved into: Ten-2, soluble form; Ten-2 intracellular domain (Ten-2 ICD)]
[TENM2 KIAA1127 ODZ2 TNM2] Teneurin-2 (Ten-2) (Protein Odd Oz/ten-m homolog 2) (Tenascin-M2) (Ten-m2) (Teneurin transmembrane protein 2) [Cleaved into: Ten-2, soluble form; Ten-2 intracellular domain (Ten-2 ICD)]
[GRHL2 BOM TFCP2L3] Grainyhead-like protein 2 homolog (Brother of mammalian grainyhead) (Transcription factor CP2-like 3)
[ATG16L1 APG16L UNQ9393/PRO34307] Autophagy-related protein 16-1 (APG16-like 1)
[Grhl2 Bom Tcfcp2l3] Grainyhead-like protein 2 homolog (Brother of mammalian grainyhead) (Transcription factor CP2-like 3)
[INAVA C1orf106] Innate immunity activator protein
[IRGM IFI1 IRGM1 LRG47] Immunity-related GTPase family M protein (EC 3.6.5.-) (Immunity-related GTPase family M protein 1) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47 homolog) (LRG-47)
[Hopx Hod Hop Ob1] Homeodomain-only protein (Homeobox-only protein) (Odd homeobox protein 1) (mOB1)
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[IL10RA IL10R] Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210)
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[OR1D2 OLFR1] Olfactory receptor 1D2 (Olfactory receptor 17-4) (OR17-4) (Olfactory receptor OR17-6) (Olfactory receptor-like protein HGMP07E)
[DHH] Desert hedgehog protein (DHH) (HHG-3) [Cleaved into: Desert hedgehog protein N-product; Desert hedgehog protein C-product]
[HOPX HOD HOP LAGY NECC1 OB1] Homeodomain-only protein (Lung cancer-associated Y protein) (Not expressed in choriocarcinoma protein 1) (Odd homeobox protein 1)
[DUOX2 LNOX2 THOX2] Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase p138-tox) (NADPH oxidase/peroxidase DUOX2) (NADPH thyroid oxidase 2) (Thyroid oxidase 2) (p138 thyroid oxidase)
[IRF5] Interferon regulatory factor 5 (IRF-5)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)

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