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Set1/Ash2 histone methyltransferase complex subunit ASH2 (Absent, small, or homeotic discs protein 2)

 ASH2_DROME              Reviewed;         556 AA.
Q94545; D3DMU8; Q8IMW1; Q960W8;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 2.
27-SEP-2017, entry version 148.
RecName: Full=Set1/Ash2 histone methyltransferase complex subunit ASH2 {ECO:0000303|PubMed:21694722};
AltName: Full=Absent, small, or homeotic discs protein 2 {ECO:0000312|EMBL:AAO41602.1};
Name=ash2 {ECO:0000312|EMBL:AAC47328.2,
ECO:0000312|FlyBase:FBgn0000139}; ORFNames=CG6677;
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:AAC47328.2}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=8889525;
Adamson A.L., Shearn A.;
"Molecular genetic analysis of Drosophila ash2, a member of the
trithorax group required for imaginal disc pattern formation.";
Genetics 144:621-633(1996).
[2] {ECO:0000312|EMBL:AAO41602.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
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:0000312|EMBL:AAO41602.1}
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:0000305, ECO:0000312|EMBL:AAK93227.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305, ECO:0000312|EMBL:AAR96120.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 217-556 (ISOFORM C).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Booth B., Carlson J., Chavez C., Frise E., George R.,
Pacleb J., Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8555105; DOI=10.1016/0925-4773(95)00430-0;
LaJeunesse D., Shearn A.;
"Trans-regulation of thoracic homeotic selector genes of the
Antennapedia and bithorax complexes by the trithorax group genes:
absent, small, and homeotic discs 1 and 2.";
Mech. Dev. 53:123-139(1995).
[7] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12068954;
Amoros M., Corominas M., Deak P., Serras F.;
"The ash2 gene is involved in Drosophila wing development.";
Int. J. Dev. Biol. 46:321-324(2002).
[8] {ECO:0000305}
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=12626737; DOI=10.1073/pnas.0538075100;
Beltran S., Blanco E., Serras F., Perez-Villamil B., Guigo R.,
Artavanis-Tsakonas S., Corominas M.;
"Transcriptional network controlled by the trithorax-group gene ash2
in Drosophila melanogaster.";
Proc. Natl. Acad. Sci. U.S.A. 100:3293-3298(2003).
[9]
ERRATUM.
Beltran S., Blanco E., Serras F., Perez-Villamil B., Guigo R.,
Artavanis-Tsakonas S., Corominas M.;
Proc. Natl. Acad. Sci. U.S.A. 109:17141-17141(2012).
[10] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15371308; DOI=10.1242/dev.01380;
Angulo M., Corominas M., Serras F.;
"Activation and repression activities of ash2 in Drosophila wing
imaginal discs.";
Development 131:4943-4953(2004).
[11] {ECO:0000305}
FUNCTION, INTERACTION WITH SKTL, AND DISRUPTION PHENOTYPE.
PubMed=15280236; DOI=10.1534/genetics.103.018721;
Cheng M.K., Shearn A.;
"The direct interaction between ASH2, a Drosophila trithorax group
protein, and SKTL, a nuclear phosphatidylinositol 4-phosphate 5-
kinase, implies a role for phosphatidylinositol 4,5-bisphosphate in
maintaining transcriptionally active chromatin.";
Genetics 167:1213-1223(2004).
[12] {ECO:0000305}
FUNCTION, INTERACTION WITH HCF, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=17466076; DOI=10.1186/gb-2007-8-4-r67;
Beltran S., Angulo M., Pignatelli M., Serras F., Corominas M.;
"Functional dissection of the ash2 and ash1 transcriptomes provides
insights into the transcriptional basis of wing phenotypes and reveals
conserved protein interactions.";
Genome Biol. 8:R67.1-R67.15(2007).
[13] {ECO:0000305}
FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=21694722; DOI=10.1038/emboj.2011.194;
Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.;
"Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase
with role in transcription.";
EMBO J. 30:2817-2828(2011).
[14] {ECO:0000305}
FUNCTION, AND IDENTIFICATION IN THE SET1 AND MLL3/4 COMPLEXES.
PubMed=21875999; DOI=10.1128/MCB.06092-11;
Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
Florens L., Eissenberg J.C., Shilatifard A.;
"The COMPASS family of H3K4 methylases in Drosophila.";
Mol. Cell. Biol. 31:4310-4318(2011).
[15] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21310711; DOI=10.1093/nar/gkq1322;
Perez-Lluch S., Blanco E., Carbonell A., Raha D., Snyder M.,
Serras F., Corominas M.;
"Genome-wide chromatin occupancy analysis reveals a role for ASH2 in
transcriptional pausing.";
Nucleic Acids Res. 39:4628-4639(2011).
[16] {ECO:0000305}
FUNCTION, INTERACTION WITH TRR, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=23197473; DOI=10.1091/mbc.E12-04-0267;
Carbonell A., Mazo A., Serras F., Corominas M.;
"Ash2 acts as an ecdysone receptor coactivator by stabilizing the
histone methyltransferase Trr.";
Mol. Biol. Cell 24:361-372(2013).
-!- FUNCTION: Transcriptional regulator. Regulates a number of genes
involved in wing development including activation of net and bs
and repression of rho and kni and controls vein-intervein
patterning during wing development. Required for correct
expression of a number of homeotic genes including Scr in the
first leg imaginal disk and Ubx in the third leg imaginal disk and
haltere disks. Required for stabilization of the histone-lysine N-
methyltransferase trr and for trimethylation of 'Lys-4' of histone
H3. Plays a role in maintenance of transcriptionally active
chromatin through down-regulation of histone H1
hyperphosphorylation. {ECO:0000269|PubMed:12068954,
ECO:0000269|PubMed:12626737, ECO:0000269|PubMed:15280236,
ECO:0000269|PubMed:15371308, ECO:0000269|PubMed:17466076,
ECO:0000269|PubMed:21310711, ECO:0000269|PubMed:21694722,
ECO:0000269|PubMed:21875999, ECO:0000269|PubMed:23197473,
ECO:0000269|PubMed:8555105}.
-!- SUBUNIT: Core component of several methyltransferase-containing
complexes. Component of the SET1 complex, composed at least of the
catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1,
hcf and Dpy-30L1. Component of the MLL3/4 complex composed at
least of the catalytic subunit trr, ash2, Rbbp5, Dpy-30L1, wds,
hcf, ptip, Pa1, Utx, Lpt and Ncoa6. Interacts with hcf, sktl and
trr. {ECO:0000269|PubMed:15280236, ECO:0000269|PubMed:17466076,
ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999,
ECO:0000269|PubMed:23197473}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17466076,
ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473,
ECO:0000269|PubMed:8889525}. Chromosome
{ECO:0000269|PubMed:17466076, ECO:0000269|PubMed:21694722,
ECO:0000269|PubMed:23197473, ECO:0000269|PubMed:8889525}.
Note=Accumulates on salivary gland polytene chromosomes.
{ECO:0000269|PubMed:17466076, ECO:0000269|PubMed:21694722,
ECO:0000269|PubMed:23197473, ECO:0000269|PubMed:8889525}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=C {ECO:0000269|PubMed:12537569};
IsoId=Q94545-1; Sequence=Displayed;
Name=B;
IsoId=Q94545-2; Sequence=VSP_054947, VSP_054948;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: In larvae and pupae, expressed in imaginal
disks, salivary gland and fat body cells. No expression detected
in central nervous system (at protein level).
{ECO:0000269|PubMed:8889525}.
-!- DEVELOPMENTAL STAGE: Expressed in larval and pupal stages (at
protein level). Expression also detected at early embryonic stages
and in adult. {ECO:0000269|PubMed:12626737,
ECO:0000269|PubMed:8889525}.
-!- DISRUPTION PHENOTYPE: Generally pupal-lethal with mutants showing
a wide array of homeotic transformations. Adult escapers are
sterile and show pattern formation abnormalities in legs,
including tissue overgrowth and small supernumerary legs. In
wings, the pattern formation defects observed include duplicated
bristles and sockets, transformation of campaniform sensilla (a
class of sensory organ) to bristles, ectopic campaniform sensilla
and reduction of intervein tissue with increase of longitudinal
veins and cross-vein tissue. Mutant wing imaginal disk shows
ectopic expression of neur, normally expressed in all sensory
organ precursors in the posterior region of the wing disk.
Increased histone H1 hyperphosphorylation in polytene chromosomes.
Reduced trimethylation of histone H3 'Lys-4', reduced levels of
trr protein and severe defects in pupariation and metamorphosis
due to a lack of activation of ecdysone-responsive genes.
{ECO:0000269|PubMed:12068954, ECO:0000269|PubMed:15280236,
ECO:0000269|PubMed:15371308, ECO:0000269|PubMed:17466076,
ECO:0000269|PubMed:21310711, ECO:0000269|PubMed:23197473,
ECO:0000269|PubMed:8555105, ECO:0000269|PubMed:8889525}.
-!- SEQUENCE CAUTION:
Sequence=ADC27634.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; U73809; AAC47328.2; -; mRNA.
EMBL; AE014297; AAN14010.1; -; Genomic_DNA.
EMBL; AE014297; AAO41602.1; -; Genomic_DNA.
EMBL; AY051803; AAK93227.1; -; mRNA.
EMBL; BT011328; AAR96120.1; -; mRNA.
EMBL; BT120264; ADC27634.1; ALT_SEQ; mRNA.
PIR; S72249; S72249.
RefSeq; NP_733024.1; NM_170160.2. [Q94545-2]
RefSeq; NP_788735.1; NM_176558.3. [Q94545-1]
UniGene; Dm.2415; -.
ProteinModelPortal; Q94545; -.
SMR; Q94545; -.
BioGrid; 67862; 30.
IntAct; Q94545; 7.
MINT; MINT-8288314; -.
STRING; 7227.FBpp0084040; -.
PaxDb; Q94545; -.
PRIDE; Q94545; -.
EnsemblMetazoa; FBtr0084659; FBpp0084039; FBgn0000139. [Q94545-2]
EnsemblMetazoa; FBtr0084660; FBpp0084040; FBgn0000139. [Q94545-1]
GeneID; 42936; -.
KEGG; dme:Dmel_CG6677; -.
UCSC; CG6677-RB; d. melanogaster.
UCSC; CG6677-RC; d. melanogaster. [Q94545-1]
CTD; 42936; -.
FlyBase; FBgn0000139; ash2.
eggNOG; KOG2626; Eukaryota.
eggNOG; ENOG410Y5GC; LUCA.
GeneTree; ENSGT00390000010474; -.
KO; K14964; -.
OMA; NYVFVCK; -.
OrthoDB; EOG091G069C; -.
PhylomeDB; Q94545; -.
Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
GenomeRNAi; 42936; -.
PRO; PR:Q94545; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0000139; -.
ExpressionAtlas; Q94545; differential.
Genevisible; Q94545; DM.
GO; GO:0044665; C:MLL1/2 complex; IDA:FlyBase.
GO; GO:0044666; C:MLL3/4 complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0007420; P:brain development; TAS:UniProtKB.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
GO; GO:0007444; P:imaginal disc development; TAS:UniProtKB.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
GO; GO:0002168; P:instar larval development; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0035209; P:pupal development; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00622; SPRY; 1.
SMART; SM00249; PHD; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 2.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
1: Evidence at protein level;
Alternative splicing; Chromosome; Complete proteome;
Developmental protein; DNA-binding; Metal-binding; Nucleus;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 556 Set1/Ash2 histone methyltransferase
complex subunit ASH2.
/FTId=PRO_0000429418.
DOMAIN 288 510 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 34 90 PHD-type. {ECO:0000255}.
VAR_SEQ 1 206 Missing (in isoform B).
{ECO:0000303|Ref.5}.
/FTId=VSP_054947.
VAR_SEQ 207 216 RLTDDGYTQA -> MASSFTDEES (in isoform B).
{ECO:0000303|Ref.5}.
/FTId=VSP_054948.
SEQUENCE 556 AA; 63229 MW; 6F895B62853CD37E CRC64;
MEDSQMDTSS PTESSSEVNF TAEEDKSQET RSAAGVCYCG KERNLNIVEL LCATCSRWVH
ETCVSYQLGK GKLLPFITNY VFVCKNCSAS GLESFRKSQA TISQMCHCAI ANMQQAASRD
GRRQIQFSKD KEIIPYIEQY WEAMTTMPRR LTQSWYSTVQ RSLVKDVQTL FTYEEHAEHG
AMYGLFHQDL RIIKPNYESM SKSGALRLTD DGYTQASLSK NNRQKRKFPG TDSGPTGKKG
RPSSDITANV KLPPHGYPLE HPFNKDGYRY ILAEPDPHAP FRQEFDESSD WAGKPIPGWL
YRILVPHSVL LALHDRAPQL KISEDRLAVT GERGYCMVRA THSVNRGCWY FEVTIEEMPD
GAATRLGWGR EYGNLQAPLG YDKFGYSWRS RKGTKFTESH GKHYSDAYVE GDTLGFLIEL
PEEASLDYLP NTFKDRPLVK FKSHLYYEDK DKITETLKNL HILQGSRIEF FKNGQSQGVA
FEDIYAGSYF PAISIHKSAT VSVNFGPAFK YPEVLVEHKA KGMHDRVEEL ITEQCLADTL
YLTEHDGRLR LDNMGL


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CSB-EL002210MO Mouse Set1_Ash2 histone methyltransferase complex subunit ASH2(ASH2L) ELISA kit SpeciesMouse 96T
ARP34203_T200 Anti-Set1_Ash2 histone methyltransferase complex subunit ASH2 (ASH2L) Species_Reactivity: Human
CSB-PA002210GA01HU Rabbit anti-human ash2 (absent, small, or homeotic)-like (Drosophila) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA002210GA01HU Rabbit anti-human ash2 (absent, small, or homeotic)-like (Drosophila) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul


 

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